C13A1_CAEEL
ID C13A1_CAEEL Reviewed; 519 AA.
AC Q27520;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative cytochrome P450 CYP13A1;
DE EC=1.14.-.-;
GN Name=cyp-13A1; Synonyms=cyp13a1; ORFNames=T10B9.8;
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;
CC Evidence={ECO:0000250|UniProtKB:Q16678};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; Z48717; CAA88610.1; -; Genomic_DNA.
DR PIR; T24784; T24784.
DR RefSeq; NP_496108.1; NM_063707.4.
DR AlphaFoldDB; Q27520; -.
DR SMR; Q27520; -.
DR STRING; 6239.T10B9.8; -.
DR EPD; Q27520; -.
DR PaxDb; Q27520; -.
DR PeptideAtlas; Q27520; -.
DR EnsemblMetazoa; T10B9.8.1; T10B9.8.1; WBGene00011677.
DR EnsemblMetazoa; T10B9.8.2; T10B9.8.2; WBGene00011677.
DR GeneID; 188361; -.
DR UCSC; T10B9.8; c. elegans.
DR CTD; 188361; -.
DR WormBase; T10B9.8; CE01660; WBGene00011677; cyp-13A1.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00970000196408; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q27520; -.
DR OMA; KNHARFR; -.
DR OrthoDB; 786853at2759; -.
DR PhylomeDB; Q27520; -.
DR PRO; PR:Q27520; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011677; Expressed in multicellular organism and 2 other tissues.
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..519
FT /note="Putative cytochrome P450 CYP13A1"
FT /id="PRO_0000052261"
FT BINDING 465
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|UniProtKB:Q16678"
SQ SEQUENCE 519 AA; 60044 MW; 3AF37EDC43539D7A CRC64;
MGYFWFPWFS AIFVAVFSYY IWQWTFWRRR GVVGPMGFPV LGVFLNSLDN NFPFPLQCRE
WTKKFGKIYG FTEGTLKTLV ISDPELVHEV FVTQYDNFYG RKRNPIQGDS EKEKRTNLFA
AQGFRWKRLR AISSPTFSNS SLRKLYQTVE DSALELLRHI EKQSAGGKQI DMLKFYQEFT
LDVIGRIAMG QTDSQMFKNP IMPIVSKLFQ GNFAKLFLIG GIFPTFLVEI IRQILLKNLK
VGSFRKINEI TLDAIHNRIK QREEDQKNGI EIGEPADFID LFLDAKAEDV EHFGENNGDF
SKSTTYTNRQ LTTEEIVGQC TVFLIAGFDT TALSLSYATY LLATHPEIQK KLQEEVNREC
PNPEVTIDQL SKLKYMECVF KEALRLYPLG AFANSRRCMR NTKLGNMKVE VGTMIQVDTW
TLHTDPNIWG DDAEDFKPER WQTPNSDQIY QKSGYIPFGL GPRQCIGMRL AYMEEKILLV
HILRKFTFET GAKTEIPLKL IGRATTQPES VWMHLNPRN
