C13A2_CAEEL
ID C13A2_CAEEL Reviewed; 515 AA.
AC Q27518;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative cytochrome P450 CYP13A2;
DE EC=1.14.-.-;
GN Name=cyp-13A2; Synonyms=cyp13a2; ORFNames=T10B9.7;
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; CAA88607.1; -; Genomic_DNA.
DR PIR; T24781; T24781.
DR RefSeq; NP_496109.1; NM_063708.3.
DR AlphaFoldDB; Q27518; -.
DR SMR; Q27518; -.
DR BioGRID; 53027; 1.
DR DIP; DIP-25672N; -.
DR STRING; 6239.T10B9.7; -.
DR EPD; Q27518; -.
DR PaxDb; Q27518; -.
DR PeptideAtlas; Q27518; -.
DR EnsemblMetazoa; T10B9.7.1; T10B9.7.1; WBGene00011676.
DR GeneID; 188360; -.
DR KEGG; cel:CELE_T10B9.7; -.
DR UCSC; T10B9.7; c. elegans.
DR CTD; 188360; -.
DR WormBase; T10B9.7; CE01659; WBGene00011676; cyp-13A2.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q27518; -.
DR OMA; LMLICQV; -.
DR OrthoDB; 786853at2759; -.
DR PhylomeDB; Q27518; -.
DR PRO; PR:Q27518; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011676; 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..515
FT /note="Putative cytochrome P450 CYP13A2"
FT /id="PRO_0000052262"
FT BINDING 460
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 515 AA; 59232 MW; 38942AC8E3617F98 CRC64;
MSLGFVLAVT FSIFLGILTY YLWIWTYWMR KGVKGPRGRP FVGVLDVLLE HETPGLIKLG
EWTKKYGKVY GYTDGTQRTL VVADPAMVHE IFVKQFDNFY GRKLNPIQGN PEKEQRVHLL
AAQGYRWKRL RTISSQSFSN ASLKKMKRTV EDSALELLRH IEKQTAGGEQ IDMLRFYQEY
TMDVIGRFAM GQTDSMMFKN PIVNVVREIF CGSRKNLMLI CQVFPPIGQF IRDLTFKFPR
IPAFKLYSIM QDVVAARIAQ REREKGAESG EPQDFIDLFL DARSDDVDFS AEAREDFSKR
NLKITKELSA DEVVGQCFLF LIGGFDTTAL SLSYVTYLLA VNPKIQEKVI EEIAREFGTS
EVEFEKLGRL KYMDCVIKEA LRLYPLASIS NSRKCMKTTT VNGVKIEAGV YVQMDTWSLH
YDPELWGEDV KEFKPERWST DEPLEHKGAY LPFGLGPRQC IGMRLAIMEQ KILLTHLLKN
YTFETGNKTR IPLKLVGSAT TSPEDVFVHL RPRIW
