C13A8_CAEEL
ID C13A8_CAEEL Reviewed; 509 AA.
AC Q27516; O01997;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative cytochrome P450 CYP13A8;
DE EC=1.14.-.-;
GN Name=cyp-13A8; Synonyms=cyp13a8; ORFNames=T10B9.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC They oxidize a variety of structurally unrelated compounds, including
CC steroids, fatty acids, and xenobiotics.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; Z48717; CAA88611.1; -; Genomic_DNA.
DR EMBL; Z95623; CAA88611.1; JOINED; Genomic_DNA.
DR PIR; T24785; T24785.
DR RefSeq; NP_496115.1; NM_063714.1.
DR AlphaFoldDB; Q27516; -.
DR SMR; Q27516; -.
DR BioGRID; 53025; 3.
DR STRING; 6239.T10B9.4; -.
DR PaxDb; Q27516; -.
DR PeptideAtlas; Q27516; -.
DR EnsemblMetazoa; T10B9.4.1; T10B9.4.1; WBGene00011674.
DR GeneID; 188358; -.
DR KEGG; cel:CELE_T10B9.4; -.
DR UCSC; T10B9.4; c. elegans.
DR CTD; 188358; -.
DR WormBase; T10B9.4; CE13541; WBGene00011674; cyp-13A8.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q27516; -.
DR OMA; LYDCKGF; -.
DR OrthoDB; 786853at2759; -.
DR PhylomeDB; Q27516; -.
DR PRO; PR:Q27516; -.
DR Proteomes; UP000001940; Chromosome II.
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; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..509
FT /note="Putative cytochrome P450 CYP13A8"
FT /id="PRO_0000052268"
FT BINDING 455
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:0000250"
SQ SEQUENCE 509 AA; 58565 MW; 718D86C86B7D8EEE CRC64;
MIFELILISI VTYYFWHWTF WKRRGLPGPW GVPIFGKAGA MLEDSFPPGY TLQKWTKEYG
KIYGFTEGMQ KVMVISDPDL VQEILVKQYD NFYGRKHNPV QGDPDKDKDI HIVGAQGFRW
KRLRTITAPA FSNGSIKKVL TTMEDSTQEL MKKLREESEN GKAVNMHLFY QEYTFDVISR
VAMGQPDSQM FKNPLLKDVK GFFEHNRWQI WMFSGGFPFA VSFLKWLFIK VGKFGAGPFI
VVQKSVTDAV MSRIAQREAD KKHGVEPGEA ADYIDMFLNA RAEVEHFGES NDEFHKSSSY
NNRQLTTQEI ISQCFVFLVA GFDTTAISLS YVTYFLALNP KIQSKLQDEV DKECPNDEIT
FDQLSKLKYM DNVIKESLRL FPFASFANSR RCMRNTVIGE QIVEAGVDVM IDTWTLHHDK
NVWGNDVEEF KPERWDSPLT PQQAYLSFGA GPRVCLGMRF ALLEQKGLLS HILKKYTFET
NAKTQLPIKL VGRATARPEN LFLSLKPRV
