ID   C13A6_CAEEL             Reviewed;         518 AA.
AC   Q27515;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Putative cytochrome P450 CYP13A6;
DE            EC=1.14.-.-;
GN   Name=cyp-13A6; Synonyms=cyp13a6; ORFNames=T10B9.3;
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; CAA88605.1; -; Genomic_DNA.
DR   PIR; T24779; T24779.
DR   RefSeq; NP_496113.1; NM_063712.3.
DR   AlphaFoldDB; Q27515; -.
DR   SMR; Q27515; -.
DR   STRING; 6239.T10B9.3; -.
DR   PaxDb; Q27515; -.
DR   PeptideAtlas; Q27515; -.
DR   EnsemblMetazoa; T10B9.3.1; T10B9.3.1; WBGene00011673.
DR   GeneID; 188357; -.
DR   KEGG; cel:CELE_T10B9.3; -.
DR   UCSC; T10B9.3; c. elegans.
DR   CTD; 188357; -.
DR   WormBase; T10B9.3; CE01657; WBGene00011673; cyp-13A6.
DR   eggNOG; KOG0158; Eukaryota.
DR   GeneTree; ENSGT00970000195979; -.
DR   HOGENOM; CLU_001570_5_2_1; -.
DR   InParanoid; Q27515; -.
DR   OMA; SLYWRNK; -.
DR   OrthoDB; 467733at2759; -.
DR   PhylomeDB; Q27515; -.
DR   PRO; PR:Q27515; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011673; Expressed in larva 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..518
FT                   /note="Putative cytochrome P450 CYP13A6"
FT                   /id="PRO_0000052266"
FT   BINDING         463
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;  59445 MW;  3B17B7A30E2792CA CRC64;
     MIFVLLSAVL LGVFTYSVWI WSYFIRKGIK GPRGFPGIGM LIQTIDHENP PFLKYRDWTK
     QYGPVYGFTE GPQQTMIISE PEMVNEIFKK QFDNFYGRKL RPIIGDPEKD KRVNIFSTQG
     KRWKRLRTLS SPSFSNNSLR KVRNSVQECG TEILWNIEQK VRKNEDIDML IVYQEYTLGV
     ISRIALGQSE SNMFKNPLLP KVQAIFNGSW HVFLITGIFP PLAGVFRKMS KMLPASFIPA
     FKIFDLIEVA VQARIDQRAK DEIKGVEPGE PQDFIDLFLD ARVPDVKILS GEANEDFAKS
     SVVKINKELT FDEIIAQCFV FLAAGFDTTA LSLSYATYLL ATHPEIQTKL QEEVDRECPD
     PEIFFDHLSK LKYLECVMKE TLRLYPLGTT ANTRKCMRET TINGVNFDEG MNIQVDTWTL
     HHNPRIWGED VEDFKPERWE NGACEHLEHN GSYIPFGSGP RQCIGMRLAQ MEQKILLAQI
     LKEYSFRTTK NTQIPVKLVG KLTLSPESVI VKLEPRDS