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Information on EC 1.8.3.1 - sulfite oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9S850
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1.8.3.1 sulfite oxidaseIUBMB Comments
A molybdohemoprotein.
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Word Map
- 1.8.3.1
- molybdenum
- sulfur
- xanthine
- heme
- thiosulfate
- moco
- epr
- seizures
- molybdopterin
-
molybdoenzymes
-
sulfur-containing
- tungsten
-
molybdenum-containing
- pterin
- s-sulfocysteine
- soxs
- sulfurtransferase
-
ectopia
-
low-ph
-
pyranopterins
- lentis
-
dithiolene
-
amidoxime
-
eseem
-
hyperfine
- food industry
- agriculture
-
high-ph
- analysis
-
oxidase-deficient
- medicine
-
xanthinuria
-
marc
- molecular biology
- encephalomalacia
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
sulfite oxidase, shopper, atsox, sulfite:acceptor oxidoreductase, at-so, yedyz, sulfite oxidase homologue, sulfite acceptor oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
oxidase, sulfite
-
-
-
-
sulphite oxidase cytochrome b9
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
additional information
-
the enzyme also functions as a selenite oxidase
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
sulfite:oxygen oxidoreductase
A molybdohemoprotein.
CAS REGISTRY NUMBER
COMMENTARY
9029-38-3
-
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
selenite + ferricyanide + H2O
? + ferrocyanide
-
approximately 5% of the observed sulfite activity
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
significantly slower activity than that observed with ferricyanide
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
additional information
?
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
?
additional information
?
-
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
?
additional information
?
-
sulfite ligand docking study, arginine residues particularly Arg374 is crucial for SOX-sulfite binding and two other residues Arg51 and Arg103 are also implicated to be important for SOX-sulfite bindings in plants
-
-
?
additional information
?
-
-
sulfite ligand docking study, arginine residues particularly Arg374 is crucial for SOX-sulfite binding and two other residues Arg51 and Arg103 are also implicated to be important for SOX-sulfite bindings in plants
-
-
?
additional information
?
-
-
No activity is found with cytochrome c as electron acceptor, since the heme domain known to mediate electron transfer between the molybdenum cofactor-domain and cytochrome c in rat hepatic SO is missing in the plant enzyme
-
-
?
additional information
?
-
-
the enzyme does not react with cytochrome c
-
-
?
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
additional information
?
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
?
additional information
?
-
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdopterin
SOX enzyme is characterized with both oxidoreductase molybdopterin binding and Moco oxidoreductase dimerization domains
additional information
-
the enzyme is lacking the heme domain that is known from vertebrate sulfite oxidase
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mo
Molybdenum
Mo
-
coordination of sulfate to the Mo(V) center in the blocked form of sulfite oxidase
Molybdenum
Molybdenum
dimeric enzyme contains only a single molybdenum cofactor domain without an additional redox center
Molybdenum
-
molybdenum covalently bound to two sulfur atoms of a unique tricyclic pterin moiety referred to as molybdopterin, essential for dimerization of the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
potassium nitrate
50% inhibition at 1 mM, in Tris/HCl 20 mM, pH 8.5
RNAi
-
abrogates sulfite oxidase expression, whereby accumulating relatively less sulfate after SO2 application and showing enhanced induction of senescence and wounding associated transcripts, leaf necrosis and chlorophyll bleaching
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
SO is constitutively expressed and is not significantly induced by SO2, whereas the SiR transcript involved in sulfur assimilation is highly induced by SO2 in an SO-dependent manner
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
presence of coordinated sulfate in the sulfite reduced low-pH form of the plant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotypes An-1, Cvi, Col-0, C24, Eri, Kas-1, Kond, Kyo-2, Ler and Sha
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
SO shows constitutive expression without any pronounced diurnal rhythm. No difference at the protein level in younger or older rosette or stem leaves
additional information
enzyme expression levels in ecotypes An-1, Cvi, Col-0, C24, Eri, Kas-1, Kond, Kyo-2, Ler and Sha under different conditions, overview
additional information
-
enzyme expression levels in ecotypes An-1, Cvi, Col-0, C24, Eri, Kas-1, Kond, Kyo-2, Ler and Sha under different conditions, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
physiological function
