ID A0A3B4V519_SERDU Unreviewed; 536 AA.
AC A0A3B4V519;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000025818.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000025818.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B4V519; -.
DR STRING; 41447.ENSSDUP00000025818; -.
DR Ensembl; ENSSDUT00000026285.1; ENSSDUP00000025818.1; ENSSDUG00000018708.1.
DR GeneTree; ENSGT00950000182913; -.
DR OMA; VHHPFDG; -.
DR Proteomes; UP000261420; Unplaced.
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 Sensory transduction {ECO:0000256|ARBA:ARBA00023305};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 318
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 531
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 536 AA; 61129 MW; 277DB822F7AF9F1B CRC64;
MSLLSGDRFE HPAGGYRKIF ETCEELSEPL PATVTGRIPS FLKGSLLRLG PGLFEVGDEP
FYHLFDGQAL MHKFDFKNGQ VTYYRKFVRT DAYVRAITEK RVVITEFGTF AYPDPCKNIF
SRFFSYFKGV EVTDNCLVNV YPVGEDFYAV TETNYITKVN PDTLETLKKV IDMCNYININ
GVTAHPHIEN DGTVYNIGNC MGKGATLAYN IVKIPPEQKD KSDPIEKSKV VVQFPSAERF
KPSYVHSFGM SENYFVFVET PVKINLLKFL SAWSIRGSNY MDCFESNESQ GTLFHVARKD
PGEYIDHKFK GAPIGMFHHI NTYEDQGFIV FDLCAWKGFE FVYNYLWLAN LRANWEEVKK
AAMMAPQPEV RRYVIPLDVH KEEQGKNLVS LPYTTATAVM HADGTIWLEP EVLFSGPRQA
FEFPQINYNR FGGKNYTYTY GLGLNHFIPD RICKLNVKTR ETWVWQEPDS YPSEPLFVQT
PDGIDEDDGV LLTIVAAPGS QRPAYLLILN AKDLSEVARA EVECNIPVTF HGMYKP
//
