ID A0A060W822_ONCMY Unreviewed; 553 AA.
AC A0A060W822;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Retinoid isomerohydrolase {ECO:0000256|ARBA:ARBA00040820};
DE EC=3.1.1.64 {ECO:0000256|ARBA:ARBA00039141};
DE EC=5.3.3.22 {ECO:0000256|ARBA:ARBA00038936};
DE AltName: Full=Lutein isomerase {ECO:0000256|ARBA:ARBA00041301};
DE AltName: Full=Meso-zeaxanthin isomerase {ECO:0000256|ARBA:ARBA00042900};
GN ORFNames=GSONMT00069230001 {ECO:0000313|EMBL:CDQ63463.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ63463.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ63463.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ63463.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = 11-cis-retinol + H(+)
CC + hexadecanoate; Xref=Rhea:RHEA:31775, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16302,
CC ChEBI:CHEBI:17616; EC=3.1.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00035843};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:31771, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16302, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:63410; EC=3.1.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00036037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein = (3R,3'S)-zeaxanthin; Xref=Rhea:RHEA:12729,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:138919; EC=5.3.3.22;
CC Evidence={ECO:0000256|ARBA:ARBA00035787};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787, ECO:0000256|RuleBase:RU003799}.
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DR EMBL; FR904442; CDQ63463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060W822; -.
DR STRING; 8022.A0A060W822; -.
DR PaxDb; 8022-A0A060W822; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0120254; P:olefinic compound metabolic process; IEA:UniProt.
DR GO; GO:0001523; P:retinoid metabolic process; IEA:UniProt.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR PANTHER; PTHR10543:SF57; RETINOID ISOMEROHYDROLASE; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00023305};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 548
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 553 AA; 62874 MW; D9DC3763B822B68C CRC64;
MVVQSSQIKL APGLQFLTFF SRFEHPAGGY KKIFETVEEL SEPVPATVTG LIPSFLKGSL
LRLGPGLFEV GDEPFYHLFD GQALMHKFDF KNGQVTYFNK YVKTDAYVRA ITEKRVVITE
FGTFAYPDPC KNIFSRFFTY FKGVEVTDNC LVNVYPIGED YYAVTETNYI TKVNTDTLDT
LKKVDLCNYV NINGVTAHPH IERDGTVFNI GNCMGKGASL AYNVVRIPPT QKDKSDPIEK
SKVVVQFPSA ERFKPSYVHS FGMSENYFVF VETPVKINLL KFLSAWSIRG SNYMDCFESN
EVLGTLFHIA RKDIGGGQGE YIDHKFRAAP INLFHHINTY EDNGFIVADV CTWKGFEFVY
NYLWLANLRS NWEEVKKAAM MAPQPEVRRY VIPLDIHREE QGKNLICLPY TTATAVMRTD
GTIWLEPEVL FSGPRQAFEF PQINYEKHGG KNYSYAYALG LNHFIPDRII KLNVKTKETW
VWQEPDSYPS EPLFVQTPDG VDEDDGVLLT VVVSPGAQKS GYMLILNAKD MSEIARAEVD
CPIPVTFHGM YKK
//
