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Information on EC 1.3.7.4 - phytochromobilin:ferredoxin oxidoreductase
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1.3.7.4 phytochromobilin:ferredoxin oxidoreductaseIUBMB Comments
Catalyses the two-electron reduction of biliverdin IXalpha. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin.
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Word Map
- 1.3.7.4
-
litoria
-
phytochrome
-
lycoris
-
calpurnia
-
alstroemeria
-
amaryllidaceae
-
matricaria
-
tabebuia
-
phytochrome-deficient
-
phyllostachys
-
venerupis
-
bilins
- galanthamine
-
ethnobotanical
- biotechnology
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
aurea, phytochromobilin synthase, zmhy2, cshy2, pphib synthase, 3z-phytochromobilin:ferredoxin oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HY2
PFB synthase
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-
-
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phytochromobilin synthase
PphiB synthase
HY2
-
-
-
-
phytochromobilin synthase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3Z)-phytochromobilin + oxidized ferredoxin = biliverdin IXalpha + reduced ferredoxin + 2 H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
-
redox reaction
-
-
-
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reduction
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-
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(3Z)-phytochromobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of biliverdin IXalpha. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin.
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CAS REGISTRY NUMBER
COMMENTARY
138263-99-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
-
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
biosynthesis of bilin pigments
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-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
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-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
substrate binding structure analysis, overview
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-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
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-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
conserved surface-charged residues on HY2 and Arabidopsis ferredoxin AtFd2 are important in the protein-protein interaction as well as biliverdin reduction activity of HY2, mutational analysis, overview. The C12 propionate group of biliverdin is important for HY2-catalyzed biliverdin reduction
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-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
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-
-
-
r
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
-
?
additional information
?
-
two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. PPhiB synthase catalyzes the reduction of BV to produce 2(R), 3Z/E-PPhiB using reducing equivalents from ferredoxin. The 2,3,31,32-diene system of the A-ring is site-specifically reduced. The ZZZssa configurations of BV and PPhiB are displayed as observed in the present crystal structure
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-
additional information
?
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two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. PPhiB synthase catalyzes the reduction of BV to produce 2(R), 3Z/E-PPhiB using reducing equivalents from ferredoxin. The 2,3,31,32-diene system of the A-ring is site-specifically reduced. The ZZZssa configurations of BV and PPhiB are displayed as observed in the present crystal structure
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
-
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
biosynthesis of bilin pigments
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
heme might play roles in adventitious roots initiation via long-distance transport from leaves to stems
Ferredoxin
one of the six Arabidopsis ferredoxins, AtFd2, is the preferred electron donor for HY2. Activity with ferredoxin AtFd2 mutants D78N, E81Q, E82Q, Y89F, R92Q, and D112N, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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NADPH regenerating system with glucose-6-phosphate and glucose-6-phosphate dehydrogenase stimulates
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Molecular mechanisms of Lycoris aurea agglutinin-induced apoptosis and G2 /M cell cycle arrest in human lung adenocarcinoma A549 cells, both in vitro and in vivo.
Anthrax
Antioxidant and Antimicrobial Activity of Solvent Fractions of Calpurnia aurea (Ait.) Benth. (Fabaceae).
Bacterial Infections
Antibacterial Activities of Calpurnia aurea against Selected Animal Pathogenic Bacterial Strains.
Candidiasis, Oral
The complete mitogenome of scaly thrush Zoothera aurea (Passeriformes, Turdidae).
Candidiasis, Oral
Urogonimus turdi (Digenea: Leucochloridiidae) from the White's Thrush, Zoothera aurea, in the Republic of Korea.
Carcinoma
Alkaloids from Lycoris aurea and their cytotoxicities against the head and neck squamous cell carcinoma.
Carcinoma, Squamous Cell
Alkaloids from Lycoris aurea and their cytotoxicities against the head and neck squamous cell carcinoma.
Chronic Periodontitis
Evaluation of antibacterial properties of Matricaria aurea on clinical isolates of periodontitis patients with special reference to red complex bacteria.
