ID   C13B1_CAEEL             Reviewed;         510 AA.
AC   O17624; O17625; Q27491; Q9TVN5;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 3.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Putative cytochrome P450 cyp-13B1;
DE            EC=1.14.-.-;
GN   Name=cyp-13B1 {ECO:0000312|WormBase:F02C12.5};
GN   ORFNames=F02C12.5 {ECO:0000312|WormBase:F02C12.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19575768; DOI=10.1111/j.1474-9726.2009.00501.x;
RA   Oliveira R.P., Porter Abate J., Dilks K., Landis J., Ashraf J.,
RA   Murphy C.T., Blackwell T.K.;
RT   "Condition-adapted stress and longevity gene regulation by Caenorhabditis
RT   elegans SKN-1/Nrf.";
RL   Aging Cell 8:524-541(2009).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases
CC       (Probable). They oxidize a variety of structurally unrelated compounds,
CC       including steroids, fatty acids, and xenobiotics (Probable). May play a
CC       role in the regulation of lifespan (PubMed:19575768).
CC       {ECO:0000269|PubMed:19575768, ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q16678};
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a 25% increase
CC       in lifespan. {ECO:0000269|PubMed:19575768}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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DR   EMBL; Z54269; CAB54208.1; -; Genomic_DNA.
DR   EMBL; Z92827; CAB54208.1; JOINED; Genomic_DNA.
DR   PIR; T19575; T19575.
DR   PIR; T19576; T19576.
DR   PIR; T19577; T19577.
DR   RefSeq; NP_510233.1; NM_077832.3.
DR   AlphaFoldDB; O17624; -.
DR   SMR; O17624; -.
DR   BioGRID; 46365; 1.
DR   DIP; DIP-25013N; -.
DR   STRING; 6239.F02C12.5a; -.
DR   EPD; O17624; -.
DR   PaxDb; O17624; -.
DR   PeptideAtlas; O17624; -.
DR   EnsemblMetazoa; F02C12.5.1; F02C12.5.1; WBGene00008519.
DR   GeneID; 181462; -.
DR   KEGG; cel:CELE_F02C12.5; -.
DR   UCSC; F02C12.5c; c. elegans.
DR   CTD; 181462; -.
DR   WormBase; F02C12.5; CE23627; WBGene00008519; cyp-13B1.
DR   eggNOG; KOG0158; Eukaryota.
DR   GeneTree; ENSGT00970000196718; -.
DR   InParanoid; O17624; -.
DR   OrthoDB; 825914at2759; -.
DR   PhylomeDB; O17624; -.
DR   PRO; PR:O17624; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00008519; Expressed in embryo and 3 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..510
FT                   /note="Putative cytochrome P450 cyp-13B1"
FT                   /id="PRO_0000051924"
FT   BINDING         456
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|UniProtKB:Q16678"
SQ   SEQUENCE   510 AA;  58260 MW;  B05B299244154584 CRC64;
     MGAIIVLVVL FATIAGYFKW IHTYWRRRGI SGPEGLPFIG NYYDLADVNK PRGYLIHKWT
     QKFGKVFGYY EGAVPVLVVS DMDMLQELFL KKFDNFYARK STNHIHGNLE CSKSEPRINL
     FTSRGARWKR LRALASPGFS VKALKQVHDV MEDSAINMVD LMAKHEDGKP FNIHAYFQEF
     TYDVISRLAM GQPNSELFNN SGVEIVKSIF MRTHRVLPWY FTVLFPQFEH LVKRMFYNHA
     AVQGGDIEKL LLICKKTVES RIQEREENAK LGFENAENDF IDMFLNYYSE QVEDIEFGST
     VEKKVTAEDV IGACFVFLLA GFDTTANSLA YASYLLAKHP EKMKLAQEEV DTVVGSENVS
     YDDMTKLKYL DAVVRESLRL YPVAWFACSR ECVKPTTLGD IYIDKGVKIE ADVMSLHRSK
     EIWGENADDF VPERWLEPSS RHTMSWIPFG AGPRQCVGMR LGLSEAKTAL AHLLRRYDLV
     AGVETEKELN ILGCTTTSPE AVTLYLKPRI