C13A7_CAEEL
ID C13A7_CAEEL Reviewed; 518 AA.
AC Q27519;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Putative cytochrome P450 CYP13A7;
DE EC=1.14.-.-;
GN Name=cyp-13A7; Synonyms=cyp13a7; ORFNames=T10B9.10;
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; CAA88609.1; -; Genomic_DNA.
DR PIR; T24783; T24783.
DR RefSeq; NP_496114.1; NM_063713.1.
DR AlphaFoldDB; Q27519; -.
DR SMR; Q27519; -.
DR BioGRID; 53029; 1.
DR DIP; DIP-27079N; -.
DR STRING; 6239.T10B9.10; -.
DR PaxDb; Q27519; -.
DR PeptideAtlas; Q27519; -.
DR EnsemblMetazoa; T10B9.10.1; T10B9.10.1; WBGene00000372.
DR GeneID; 188362; -.
DR KEGG; cel:CELE_T10B9.10; -.
DR UCSC; T10B9.10; c. elegans.
DR CTD; 188362; -.
DR WormBase; T10B9.10; CE01655; WBGene00000372; cyp-13A7.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00970000195979; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q27519; -.
DR OMA; RFMNDNG; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; Q27519; -.
DR PRO; PR:Q27519; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000372; Expressed in material anatomical entity and 1 other tissue.
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..518
FT /note="Putative cytochrome P450 CYP13A7"
FT /id="PRO_0000052267"
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 518 AA; 59000 MW; CC04283EF87B9EA7 CRC64;
MSFSILIAIA IFVGIISYYL WIWSFWIRKG VKGPRGLPFL GVIHKFTNYE NPGALKFSEW
TKKYGPVYGI TEGVEKTLVI SDPEFVHEVF VKQFDNFYGR KLTAIQGDPN KNKRVPLVAA
QGHRWKRLRT LASPTFSNKS LRKIMGTVEE SVTELVRSLE KASAEGKTLD MLEYYQEFTM
DIIGKMAMGQ EKSLMFRNPM LDKVKTIFKE GRNNVFMISG IFPFVGIALR NIFAKFPSLQ
MATDIQSILE KALNKRLEQR EADEKAGIEP SGEPQDFIDL FLDARSTVDF FEGEAEQDFA
KSEVLKVDKH LTFDEIIGQL FVFLLAGYDT TALSLSYSSY LLATHPEIQK KLQEEVDREC
PDPEVTFDQL SKLKYLECVV KEALRLYPLA SLVHNRKCLK TTNVLGMEIE AGTNINVDTW
SLHHDPKVWG DDVNEFKPER WESGDELFFA KGGYLPFGMG PRICIGMRLA MMEMKMLLTN
ILKNYTFETT PETVIPLKLV GTATIAPSSV LLKLKSRF