BODG_PONAB
ID BODG_PONAB Reviewed; 387 AA.
AC Q5R5D8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Gamma-butyrobetaine dioxygenase;
DE EC=1.14.11.1;
DE AltName: Full=Gamma-butyrobetaine hydroxylase;
DE Short=Gamma-BBH;
DE AltName: Full=Gamma-butyrobetaine,2-oxoglutarate dioxygenase;
GN Name=BBOX1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of L-carnitine from gamma-
CC butyrobetaine. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine
CC + CO2 + succinate; Xref=Rhea:RHEA:24028, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16244, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17126, ChEBI:CHEBI:30031; EC=1.14.11.1;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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DR EMBL; CR860924; CAH93028.1; -; mRNA.
DR RefSeq; NP_001126790.1; NM_001133318.1.
DR AlphaFoldDB; Q5R5D8; -.
DR SMR; Q5R5D8; -.
DR STRING; 9601.ENSPPYP00000003911; -.
DR GeneID; 100173794; -.
DR KEGG; pon:100173794; -.
DR CTD; 8424; -.
DR eggNOG; KOG3888; Eukaryota.
DR InParanoid; Q5R5D8; -.
DR OrthoDB; 868657at2759; -.
DR UniPathway; UPA00118; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008336; F:gamma-butyrobetaine dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0045329; P:carnitine biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.30.2020.30; -; 1.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR012775; GBBH.
DR InterPro; IPR010376; GBBH-like_N.
DR InterPro; IPR038492; GBBH-like_N_sf.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF06155; GBBH-like_N; 1.
DR Pfam; PF02668; TauD; 1.
DR TIGRFAMs; TIGR02409; carnitine_bodg; 1.
PE 2: Evidence at transcript level;
KW Carnitine biosynthesis; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..387
FT /note="Gamma-butyrobetaine dioxygenase"
FT /id="PRO_0000260155"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZU7"
SQ SEQUENCE 387 AA; 44660 MW; 348C64E21A8BB0D5 CRC64;
MACTIQKAEA LDGARLMQIL WYDEEESLYP AVWLRDNCPC SDCYLDSAKA RKLLAEALDV
NIGIKGLTFD RKKVYITWPD EHYSEFQADW LKKRCLSKQA RAKLQRELFF PECQYWGSEL
QLPTLDFEDV LRYDEHAYKW LSTLKKVGIV RLTGASDKPG EVSKLGKRMG FLYLTFYGHT
WQVQDKIDAN NVAYTTGKLS FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK
LKKNNPQAFQ ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRIN FNNATRDTIF
DVPVERVQPF YAALKEFVDL MNSKESKFTF KMNPGDVITF DNWRLLHGRR SYEAGTEISR
HLEGAYADWD VVMSRLRILR QRVENGN
