PHYD1_CAEBR
ID PHYD1_CAEBR Reviewed; 288 AA.
AC P0C660; A8WMU1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Phytanoyl-CoA dioxygenase domain-containing protein 1 homolog;
DE EC=1.-.-.-;
GN ORFNames=CBG00325;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Has alpha-ketoglutarate-dependent dioxygenase activity. Does
CC not show detectable activity towards fatty acid CoA thioesters. Is not
CC expected to be active with phytanoyl CoA (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the PhyH family. PHYHD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; HE600968; CAP21796.1; -; Genomic_DNA.
DR RefSeq; XP_002632320.1; XM_002632274.1.
DR AlphaFoldDB; P0C660; -.
DR SMR; P0C660; -.
DR STRING; 6238.CBG00325; -.
DR EnsemblMetazoa; CBG00325.1; CBG00325.1; WBGene00023733.
DR GeneID; 8574317; -.
DR KEGG; cbr:CBG_00325; -.
DR CTD; 8574317; -.
DR WormBase; CBG00325; CBP05721; WBGene00023733; -.
DR eggNOG; KOG3290; Eukaryota.
DR HOGENOM; CLU_048953_0_0_1; -.
DR InParanoid; P0C660; -.
DR OMA; KYSEDNW; -.
DR OrthoDB; 1316775at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..288
FT /note="Phytanoyl-CoA dioxygenase domain-containing protein
FT 1 homolog"
FT /id="PRO_0000313637"
FT BINDING 95
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 149..151
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 288 AA; 32833 MW; CE962159F24B2635 CRC64;
MSDLRQNFER DGFVVIENVF NDQEIEEIKG AIGKIVEDMN LAEHPKSVFS TYDEDKHAAD
SYFLNSSDKI RFFFEEGAVD KDGELTVPKD KALNKIGHGL HLLDPTFKKM TFNSKIQKIF
QGIGYQEPEV VQSMYIFKQP KIGGAVTDHV DSTFLRVNPI DHLTGVWIAI DEASVENGCL
SFIPGSHKDT STSDYRFVRT HDTTGGPLLK FIGTRPTYDQ SKFQHVPISK GSLILIHGLV
VHKSEANTSD KSRHAYTIHV MEKQNTEWSK DNWLQETEQY KFPNLYKQ