Dyslipidemias
Evaluation of hypoglycemic, antihyperglycemic and antihyperlipidemic activities of 80% methanolic seed extract of Calpurnia aurea (Ait.) Benth. (Fabaceae) in mice.
Endometrial Neoplasms
Effects of Induced Exosomes from Endometrial Cancer Cells on Tumor Activity in the Presence of Aurea helianthus Extract.
Fibrosarcoma
A Comparative Study upon the Therapeutic Indices of Some Natural and Synthetic Anti-inflammatory Agents.
Hyperalgesia
Tabebuia aurea decreases hyperalgesia and neuronal injury induced by snake venom.
Hypertension
Analyzing factors that influence the folk use and phytonomy of 18 medicinal plants in Navarra.
Hypertension
Antihypertensive activity of 80% methanol seed extract of Calpurnia aurea (Ait.) Benth. subsp. aurea (Fabaceae) is mediated through calcium antagonism induced vasodilation.
Infections
Antimicrobial activities of some selected traditional Ethiopian medicinal plants used in the treatment of skin disorders.
Infections
Hairy roots of Datura candida×D. aurea: effect of culture medium composition on growth and alkaloid biosynthesis.
Infections
Interaction between temperature and sublethal infection with the amphibian chytrid fungus impacts a susceptible frog species.
Infections
Low disease-causing threshold in a frog species susceptible to chytridiomycosis.
Influenza, Human
Antiviral activity of Basidiomycete mycelia against influenza type A (serotype H1N1) and herpes simplex virus type 2 in cell culture.
Neoplasms
Chemical profiling, antiviral and antiproliferative activities of the essential oil of Phlomis aurea Decne grown in Egypt.
Neoplasms
Disseminated neoplasia in clams Venerupis aurea from Galicia (NW Spain): histopathology, ultrastructure and ploidy of the neoplastic cells, and comparison of diagnostic procedures.
Neoplasms
Effects of Induced Exosomes from Endometrial Cancer Cells on Tumor Activity in the Presence of Aurea helianthus Extract.
Neoplasms
Methanolic Extract Isolated from Root of Lycoris aurea Inhibits Cancer Cell Growth and Endothelial Cell Tube Formation In Vitro.
Neoplasms
Phytochemical Screening and In-Vitro Antibacterial and Anticancer Activity of Crude Extract of Matricaria aurea.
Paronychia
Ethnobotanical survey in the Palestinian area: a classification of the healing potential of medicinal plants.
Periodontitis
Evaluation of antibacterial properties of Matricaria aurea on clinical isolates of periodontitis patients with special reference to red complex bacteria.
Skin Diseases
Analyzing factors that influence the folk use and phytonomy of 18 medicinal plants in Navarra.
Squamous Cell Carcinoma of Head and Neck
Alkaloids from Lycoris aurea and their cytotoxicities against the head and neck squamous cell carcinoma.
