BODG_RAT
ID BODG_RAT Reviewed; 387 AA.
AC Q9QZU7;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Gamma-butyrobetaine dioxygenase;
DE EC=1.14.11.1;
DE AltName: Full=Gamma-butyrobetaine hydroxylase {ECO:0000303|PubMed:10526231};
DE Short=Gamma-BBH;
DE AltName: Full=Gamma-butyrobetaine,2-oxoglutarate dioxygenase;
GN Name=Bbox1; Synonyms=Bbh {ECO:0000303|PubMed:10526231};
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 [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10526231; DOI=10.1016/s1388-1981(99)00135-3;
RA Galland S., Le Borgne F., Bouchard F., Georges B., Clouet P.,
RA Grand-Jean F., Demarquoy J.;
RT "Molecular cloning and characterization of the cDNA encoding the rat liver
RT gamma-butyrobetaine hydroxylase.";
RL Biochim. Biophys. Acta 1441:85-92(1999).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=9753662; DOI=10.1006/bbrc.1998.9343;
RA Vaz F.M., van Gool S., Ofman R., Ijlst L., Wanders R.J.A.;
RT "Carnitine biosynthesis: identification of the cDNA encoding human gamma-
RT butyrobetaine hydroxylase.";
RL Biochem. Biophys. Res. Commun. 250:506-510(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the formation of L-carnitine from gamma-
CC butyrobetaine.
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;
CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in the liver and in some extend in the
CC testis and the epididymis. {ECO:0000269|PubMed:10526231}.
CC -!- DEVELOPMENTAL STAGE: Undetectable during the perinatal period. During
CC development, expression appears after the weaning of the young rat and
CC reaches a maximal expression at the adult stage.
CC {ECO:0000269|PubMed:10526231}.
CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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DR EMBL; AF160958; AAD53264.1; -; mRNA.
DR RefSeq; NP_072151.1; NM_022629.1.
DR RefSeq; XP_017447515.1; XM_017592026.1.
DR AlphaFoldDB; Q9QZU7; -.
DR SMR; Q9QZU7; -.
DR STRING; 10116.ENSRNOP00000006197; -.
DR iPTMnet; Q9QZU7; -.
DR PhosphoSitePlus; Q9QZU7; -.
DR PaxDb; Q9QZU7; -.
DR PRIDE; Q9QZU7; -.
DR Ensembl; ENSRNOT00000080175; ENSRNOP00000073497; ENSRNOG00000059519.
DR GeneID; 64564; -.
DR KEGG; rno:64564; -.
DR UCSC; RGD:619756; rat.
DR CTD; 8424; -.
DR RGD; 619756; Bbox1.
DR eggNOG; KOG3888; Eukaryota.
DR GeneTree; ENSGT00530000063582; -.
DR InParanoid; Q9QZU7; -.
DR OrthoDB; 868657at2759; -.
DR PhylomeDB; Q9QZU7; -.
DR TreeFam; TF313805; -.
DR BioCyc; MetaCyc:MON-14431; -.
DR BRENDA; 1.14.11.1; 5301.
DR Reactome; R-RNO-71262; Carnitine synthesis.
DR SABIO-RK; Q9QZU7; -.
DR UniPathway; UPA00118; -.
DR PRO; PR:Q9QZU7; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008336; F:gamma-butyrobetaine dioxygenase activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 1: Evidence at protein level;
KW Carnitine biosynthesis; Cytoplasm; Dioxygenase; Direct protein sequencing;
KW Iron; Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..387
FT /note="Gamma-butyrobetaine dioxygenase"
FT /id="PRO_0000207087"
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:0007744|PubMed:22673903"
SQ SEQUENCE 387 AA; 44546 MW; 357804BFB35BF274 CRC64;
MHCAILKAEA VDGARLMQIF WHDGAESLYP AVWLRDNCQC SDCYLHSAKA RKLLLEALDV
NIRMDDLTFD QKKVYITWPN GHYSEFEANW LKKRCFSQEA RAGLQGELFL PECQYWGSEL
QLPTLNFEDV LNDDDHAYKW LSSLKKVGIV RLTGAADKRG EIIKLGKRIG FLYLTFYGHT
WQVQDKIDAN NVAYTTGKLS FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK
LKEKNPQAFS ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRIN FNNATRDTVF
DVPIERVQPF YAALKEFVDL MNSKEYKYTF KMNPGDVITF DNWRLLHGRR SYEAGTEISR
HLEGAYADWD VVMSRLRILR QRVMNGN
