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Database: UniProt
Entry: A0A3P9NUQ8_POERE
LinkDB: A0A3P9NUQ8_POERE
Original site: A0A3P9NUQ8_POERE 
ID   A0A3P9NUQ8_POERE        Unreviewed;       528 AA.
AC   A0A3P9NUQ8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   Name=RPE65 {ECO:0000313|Ensembl:ENSPREP00000013302.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000013302.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000013302.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000013302.1};
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; A0A3P9NUQ8; -.
DR   STRING; 8081.ENSPREP00000013302; -.
DR   Ensembl; ENSPRET00000013438.1; ENSPREP00000013302.1; ENSPREG00000009027.1.
DR   GeneTree; ENSGT00950000182913; -.
DR   OMA; GTWIHIA; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000009027; Expressed in head.
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   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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000242638};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00023305};
KW   Vision {ECO:0000256|ARBA:ARBA00023305}.
FT   BINDING         177
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         310
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         523
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   528 AA;  60169 MW;  3B27ECE12DC16FE2 CRC64;
     IFEHPAGSYK KIFETCEELA EPLPATVTGR IPSFLKGSLL RLGPGLFEVG DEPFYHLFDG
     QALMHKFDFK NGQVTYYRKF VRTDAYVRAI TEKRVVITEF GTFAYPDPCK NIFSRFFSYF
     KGVEVTDNCL VNVYPIGEDF YAVTETNYIT KVNTDTLETL KKVDMCNFVN INGVTAHPHI
     EQDGTVYNIG NCMGKGATLA YNIVKIPPTQ KDKSDPIEKS KVVVQFPSAE RFKPSYVHSF
     GMSENYFVFV ETPVKINLLK FLSAWSIRGS NYMDCFESNE SQGTIFHVAK KDPGEYIDLK
     FKGAPIGMFH HINTYEDQGF IVLDICSWKG FEFVYNYLWL ANLRANWEEV KKAAMMAPQP
     EVRRYVIPLD VHKEEQGKNL VSLPYTTATA VMHADGMVWL EPEVLFSGPR QAFEFPQINY
     QKYGGKNYSY AYGLGLNHFI PDRICKLNVR TKETWVWQEP ESYPSEPLFV QTPDGVDEDD
     GVLLTIVAAP GSQRPAYMLI LNAKDLSEIA RAEVECSIPV TFHGMYKQ
//
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