Tuberculosis
In vitro anti-mycobacterial activity of selected medicinal plants against Mycobacterium tuberculosis and Mycobacterium bovis strains.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
sub-micromolar Km for biliverdin IXa
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
spatiotemporal expression patterns of CsHY2
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the CsHY2 protein sequence contains an N-terminal chloroplast transit peptide (cTP)
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
enzyme phytochromobilin synthase function in the heme pathway in tetrapyrrole metabolism, overview
physiological function
additional information
evolution
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synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, overview
evolution
enzyme structure analysis and comparison, overview. PPhiB synthase is a member of the ferredoxin-dependent bilin reductase (FDBR) family. The FDBR family comprises several different but closely related proteins including phycocyanobilin: ferredoxin oxidoreductase (PcyA, EC 1.3.7.5), 15,16-dihydrobiliverdin:ferredoxin oxidoreductase (PebA, EC 1.3.7.2), phycoerythrobilin:ferredoxin oxidoreductase (PebB, EC 1.3.7.3), phycoerythrobilin synthase (PebS, EC 1.3.7.6), and PPhiB synthase (EC 1.3.7.4). These enzymes are widely distributed in oxygenic phototrophs
evolution
phylogenetic analysis of CsHY2 homologues from different plants
malfunction
a recessive mutant, exhibiting highly enhanced submergence resistance, is identified. Phenotypical analyses show that this resistant to flooding (rf) mutant displays slightly chlorotic leaves and spontaneous initiation of adventitious roots (ARs) on stems. The mutation is mapped to the phytochromobilin synthase gene AUREA (AU), in which a single amino acid substitution from asparagine to tyrosine is found. Temporal coincidence of the two phenotypes is evidenced in the rf mutant: chlorosis and spontaneous AR formation, revealing that AU functions by maintaining heme homeostasis. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The rf mutant is highly resistant to waterlogging in contrast to the wild-type, phenotypes, overview. Active HO-1 is necessary for the scion of rf to stimulate ARs in the stock of wild-type, but there is insufficient HO-1 in the wild-type hypocotyls to initiate AR primordium
malfunction
the long hypocotyl mutant C1238 is identified from an EMS-induced mutagenesis population of the cucumber inbred line CCMC with normal hypocotyl and green leaves. The mutant C1238 exhibits apparently elongated hypocotyl and yellow-green leaves at the seedling stage
physiological function
HY2 synthesizes the open chain tetrapyrrole chromophore for light-sensing phytochromes. It catalyzes the double bond reduction of a heme-derived tetrapyrrole intermediate biliverdin IXalpha at the A-ring diene system
physiological function
-
plants utilize 3Z-phytochromobilin:ferredoxin oxidoreductase to reduce the diene system of the A ring of biliverdin IXalpha to form PthetaB
physiological function
-
Hy2 mutants display a long hypocotyl in white light. Mutant seedlings grown under continuous far-red light display a typical blind phenotype showing very long hypocotyls and closed cotyledons. When grown in short-day regime, wild-type bolts after having produced about 44 leaves whereas the null mutants flower after 18 to 20 leaves
physiological function
in addition to the classic function of the enzyme phytochromobilin synthase (gene AUREA, AU), in phytochrome and chlorophyll biogenesis in leaves, a role in mediating adventitious roots (AR) formation on stems is uncovered. Genetic evidence for the involvement of the AU-heme oxygenase-1-heme pathway in AR initiation is found in tomato. Dual roles of phytochromobilin synthase in chlorophyll synthesis and AR primordia initiation, overview. Communication between leaves and hypocotyls is responsible for AR initiation
physiological function
PPhiB synthase is a ferredoxin-dependent bilin reductase (FDBR) that catalyzes the site-specific reduction of bilins, which are sensory and photosynthesis pigments, and produces phytochromobilin (PPhiB) from biliverdin, a heme-derived linear tetrapyrrole pigment. Phytochromobilin is a red/far-red light sensory pigment in plant phytochrome
physiological function
the CsHY2 protein plays a role in the chloroplast, which is consistent with the plastid localization of PPhiB synthesis and the RNA-seq data, suggesting that tetrapyrrole chromophore biosynthesis and chlorophyll metabolism are mainly in the chloroplast in Cucumis sativus
additional information
