ID   A0A3Q1GZT6_ANATE        Unreviewed;       526 AA.
AC   A0A3Q1GZT6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Retinal Mueller cells isomerohydrolase-like {ECO:0000313|Ensembl:ENSATEP00000000435.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000000435.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000000435.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006787, ECO:0000256|RuleBase:RU003799}.
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DR   AlphaFoldDB; A0A3Q1GZT6; -.
DR   STRING; 64144.ENSATEP00000000435; -.
DR   Ensembl; ENSATET00000000448.2; ENSATEP00000000435.2; ENSATEG00000000298.2.
DR   GeneTree; ENSGT00950000182913; -.
DR   Proteomes; UP000265040; Unplaced.
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:SF43; ALL-TRANS-RETINYL ESTER 13-CIS ISOMEROHYDROLASE-RELATED; 1.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR604294-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040}.
FT   BINDING         180
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         306
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         519
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   526 AA;  59671 MW;  BD2F824CFD2A0B68 CRC64;
     IYSGVEHPAA GYRKIFESVE ELTEPIPAKI TGVVPSWLGG SLLRMGPGLF EVGDEPFHHM
     FDGLALVHKF DLKNGQVTYY RKFIRSDSYV RAMTENRVVI TEFGTAAYPD PCKNIFSRFF
     TYFRGAEVTD NCLVNIYPIG EDFYAVTETN YITKVDPDSL ETLKKVDLCK YLSVNGLTAH
     PHTDTDGTIY NIGNCFGKNM SLAYNIVKIP PAHKDPIEKS QVVVQLPSSE RLKPSYIHSF
     GMTDNYFVFV EQPVKINLLK FLTLWNIRGA TYMDCFESND SMGVSRNPAG YLSSHKFRTS
     AFNLFHHINA YEDEGYVIVD LCTWKGHDFV YNYLYLANLK GEWEEVKRAA LRAPQPEVRR
     YVLPLDIHRE DQGKNLVSLS YTTATAVLHS DGTIWLEPEV LFSGPRQAFE FPQINYSQYR
     GKKYSFAYGL GLTHFIPDRI VKLNVQTKET WVWQEEECYP SEPLFVPTPG ATEEDDGVLL
     SVVVKPGAER PSFLLILDAM KLTELARADV NTIIPVTLHG TYKPAS
//