PHYD1_CAEEL
ID PHYD1_CAEEL Reviewed; 288 AA.
AC Q9NAM7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phytanoyl-CoA dioxygenase domain-containing protein 1 homolog;
DE EC=1.-.-.-;
GN ORFNames=Y105C5B.9;
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: 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; AL110479; CAB54355.1; -; Genomic_DNA.
DR PIR; T26383; T26383.
DR RefSeq; NP_502898.1; NM_070497.1.
DR AlphaFoldDB; Q9NAM7; -.
DR SMR; Q9NAM7; -.
DR BioGRID; 43523; 2.
DR STRING; 6239.Y105C5B.9; -.
DR EPD; Q9NAM7; -.
DR PaxDb; Q9NAM7; -.
DR PeptideAtlas; Q9NAM7; -.
DR EnsemblMetazoa; Y105C5B.9.1; Y105C5B.9.1; WBGene00013650.
DR GeneID; 178445; -.
DR KEGG; cel:CELE_Y105C5B.9; -.
DR UCSC; Y105C5B.9; c. elegans.
DR CTD; 178445; -.
DR WormBase; Y105C5B.9; CE24085; WBGene00013650; -.
DR eggNOG; KOG3290; Eukaryota.
DR GeneTree; ENSGT00390000006287; -.
DR HOGENOM; CLU_048953_0_0_1; -.
DR InParanoid; Q9NAM7; -.
DR OMA; KYSEDNW; -.
DR OrthoDB; 1316775at2759; -.
DR PhylomeDB; Q9NAM7; -.
DR PRO; PR:Q9NAM7; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00013650; Expressed in embryo and 3 other tissues.
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_0000313638"
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; 33020 MW; 2AEBCE889408AAC7 CRC64;
MWDLREKFER DGFVVVENVF NDQEIDEMKK SISKIVNDMD LAEHPKSVFS TYDEDKHAAD
SYFLNSSDKI RFFFEEGAVD KDGELTVPKD KALNKIGHGL HFLDPTFEKM TFNSKIQNIF
KEIGYQEPGV VQSMYIFKQP KIGGAVTDHV DSTFLRVDPI DHLTGVWIAI DEASVENGCL
SFIPGSHKDT SSANYRFVRT HDTSGGALLK FIGTRPTYDQ SKFQHVPISK GSLILIHGLV
VHKSEANTSE KSRHAYTIHV MERKNTKWSE QNWLQETENY KFPDLYKD