the overall structure of tomato PPhiB synthase is similar to those of other ferredoxin-dependent bilin reductases (FDBRs), except for the addition of a long C-terminal loop and short helices. The C-terminal loop is part of the biliverdin-binding pocket and that two basic residues in the C-terminal loop form salt bridges with the propionate groups of biliverdin. The C-terminal loop is involved in the interaction with ferredoxin and biliverdin. The configuration of biliverdin bound to tomato PPhiB synthase differed from that of biliverdin ound to other FDBRs, and its orientation in PPhiB synthase is inverted relative to its orientation in the other FDBRs. Enzyme structure analysis and comparison, overview. Two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. Product release mechanism: PPhiB synthase-catalyzed stereospecific reduction produces 2(R)-PPhiB, which when bound to PPhiB synthase collides with the side chain of Val-121, releasing 2(R)-PPhiB from the synthase
additional information
-
the overall structure of tomato PPhiB synthase is similar to those of other ferredoxin-dependent bilin reductases (FDBRs), except for the addition of a long C-terminal loop and short helices. The C-terminal loop is part of the biliverdin-binding pocket and that two basic residues in the C-terminal loop form salt bridges with the propionate groups of biliverdin. The C-terminal loop is involved in the interaction with ferredoxin and biliverdin. The configuration of biliverdin bound to tomato PPhiB synthase differed from that of biliverdin ound to other FDBRs, and its orientation in PPhiB synthase is inverted relative to its orientation in the other FDBRs. Enzyme structure analysis and comparison, overview. Two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. Product release mechanism: PPhiB synthase-catalyzed stereospecific reduction produces 2(R)-PPhiB, which when bound to PPhiB synthase collides with the side chain of Val-121, releasing 2(R)-PPhiB from the synthase
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PFBS_ARATH
329
0
38130
Swiss-Prot
Chloroplast (Reliability: 2)
A0A7C9CVJ7_OPUST
325
0
37618
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6QF80_ROSCH
336
0
38807
TrEMBL
Chloroplast (Reliability: 2)
A0A7C9CWU5_OPUST
329
0
38060
TrEMBL
Mitochondrion (Reliability: 5)
G7KEL5_MEDTR
329
0
37282
TrEMBL
Chloroplast (Reliability: 1)
A0A7C8YVD8_OPUST
195
0
22444
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B2QW10_GLYSO
273
1
31935
TrEMBL
Secretory Pathway (Reliability: 4)
Q588D6_SOLLC
342
0
39405
TrEMBL
Chloroplast (Reliability: 2)
A0A2G9G9M1_9LAMI
343
0
39524
TrEMBL
Chloroplast (Reliability: 2)
A0A7C9CVP1_OPUST
141
0
15974
TrEMBL
Mitochondrion (Reliability: 5)
A0A7C8YV50_OPUST
218
0
25116
TrEMBL
Mitochondrion (Reliability: 5)
B9RSJ6_RICCO
330
0
38083
TrEMBL
Chloroplast (Reliability: 4)
A0A0B2SFY0_GLYSO
334
0
38524
TrEMBL
Chloroplast (Reliability: 4)
A0A2I0BGT6_9ASPA
302
0
34728
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0B2PZ30_GLYSO
140
0
16556
TrEMBL
Secretory Pathway (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38100
calculated from amino acid sequence, precursor protein with putative N-terminal plastid transit peptide
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and selenomethionine-labeled phytochromobilin synthase in complex with substrate biliverdin IXalpha, sitting drop vapor diffusion method, mixing of protein in 150 mM KCl, and 20 mM Tris-HCl, pH 7.4, with reservoir solution, at 4°C. Tiny needle-shaped crystals of the BV-PPhiB synthase complex are obtained with a reservoir solution containing 20% w/v PEG 8000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M MgCl2. Isomorphous crystals are also obtained with a reservoir solution containing 30% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M MgCl2, X-ray diffraction structure determination and analysis at 1.95-2.2 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D116N
-
mutant still retains the ability of substrate binding, but with only 1.5% relative activity of wild type protein
D146N
-
mutant completely loses catalytic activity and also the ability of biliverdin binding
E110Q
site-directed mutagenesis, the mutant shows 321.7% of wild-type activity
E187Q
site-directed mutagenesis, the mutant shows 20.3% of wild-type activity
H259Q
site-directed mutagenesis, the mutant shows 123.4% of wild-type activity
K183Q
site-directed mutagenesis, the mutant shows 24.6% of wild-type activity
K255Q
site-directed mutagenesis, the mutant shows 11.7% of wild-type activity
K263Q
site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
R200Q
site-directed mutagenesis, the mutant shows 12.5% of wild-type activity
R200Q/R264Q
site-directed mutagenesis, the mutant shows 11.9% of wild-type activity
R252Q
-
mutant loses catalytic activity and the ability of substrate binding
R264Q
site-directed mutagenesis, the mutant shows 18.9% of wild-type activity
