CRTDH_FLAS9
ID CRTDH_FLAS9 Reviewed; 488 AA.
AC Q7WT72;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=1-hydroxycarotenoid 3,4-desaturase {ECO:0000303|PubMed:15251462};
DE EC=1.3.99.27 {ECO:0000269|PubMed:15251462};
DE AltName: Full=1'-hydroxy-gamma-carotene 3,4-desaturase {ECO:0000303|PubMed:12804761};
DE AltName: Full=1-hydroxycarotenoid 3,4-dehydrogenase {ECO:0000303|PubMed:15251462};
GN Name=crtD {ECO:0000303|PubMed:12804761};
OS Flavobacterium sp. (strain P99-3).
OC Bacteria; Bacteroidetes; Flavobacteriia.
OX NCBI_TaxID=216393;
RN [1] {ECO:0000312|EMBL:BAC77671.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P99-3 {ECO:0000312|EMBL:BAC77671.1};
RX PubMed=12804761; DOI=10.1016/s0014-5793(03)00513-1;
RA Teramoto M., Takaichi S., Inomata Y., Ikenaga H., Misawa N.;
RT "Structural and functional analysis of a lycopene beta-monocyclase gene
RT isolated from a unique marine bacterium that produces myxol.";
RL FEBS Lett. 545:120-126(2003).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=15251462; DOI=10.1016/j.febslet.2004.05.085;
RA Teramoto M., Raehlert N., Misawa N., Sandmann G.;
RT "1-Hydroxy monocyclic carotenoid 3,4-dehydrogenase from a marine bacterium
RT that produces myxol.";
RL FEBS Lett. 570:184-188(2004).
CC -!- FUNCTION: Catalyzes the introduction of a C-3,4 double bond into 1'-
CC hydroxy-gamma-carotene and rhodopin (1-hydroxylycopene) to yield 1'-
CC hydroxytorulene and (3E)-3,4-didehydrorhodopin, respectively. Can also
CC 1-hydroxy-all-trans-1,2-dihydro-neurosporene, 1,1'-dihydroxy-1,1',2,2'-
CC tetrahydroneurosporene and 1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene
CC (PubMed:15251462). Probably involved in the synthesis of myxol, a
CC gamma-carotene derivative (Probable). May use FAD as a proton acceptor
CC (By similarity). {ECO:0000250|UniProtKB:L7WC64,
CC ECO:0000269|PubMed:15251462, ECO:0000305|PubMed:15251462}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + rhodopin = (3E)-3,4-didehydrorhodopin + AH2;
CC Xref=Rhea:RHEA:30919, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:35331, ChEBI:CHEBI:62481; EC=1.3.99.27;
CC Evidence={ECO:0000269|PubMed:15251462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-hydroxy-gamma-carotene + A = 1'-hydroxytorulene + AH2;
CC Xref=Rhea:RHEA:59332, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:80133, ChEBI:CHEBI:80134;
CC Evidence={ECO:0000269|PubMed:15251462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hydroxy-all-trans-1,2-dihydro-neurosporene + A = AH2 +
CC demethylspheroidene; Xref=Rhea:RHEA:59336, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:62505, ChEBI:CHEBI:138077;
CC Evidence={ECO:0000269|PubMed:15251462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene + A = 1'-
CC hydroxy-demethylspheroidene + AH2; Xref=Rhea:RHEA:59340,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:138076,
CC ChEBI:CHEBI:143013; Evidence={ECO:0000269|PubMed:15251462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene + A = 1,1'-
CC dihydroxy-3,4-didehydro-1,2-dihydrolycopene + AH2;
CC Xref=Rhea:RHEA:59444, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:63065, ChEBI:CHEBI:132450;
CC Evidence={ECO:0000269|PubMed:15251462};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000255|RuleBase:RU362075,
CC ECO:0000269|PubMed:15251462}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:L7WC64}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000255|RuleBase:RU362075}.
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DR EMBL; AB097813; BAC77671.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WT72; -.
DR SMR; Q7WT72; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02734; crtI_fam; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; FAD; Flavoprotein; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..488
FT /note="1-hydroxycarotenoid 3,4-desaturase"
FT /id="PRO_0000447220"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
FT BINDING 55..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
FT BINDING 431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
FT BINDING 461
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
FT BINDING 468..469
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:L7WC64"
SQ SEQUENCE 488 AA; 55087 MW; 693361DF792B6638 CRC64;
MKKAIIIGSG IAGLAAALRL KKKGYQVSVF EKNDYAGGKL HAIELGGYRF DLGPSLFTLP
HLIDELHQLF PDVEIDFNYI KKKTACHYFW EDGTSFEAPA DLENFAVKAA EIFDEKQNTL
SKYLQNSKMK YESTKSLFLE KSLHKSNTYF SKQTLKAILK IPFLGINNTL DQENKKFSNP
KLNQLFNRYA TYNGSSPYLT PGIMSMIPYL ELGLGTYYPQ GGMHRISQSL FELAQKVGVE
FRFRKNVKKI NHSNNKVTGV TTEKGTHDAD IVLCNMDVFP TYRQLLQDIK APEKTLKQER
SSSALIFYWG IKKSFPQLDL HNILFSENYK AEFEAIFNNK SLYEDPTVYI NITSKQSPQD
APKGCENWFV MINTPGDYGQ NWENLVIKAK KNILSKIKRC LNIDVEELID VEYVLTPQGI
EKNTSSYRGA LYGAASNNKF AAFLRHPNFN KTIGNLYHVG GSVHPGGGIP LCLLSAKITA
DLIPNTNA