malfunction
physiological function
additional information
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
the enzyme serves as an anti-viral factor through sequestering Turnip crinkle virus coat protein for binding with Argonaute 1 and confers virus resistance
malfunction
-
enzyme absence confers reduced biomass accumulation in Arabidopsis plants exposed to carbon starvation. Enzyme impairment leads to a reduced sulfur reduction pathway under sucrose depletion and reduced biomass accumulation in plants grown on excess carbon supply
malfunction
-
impairment in enzyme activity results in enhanced water consumption
physiological function
-
enzyme-deficient mutants are consistently negatively affected upon SO2 exposure at 600 nl/l for 60 h and show phenotypical symptoms of injury with small necrotic spots on the leaves. The mean g(H2O) is reduced by about 60% over the fumigation period, accompanied by a reduction of net CO2 assimilation and SO2 uptake of about 50 and 35%, respectively. Sulfur metabolism is completely distorted. Whereas sulfate pool is kept constant, thiol-levels strongly increase
physiological function
-
the enzyme plays an important role in sulfite homeostasis and stomatal closure
physiological function
-
the role of the enzyme is not limited to protection against elevated sulfite toxicity but to maintaining optimal carbon and sulfur metabolism in Arabidopsis plants
additional information
three-dimensional modeling and structure-based phylogeny. Analysis of the protein-protein interaction (PPI) network of AtSOX, overview
additional information
-
three-dimensional modeling and structure-based phylogeny. Analysis of the protein-protein interaction (PPI) network of AtSOX, overview
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). SUOX_ARATH
393
0
43329
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43300
45000
45000
-
2 * 45000, the enzyme is inactive as monomer and dimerization depends on the presence of molybdenum
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
2 * 45000, the enzyme is inactive as monomer and dimerization depends on the presence of molybdenum
additional information
additional information
three-dimensional modeling and structure-based phylogeny
additional information
-
three-dimensional modeling and structure-based phylogeny
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose resin column chromatography and Superdex 200 gel filtration
nickelnitrilotriacetic acid superflow matrix followed by anion exchange chromatography on a SourceQ15 column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence analysis and comparison, phylogenetic tree
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abiotic stresses significantly regulates the sulfite scavengers including SOX and the presence of stress-related cis-regulatory motifs in upstream regions of studied SOXs is reasonable
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
plants can utilize sulfite oxidase in a sulfite oxidative pathway to cope with sulfite overflow. Protects plants from toxic doses of SO2 gas
additional information
-
SO may play a role in protecting catalase from sulfite damage. SO may possibly serve as a safety valve to detoxify excess amounts of sulfite and protect the cell from sulfitolysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eilers, T.; Schwarz, G.; Brinkmann, H.; Witt, C.; Richter, T.; Nieder, J.; Koch, B.; Hille, R.; Hansch, R.; Mendel, R.R.
Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase: a new player in plant sulfur metabolism
J. Biol. Chem.
276
46989-46994
2001
Nicotiana tabacum, Arabidopsis thaliana (Q9S850), Arabidopsis thaliana
Nowak, K.; Luniak, N.; Witt, C.; Wustefeld, Y.; Wachter, A.; Mendel, R.R.; Hansch, R.
Peroxisomal localization of sulfite oxidase separates it from chloroplast-based sulfur assimilation
Plant Cell Physiol.
45
1889-1894
2004
Arabidopsis thaliana (Q9S850), Arabidopsis thaliana
Schrader, N.; Fischer, K.; Theis, K.; Mendel, R.R.; Schwarz, G.; Kisker, C.
The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals
Structure
11
1251-1263
2003
Arabidopsis thaliana (Q9S850), Arabidopsis thaliana
Schwarz, G.; Mendel, R.R.
Molybdenum Cofactor Biosynthesis and Molybdenum Enzymes
Annu. Plant Biol.
57
623-647
2006
Arabidopsis thaliana
Astashkin, A.V.; Hood, B.L.; Feng, C.; Hille, R.; Mendel, R.R.; Raitsimring, A.M.; Enemark, J.H.
Structures of the Mo(V) forms of sulfite oxidase from Arabidopsis thaliana by pulsed EPR spectroscopy
Biochemistry
44
13274-13281
2005
Arabidopsis thaliana (Q9S850), Arabidopsis thaliana
Hemann, C.; Hood, B.L.; Fulton, M.; Haensch, R.; Schwarz, G.; Mendel, R.R.; Kirk, M.L.; Hille, R.
Spectroscopic and kinetic studies of Arabidopsis thaliana sulfite oxidase: nature of the redox-active orbital and electronic structure contributions to catalysis
J. Am. Chem. Soc.
127
16567-16577
2005
Arabidopsis thaliana
Haensch, R.; Lang, C.; Riebeseel, E.; Lindigkeit, R.; Gessler, A.; Rennenberg, H.; Mendel, R.R.
