C13A4_CAEEL
ID C13A4_CAEEL Reviewed; 520 AA.
AC Q27513;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative cytochrome P450 CYP13A4;
DE EC=1.14.-.-;
GN Name=cyp-13A4; Synonyms=cyp13a4; ORFNames=T10B9.1;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z48717; CAA88603.1; -; Genomic_DNA.
DR PIR; T24777; T24777.
DR RefSeq; NP_496111.1; NM_063710.1.
DR AlphaFoldDB; Q27513; -.
DR SMR; Q27513; -.
DR STRING; 6239.T10B9.1; -.
DR PaxDb; Q27513; -.
DR PeptideAtlas; Q27513; -.
DR PRIDE; Q27513; -.
DR EnsemblMetazoa; T10B9.1.1; T10B9.1.1; WBGene00011671.
DR GeneID; 188355; -.
DR KEGG; cel:CELE_T10B9.1; -.
DR UCSC; T10B9.1; c. elegans.
DR CTD; 188355; -.
DR WormBase; T10B9.1; CE01654; WBGene00011671; cyp-13A4.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00970000195979; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q27513; -.
DR OMA; ICHNASI; -.
DR OrthoDB; 786853at2759; -.
DR PhylomeDB; Q27513; -.
DR PRO; PR:Q27513; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011671; Expressed in adult organism.
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 CYP13A4"
FT /id="PRO_0000052264"
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; 59371 MW; 996C1172B8D64E93 CRC64;
MSLSLLIAGA LFIGFLTYYI WIWSFWIRKG VKGPRGFPFF GVILKFHDYE NPGLLKLGEW
TKKYGSIYGI TEGVEKTLVV SNPEFVHEVF VKQFDNFYGR KTNPIQGDPN KNKRAHLVLA
QGHRWKRLRT LASPTFSNKS LRKIMSTVEE TVVELMRHLD EASAKGKAVD LLDYYQEFTL
DIIGRIAMGQ TESLMFRNPM LPKVKEIFKK GGKMPFLIAG VFPIAGTLMR QLFMKFPKFS
PAFGIMNTME KALNKRLEQR AADKKAGIEP SGEPQDFIDL FLDARANVDF IEEESTLGFA
KSEVLKVDKH LTFDEIIGQL FVFLLAGYDT TALSLSYSSY LLATHPEIQK KLQEEVDREC
PDPEVTFDQI SKLKYMECVV KEALRMYPLA SLVHNRKCMK KTNVLGVEID EGTNVQVDTW
TLHYDPKVWG DDASEFKPER WETGDELFYA KGGYLPFGMG PRICIGMRLA MMEEKLLLTH
ILKKYTFDTS TETEIPLKLV GSATIAPRNV MLKLTPRHSN
