C13A5_CAEEL
ID C13A5_CAEEL Reviewed; 520 AA.
AC Q27514;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative cytochrome P450 CYP13A5;
DE EC=1.14.-.-;
GN Name=cyp-13A5; Synonyms=cyp13a5; ORFNames=T10B9.2;
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; CAA88604.1; -; Genomic_DNA.
DR PIR; T24778; T24778.
DR RefSeq; NP_496112.1; NM_063711.4.
DR AlphaFoldDB; Q27514; -.
DR SMR; Q27514; -.
DR STRING; 6239.T10B9.2; -.
DR EPD; Q27514; -.
DR PaxDb; Q27514; -.
DR PeptideAtlas; Q27514; -.
DR EnsemblMetazoa; T10B9.2.1; T10B9.2.1; WBGene00011672.
DR GeneID; 188356; -.
DR KEGG; cel:CELE_T10B9.2; -.
DR UCSC; T10B9.2; c. elegans.
DR CTD; 188356; -.
DR WormBase; T10B9.2; CE01656; WBGene00011672; cyp-13A5.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00970000195979; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q27514; -.
DR OMA; NIYVTHI; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; Q27514; -.
DR PRO; PR:Q27514; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011672; Expressed in adult 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..520
FT /note="Putative cytochrome P450 CYP13A5"
FT /id="PRO_0000052265"
FT BINDING 464
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 520 AA; 59524 MW; 0B7B19E25B7ADF3B CRC64;
MSLSILIAGA SFIGLLTYYI WIWSFWIRKG VKGPRGFPFF GVIHEFQDYE NPGLLKLGEW
TKEYGPIYGI TEGVEKTLIV SNPEFVHEVF VKQFDNFYGR KTNPIQGDPN KNKRAHLVSA
QGHRWKRLRT LSSPTFSNKN LRKIMSTVEE TVVELMRHLD DASAKGKAVD LLDYYQEFTL
DIIGRIAMGQ TESLMFRNPM LPKVKGIFKD GRKLPFLVSG IFPIAGTMFR EFFMRFPSIQ
PAFDIMSTVE KALNKRLEQR AADEKAGIEP SGEPQDFIDL FLDARANVDF FEEESALGFA
KTEIAKVDKQ LTFDEIIGQL FVFLLAGYDT TALSLSYSSY LLARHPEIQK KLQEEVDREC
PNPEVTFDQI SKLKYMECVV KEALRMYPLA SIVHNRKCMK ETNVLGVQIE KGTNVQVDTW
TLHYDPKVWG EDANEFRPER WESGDELFYA KGGYLPFGMG PRICIGMRLA MMEKKMLLTH
ILKKYTFETS TQTEIPLKLV GSATTAPRSV MLKLTPRHSN
