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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
 
 
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