ID A0A3Q3X9N9_MOLML Unreviewed; 512 AA.
AC A0A3Q3X9N9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cytochrome P450 26B1 {ECO:0000256|ARBA:ARBA00040244};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000018954.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000018954.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-18-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55856, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:139258;
CC Evidence={ECO:0000256|ARBA:ARBA00036648};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55857;
CC Evidence={ECO:0000256|ARBA:ARBA00036648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178;
CC Evidence={ECO:0000256|ARBA:ARBA00036859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC Evidence={ECO:0000256|ARBA:ARBA00036859};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR AlphaFoldDB; A0A3Q3X9N9; -.
DR STRING; 94237.ENSMMOP00000018954; -.
DR Ensembl; ENSMMOT00000019263.1; ENSMMOP00000018954.1; ENSMMOG00000014342.1.
DR OMA; FVNTFQE; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF177; CYTOCHROME P450 26B1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620}.
FT BINDING 441
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 512 AA; 57888 MW; 038CACDC66898D95 CRC64;
MLFDSFDLVS ALATLAACLV SMALLLAVSQ QLWQLRWTAT RDKNCKLPMP KGSMGFPFIG
ETCHWLLQGS GFHASRRQKY GNVFKTHLLG RPLIRVTGAE NVRKVLMGEH TLVTVDWPQS
TATLLGPNSL ANSIGDIHRK RRKVFAKVFS HEALESYLPK IQQVIQESLR VWSSNPEAIN
VYRESQRLSF TMAVRVLLGF RVSEEEMRHL FSTFQDFVDN LFSLPIDLPF SGYRKGIRAR
DTLQKSIEKA IREKPLRSQG KDYSDALDVL MESAKENGTE LTMQELKEST IELIFAAFAT
TASASTSLIM QLLRHPPVLE RLREELRARG LLHNGCLFPE GELRLDTIVS LKYLDCVIKE
VLRLFTPVSG AYRTAMQTFE LDGVQIPKGW SVMYSIRDTH DTSAVFKDVD VFDPDRFSQE
RGEDKEGRFH YLPFGGGIRS CLGKQLANLF LRILAIELAS TSRFELATRH FPRVITVPVV
HPVDGLKVKF YGLDSNQNEI MAKSEELLGA TV
//
