C13A3_CAEEL
ID C13A3_CAEEL Reviewed; 520 AA.
AC Q27517;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative cytochrome P450 CYP13A3;
DE EC=1.14.-.-;
GN Name=cyp-13A3; Synonyms=cyp13a3; ORFNames=T10B9.5;
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; CAA88606.1; -; Genomic_DNA.
DR PIR; T24780; T24780.
DR RefSeq; NP_496110.1; NM_063709.1.
DR AlphaFoldDB; Q27517; -.
DR SMR; Q27517; -.
DR STRING; 6239.T10B9.5; -.
DR PaxDb; Q27517; -.
DR EnsemblMetazoa; T10B9.5.1; T10B9.5.1; WBGene00011675.
DR GeneID; 188359; -.
DR KEGG; cel:CELE_T10B9.5; -.
DR UCSC; T10B9.5; c. elegans.
DR CTD; 188359; -.
DR WormBase; T10B9.5; CE01658; WBGene00011675; cyp-13A3.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00970000195979; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q27517; -.
DR OMA; EEVYTLW; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; Q27517; -.
DR PRO; PR:Q27517; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011675; Expressed in larva.
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 CYP13A3"
FT /id="PRO_0000052263"
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; 59640 MW; 9B03FA7DD5C789DE CRC64;
MSLSILIAIA LFIGVFTYYL WIWSFWMRKG IKGPRGLPFF GIINAFQSYE KPWILRLGDW
TKEYGPMYGF TDGVEKTLVV SDPEFVHEVF VKQFDNFYAR KQNPLQGDPD KDPRIHLVTS
QGHRWKRLRT LASPTFSNKS LRKIFSTVEE SVAEMMRHLE KGTAGGKTID ILEYYQEFTM
DIIGKIAMGQ SGSMMFENPW LDKIRAIFNT RGNIIFIICG IVPFTGSIFR WFFSKVPTAQ
TVTSLMHTLE IALTKRVEQR AADEKAGIES SGEPQDFIDL FLDVQADTDF LEDETKNGFA
RSQIVKVDKH LTFDEIIGQL FVFLLAGYDT TALSLSYSSY LLARHPEIQK KLQEEVDREC
PDPEVTFDQL SKLKYMECVI KETLRLYPLA SIVHNRKCMK STTVLGMKIE EGTNVQADTW
TLHYDPKFWG ENANEFKPER WESGDEQAVA KGAYLPFGLG PRICIGMRLA YMEEKMLLAQ
ILKKYSLETT FETHIPLKLV GIATTAPTNV HLKLKPRHSD
