BODG_MOUSE
ID BODG_MOUSE Reviewed; 387 AA.
AC Q924Y0;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N;
RA Vaz F.M., Ofman R., Wanders R.J.A.;
RT "Identification of mouse gamma-butyrobetaine hydroxylase cDNA.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AY033514; AAK54388.1; -; mRNA.
DR EMBL; BC019406; AAH19406.1; -; mRNA.
DR CCDS; CCDS16510.1; -.
DR RefSeq; NP_569719.1; NM_130452.1.
DR RefSeq; XP_006498885.1; XM_006498822.3.
DR RefSeq; XP_006498886.1; XM_006498823.3.
DR AlphaFoldDB; Q924Y0; -.
DR SMR; Q924Y0; -.
DR BioGRID; 228345; 2.
DR STRING; 10090.ENSMUSP00000046302; -.
DR iPTMnet; Q924Y0; -.
DR PhosphoSitePlus; Q924Y0; -.
DR jPOST; Q924Y0; -.
DR MaxQB; Q924Y0; -.
DR PaxDb; Q924Y0; -.
DR PRIDE; Q924Y0; -.
DR ProteomicsDB; 273622; -.
DR Antibodypedia; 2001; 397 antibodies from 30 providers.
DR DNASU; 170442; -.
DR Ensembl; ENSMUST00000046233; ENSMUSP00000046302; ENSMUSG00000041660.
DR GeneID; 170442; -.
DR KEGG; mmu:170442; -.
DR UCSC; uc008lmu.1; mouse.
DR CTD; 8424; -.
DR MGI; MGI:1891372; Bbox1.
DR VEuPathDB; HostDB:ENSMUSG00000041660; -.
DR eggNOG; KOG3888; Eukaryota.
DR GeneTree; ENSGT00530000063582; -.
DR HOGENOM; CLU_021859_2_0_1; -.
DR InParanoid; Q924Y0; -.
DR OMA; SVNILHC; -.
DR OrthoDB; 868657at2759; -.
DR PhylomeDB; Q924Y0; -.
DR TreeFam; TF313805; -.
DR Reactome; R-MMU-71262; Carnitine synthesis.
DR UniPathway; UPA00118; -.
DR BioGRID-ORCS; 170442; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Bbox1; mouse.
DR PRO; PR:Q924Y0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q924Y0; protein.
DR Bgee; ENSMUSG00000041660; Expressed in vestibular membrane of cochlear duct and 104 other tissues.
DR ExpressionAtlas; Q924Y0; baseline and differential.
DR Genevisible; Q924Y0; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008336; F:gamma-butyrobetaine dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; Iron; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..387
FT /note="Gamma-butyrobetaine dioxygenase"
FT /id="PRO_0000207086"
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; 44699 MW; 9F17F5F9CAE052BE CRC64;
MHCAILKAEA VDGAHLMQIF WHDGAESLYP AVWLRDNCQC SDCYLHSAKA RKLLLEALDV
NIRIDDLTFD RKKVYITWPN DHYSEFEANW LKKRCFSQQA RARLQGELFL PECQYWGSEL
QLPTLNFEDV LNDDDHAYKW LSSLKKVGIV RLTGAADKRG EIIKLGKRIG FLYLTFYGHT
WQVQDKIDAN NVAYTTGKLS FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK
LKEKNPQAFH ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRVN FNNATRDTVF
DVPIERVQPF YAALKEFVDL MNSKEYKYTF KMNPGDVITF DNWRLLHGRR SYEAGTEISR
HLEGAYADWD VVMSRLRILR QRVTNGN
