ID   PHYD1_RAT               Reviewed;         291 AA.
AC   Q5BJP9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phytanoyl-CoA dioxygenase domain-containing protein 1 {ECO:0000250|UniProtKB:Q5SRE7};
DE            Short=Protein PHYHD1 {ECO:0000250|UniProtKB:Q5SRE7};
DE            EC=1.14.11.- {ECO:0000250|UniProtKB:Q5SRE7};
GN   Name=Phyhd1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: 2-oxoglutarate(2OG)-dependent dioxygenase that catalyzes the
CC       conversion of 2-oxoglutarate to succinate and CO(2) in an iron-
CC       dependent manner. However, does not couple 2OG turnover to the
CC       hydroxylation of acyl-coenzyme A derivatives, implying that it is not
CC       directly involved in phytanoyl coenzyme-A metabolism. Does not show
CC       detectable activity towards fatty acid CoA thioesters.
CC       {ECO:0000250|UniProtKB:Q5SRE7}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q5SRE7};
CC   -!- SIMILARITY: Belongs to the PhyH family. PHYHD1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC091389; AAH91389.1; -; mRNA.
DR   RefSeq; NP_001013099.1; NM_001013081.1.
DR   RefSeq; XP_006233841.1; XM_006233779.2.
DR   RefSeq; XP_006233842.1; XM_006233780.3.
DR   RefSeq; XP_017447138.1; XM_017591649.1.
DR   AlphaFoldDB; Q5BJP9; -.
DR   SMR; Q5BJP9; -.
DR   STRING; 10116.ENSRNOP00000022552; -.
DR   iPTMnet; Q5BJP9; -.
DR   PhosphoSitePlus; Q5BJP9; -.
DR   PaxDb; Q5BJP9; -.
DR   PRIDE; Q5BJP9; -.
DR   GeneID; 296621; -.
DR   KEGG; rno:296621; -.
DR   UCSC; RGD:1310377; rat.
DR   CTD; 254295; -.
DR   RGD; 1310377; Phyhd1.
DR   VEuPathDB; HostDB:ENSRNOG00000016794; -.
DR   eggNOG; KOG3290; Eukaryota.
DR   HOGENOM; CLU_048953_0_0_1; -.
DR   InParanoid; Q5BJP9; -.
DR   OMA; KYSEDNW; -.
DR   OrthoDB; 1316775at2759; -.
DR   PhylomeDB; Q5BJP9; -.
DR   PRO; PR:Q5BJP9; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000016794; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; Q5BJP9; RN.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..291
FT                   /note="Phytanoyl-CoA dioxygenase domain-containing protein
FT                   1"
FT                   /id="PRO_0000313635"
FT   BINDING         102
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         141
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         156..158
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         156
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         158
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         174
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         248
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         257
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   MOD_RES         55
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SRE7"
SQ   SEQUENCE   291 AA;  32553 MW;  B94CF3D88BF696D4 CRC64;
     MACLSPSQLK KFQEDGFLLL EGFFTADECV VMQQRIGEIV AEMDVPLHCR TEFSTQEDEQ
     LQTQGNTDYF LSSGDKIRFF FEKGVFDEKG NFLVPPEKSI NKIGHALHAH DPVFRSITHS
     PKVQALVRSL GLQIPVVVQS MYIFKQPHFG GEVSPHQDAT FLYTEPLGRV LGLWIATEDA
     MLENGCLWFI PGSHTSGVSR RMIRAPSDSG PGTSFLGSEP AWDNNLFVPL PVRRGGLVLI
     HGEVVHKSEQ NLSDHSRQAY TFHLMEAAGT VWSPGNWLQP TTELPFPPLY I