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Information on EC 1.13.11.63 - beta-carotene 15,15'-dioxygenase and Organism(s) Uncultured marine bacterium 66A03 and UniProt Accession Q4PNI0

for references in articles please use BRENDA:EC1.13.11.63
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IUBMB Comments
Requires Fe2+. The enzyme cleaves beta-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products . The enzyme can also process beta-cryptoxanthin, 8'-apo-beta-carotenal, 4'-apo-beta-carotenal, alpha-carotene and gamma-carotene in decreasing order. The presence of at least one unsubstituted beta-ionone ring in a substrate greater than C(30) is mandatory . A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].
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Uncultured marine bacterium 66A03
UNIPROT: Q4PNI0
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The taxonomic range for the selected organisms is: uncultured marine bacterium 66A03
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
beta-cd, bcmo1, ninab, beta-carotene 15,15'-monooxygenase, beta-carotene oxygenase 2, betaco, beta-carotene-15,15'-dioxygenase, beta-carotene 15,15'-monooxygenase 1, beta,beta-carotene 15,15'-monooxygenase, beta,beta-carotene-15,15'-oxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-carotene 15,15'-dioxygenase
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PATHWAY SOURCE
PATHWAYS
-
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SYSTEMATIC NAME
IUBMB Comments
beta-carotene:oxygen 15,15'-dioxygenase (bond-cleaving)
Requires Fe2+. The enzyme cleaves beta-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products [8]. The enzyme can also process beta-cryptoxanthin, 8'-apo-beta-carotenal, 4'-apo-beta-carotenal, alpha-carotene and gamma-carotene in decreasing order. The presence of at least one unsubstituted beta-ionone ring in a substrate greater than C(30) is mandatory [5]. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-carotene + O2
2 all-trans-retinal
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-carotene + O2
2 all-trans-retinal
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BLH_UNCMB
275
7
31037
Swiss-Prot
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a xylose-fermenting Saccharomyces cerevisiae strain S8
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sun, L.; Kwak, S.; Jin, Y.S.
Vitamin A production by engineered Saccharomyces cerevisiae from xylose via two-phase in situ extraction
ACS Synth. Biol.
8
2131-2140
2019
uncultured marine bacterium 66A03 (Q4PNI0)
Manually annotated by BRENDA team