Plant sulfite oxidase as novel producer of H2O2: combination of enzyme catalysis with a subsequent non-enzymatic reaction step
J. Biol. Chem.
281
6884-6888
2006
Arabidopsis thaliana
Haensch, R.; Mendel, R.R.
Sulfite oxidation in plant peroxisomes
Photosynth. Res.
86
337-343
2005
Arabidopsis thaliana
Astashkin, A.V.; Johnson-Winters, K.; Klein, E.L.; Byrne, R.S.; Hille, R.; Raitsimring, A.M.; Enemark, J.H.
Direct demonstration of the presence of coordinated sulfate in the reaction pathway of Arabidopsis thaliana sulfite oxidase using 33S labeling and ESEEM spectroscopy
J. Am. Chem. Soc.
129
14800-14810
2007
Arabidopsis thaliana
Workun, G.J.; Moquin, K.; Rothery, R.A.; Weiner, J.H.
Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold
Microbiol. Mol. Biol. Rev.
72
228-48
2008
Arabidopsis thaliana (Q9S850), Bacillus licheniformis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) NRRL B-14911, Chlorella vulgaris, Deinococcus radiodurans, Erythrobacter litoralis, Escherichia coli, Gallus gallus (P07850), Homo sapiens, Maribacter sp. HTCC2170, Ogataea angusta, Paenarthrobacter aurescens, Rhizorhabdus wittichii RW1 (A5V4U9), Roseovarius nubinhibens, Rubrobacter xylanophilus, Saccharopolyspora erythraea, Spinacia oleracea, Streptomyces ambofaciens, Thermus thermophilus, Zea mays
Haensch, R.; Lang, C.; Rennenberg, H.; Mendel, R.R.
Significance of plant sulfite oxidase
Plant Biol.
9
589-595
2007
Arabidopsis thaliana, Cytisus scoparius, Gallus gallus, Hedera helix, Homo sapiens, Nicotiana plumbaginifolia, Phragmites australis, Populus tremula x Populus alba, Quercus ilex, Rattus norvegicus, Spinacia oleracea
Brychkova, G.; Xia, Z.; Yang, G.; Yesbergenova, Z.; Zhang, Z.; Davydov, O.; Fluhr, R.; Sagi, M.
Sulfite oxidase protects plants against sulfur dioxide toxicity
Plant J.
50
696-709
2007
Arabidopsis thaliana, Solanum lycopersicum (A5H1Q7), Solanum lycopersicum
Byrne, R.S.; Hansch, R.; Mendel, R.R.; Hille, R.
The oxidative half-reaction of Arabidopsis thaliana sulfite oxidase. Generation of superoxide by a peroxisomal enzyme
J. Biol. Chem.
284
35479-35484
2009
Arabidopsis thaliana
Randewig, D.; Hamisch, D.; Herschbach, C.; Eiblmeier, M.; Gehl, C.; Jurgeleit, J.; Skerra, J.; Mendel, R.; Rennenberg, H.; Hnsch, R.
Sulfite oxidase controls sulfur metabolism under SO2 exposure in Arabidopsis thaliana
Plant Cell Environ.
35
100-115
2012
Arabidopsis thaliana
Filiz, E.; Vatansever, R.; Ozyigit, I.I.
Insights into a key sulfite scavenger enzyme sulfite oxidase (SOX) gene in plants
Physiol. Mol. Biol. Plants
23
385-395
2017
Arabidopsis thaliana (Q9S850), Arabidopsis thaliana, Brachypodium distachyon (I1I8W3), Brachypodium distachyon, Populus trichocarpa (B9GJT3), Populus trichocarpa, Solanum lycopersicum (A5H1Q7), Solanum lycopersicum
Oshanova, D.; Kurmanbayeva, A.; Bekturova, A.; Soltabayeva, A.; Nurbekova, Z.; Standing, D.; Dubey, A.K.; Sagi, M.
Level of sulfite oxidase activity affects sulfur and carbon metabolism in Arabidopsis
Front. Plant Sci.
12
690830
2021
Arabidopsis thaliana
Bekturova, A.; Oshanova, D.; Tiwari, P.; Nurbekova, Z.; Kurmanbayeva, A.; Soltabayeva, A.; Yarmolinsky, D.; Srivastava, S.; Tureckova, V.; Strnad, M.; Sagi, M.
Adenosine 5' phosphosulfate reductase and sulfite oxidase regulate sulfite-induced water loss in Arabidopsis
J. Exp. Bot.
72
6447-6466
2021
Arabidopsis thaliana
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