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Database: UniProt
Entry: A0A3Q1I386_ANATE
LinkDB: A0A3Q1I386_ANATE
Original site: A0A3Q1I386_ANATE 
ID   A0A3Q1I386_ANATE        Unreviewed;       523 AA.
AC   A0A3Q1I386;
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=Cytochrome P450, family 4, subfamily V, polypeptide 8 {ECO:0000313|Ensembl:ENSATEP00000014640.2};
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:ENSATEP00000014640.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000014640.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   AlphaFoldDB; A0A3Q1I386; -.
DR   STRING; 64144.ENSATEP00000014640; -.
DR   Ensembl; ENSATET00000014872.2; ENSATEP00000014640.2; ENSATEG00000010169.2.
DR   GeneTree; ENSGT00940000157278; -.
DR   InParanoid; A0A3Q1I386; -.
DR   OrthoDB; 1611592at2759; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
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|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   523 AA;  60617 MW;  47768C0D55F98754 CRC64;
     MSFYLMAKLV NKMEVLLGTY TIALFGVSIF IATLTYITYK LLASYLHKWY EMKPIPEVPG
     TYPFIGNALQ FKTNAGDFFS QIQEYTVVFR DLPLLKLWVG MIPFVVLFHP ETVEVVLTNP
     VHMEKAYAYK FLHPWLGTGL LTSTGRKWRQ RRKMLTPTFH FSILTDFLEV MNEQAEILVG
     KLEKKAGKGP FNCFSHITLC ALDIICETAM GKKIYAQSNS DSEYVRSVYK MSDIVSRRQR
     TPWFWPDFVY NYFGEGRDHD KTLKILHSFT YKVIHERAES ISSTESDSDS DKGTRKRRAF
     LDMLLKTTYE DGNRMSHEDI QEEVDTFMFR GHDTTAASMN WALHLLGSHP EAHSKVQQEL
     QEVFGTSDRP VNTEDLKKLK YLECVIKEAL RLFPSVPFFA RSICEDCYIN GFKVSKGANA
     IIITYALHRD PRYFPEPEEF RPERFLPENS EGRPPYAYIP FSAGLRNCIG QRFALMEEKV
     ILSSILRNFS VEACQKREDL RPVGELILRP EKGIWIKLEK RTT
//
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