ID   PHYD1_BOVIN             Reviewed;         291 AA.
AC   Q0IIB1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; BC122727; AAI22728.1; -; mRNA.
DR   RefSeq; NP_001069711.1; NM_001076243.1.
DR   AlphaFoldDB; Q0IIB1; -.
DR   SMR; Q0IIB1; -.
DR   STRING; 9913.ENSBTAP00000048693; -.
DR   PaxDb; Q0IIB1; -.
DR   PRIDE; Q0IIB1; -.
DR   GeneID; 540828; -.
DR   KEGG; bta:540828; -.
DR   CTD; 254295; -.
DR   eggNOG; KOG3290; Eukaryota.
DR   InParanoid; Q0IIB1; -.
DR   OrthoDB; 1316775at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   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_0000313632"
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;  32539 MW;  98EBA60D42D89487 CRC64;
     MACLSPSQLQ KFQEDGFLVL EGFLSADECE AMQRRIDEIV AKMDVPLHCR TEFSTQEEEQ
     LRAQGSTDYF LSSGDKIRFF FEKGVFDKQG NFLVPPEKSI NKIGHALHAL DPIFRCVTHS
     HKVQALARSL GLQMPVVVQS MYIFKQPHFG GEVAPHQDAS FLYTEPLGRV LGLWIALEDA
     MLENGCLWFI PGSHTGGVSR RMVRTPAGSV PGTSFLGSEP IRDNSLFVPT PVLRGALVLI
     HGEVVHKSEQ NLSDRSRQAY TFHLMEAAGT IWSPDNWLQP TPELPFPPLY T