D123N
site-directed mutagenesis, the mutated enzyme retains biliverdin IXalpha binding activity and radical formation activity, whereas the PPhiB formation activity is negligible
D263N
site-directed mutagenesis, the mutated enzyme retains biliverdin IXalpha binding activity and radical formation activity, whereas the PPhiB formation activity is negligible
V121A
site-directed mutagenesis, single-turnover analysis demonstrates that the V121A mutated protein is slightly slower, although it produces 3Z/E-PPhiB on wild-type level, whereas no activity is detected in the V121A mutated protein in the steady-state analysis
additional information
additional information
identification of elongated hypocotyl-1 (elh1) mutant C1238, comparison of mutant seedlings with wild-type CCMC seedlings, phenotype, overview. Analysis of the effect of CsHY2 mutation on the function of phys, the expression dynamics of cucumber PHYs genes (CsPHYA1, CsPHYA2, CsPHYB, CsPHYC, and CsPHYE). The 35S:CsHY2-EGFP plasmid construct is transformed into Agrobacterium tumefaciens strain GV3101. Arabidopsis hy2-1 recessive homozygous mutants are transformed and the phenotype is analyzed. The expression level of CsHY2 in mutant is the highest in male and female flowers, followed in order by stem, true leaves, root, cotyledon, and fruit. There is no significant difference in CsHY2 expression in all these organs except cotyledons, true leaves, and stem between wild-type and mutant elh1
additional information
-
identification of elongated hypocotyl-1 (elh1) mutant C1238, comparison of mutant seedlings with wild-type CCMC seedlings, phenotype, overview. Analysis of the effect of CsHY2 mutation on the function of phys, the expression dynamics of cucumber PHYs genes (CsPHYA1, CsPHYA2, CsPHYB, CsPHYC, and CsPHYE). The 35S:CsHY2-EGFP plasmid construct is transformed into Agrobacterium tumefaciens strain GV3101. Arabidopsis hy2-1 recessive homozygous mutants are transformed and the phenotype is analyzed. The expression level of CsHY2 in mutant is the highest in male and female flowers, followed in order by stem, true leaves, root, cotyledon, and fruit. There is no significant difference in CsHY2 expression in all these organs except cotyledons, true leaves, and stem between wild-type and mutant elh1
additional information
the flooding (rf) mutation is analysed in the tomato gene AUREA (AU), it not only led to leaf chlorosis but also causes the spontaneous formation of adventitious roots (ARs) on stems. Under flooding stress, au mutants extensively form ARs along the stem, while wild-type plants produce ARs only at the root-shoot junction. After submergence for 7 days, the resistant to flooding (rf) mutants show higher sensitivity to flooding regarding AR initiation compared to wild-type. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The flooding resistance of rf mutants mainly results from the accumulation of heme and enhanced HO-1 activity, both of which function in the phytochrome synthesis pathway. In addition, the exchange of substances, including heme, between leaves and stems accounts for AR formation on stems
additional information
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the flooding (rf) mutation is analysed in the tomato gene AUREA (AU), it not only led to leaf chlorosis but also causes the spontaneous formation of adventitious roots (ARs) on stems. Under flooding stress, au mutants extensively form ARs along the stem, while wild-type plants produce ARs only at the root-shoot junction. After submergence for 7 days, the resistant to flooding (rf) mutants show higher sensitivity to flooding regarding AR initiation compared to wild-type. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The flooding resistance of rf mutants mainly results from the accumulation of heme and enhanced HO-1 activity, both of which function in the phytochrome synthesis pathway. In addition, the exchange of substances, including heme, between leaves and stems accounts for AR formation on stems
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration. The PPhiB synthase monomer is contained in the major peak of anion-exchange chromatography, and the PPhiB synthase homodimer in the minor peak, for purification, the monomeric major peak fraction is used
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
development of a system to produce phytochromobilin in Escherichia coli by coexpression of heme oxygenase and phytochromobilin:ferredoxin oxidoreductase in a single operon in conjunction with apophytochrome using two compatible plasmids
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gene AUREA (AU), quantitative real-time RT-PCR enzyme expression analysis in wild-type and mutant seedlings