Q9QZU7 (BODG_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-butyrobetaine dioxygenase
EC=1.14.11.1

Alternative name(s):
Gamma-butyrobetaine hydroxylase
Short name=Gamma-BBH
Gamma-butyrobetaine,2-oxoglutarate dioxygenase

Gene names

Name:	Bbox1
Synonyms:	Bbh

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic activity	4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2.
Cofactor	Binds 1 Fe2+ ion per subunit By similarity. Ascorbate.
Pathway	Amine and polyamine biosynthesis; carnitine biosynthesis.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in the liver and in some extend in the testis and the epididymis.
Sequence similarities	Belongs to the gamma-BBH/TMLD family.

Ontologies

Keywords
Biological process	Carnitine biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding Zinc
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	carnitine biosynthetic process Inferred from sequence or structural similarity Ref.2. Source: UniProtKB
Molecular function	gamma-butyrobetaine dioxygenase activity Inferred from mutant phenotype Ref.1. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 387	387	Gamma-butyrobetaine dioxygenase		PRO_0000207087
Sites
	Metal binding	38	1	Zinc By similarity
	Metal binding	40	1	Zinc By similarity
	Metal binding	43	1	Zinc By similarity
	Metal binding	82	1	Zinc By similarity
	Metal binding	202	1	Iron; catalytic By similarity
	Metal binding	204	1	Iron; catalytic By similarity
	Metal binding	347	1	Iron; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9QZU7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 357804BFB35BF274	FASTA	387	44,546
	10 20 30 40 50 60 MHCAILKAEA VDGARLMQIF WHDGAESLYP AVWLRDNCQC SDCYLHSAKA RKLLLEALDV 70 80 90 100 110 120 NIRMDDLTFD QKKVYITWPN GHYSEFEANW LKKRCFSQEA RAGLQGELFL PECQYWGSEL 130 140 150 160 170 180 QLPTLNFEDV LNDDDHAYKW LSSLKKVGIV RLTGAADKRG EIIKLGKRIG FLYLTFYGHT 190 200 210 220 230 240 WQVQDKIDAN NVAYTTGKLS FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK 250 260 270 280 290 300 LKEKNPQAFS ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRIN FNNATRDTVF 310 320 330 340 350 360 DVPIERVQPF YAALKEFVDL MNSKEYKYTF KMNPGDVITF DNWRLLHGRR SYEAGTEISR 370 380 HLEGAYADWD VVMSRLRILR QRVMNGN

References

[1]	"Molecular cloning and characterization of the cDNA encoding the rat liver gamma-butyrobetaine hydroxylase." Galland S., Le Borgne F., Bouchard F., Georges B., Clouet P., Grand-Jean F., Demarquoy J. Biochim. Biophys. Acta 1441:85-92(1999) [PubMed: 10526231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase." Vaz F.M., van Gool S., Ofman R., Ijlst L., Wanders R.J.A. Biochem. Biophys. Res. Commun. 250:506-510(1998) [PubMed: 9753662] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF160958 mRNA. Translation: AAD53264.1.
IPI	IPI00215321.
RefSeq	NP_072151.1. NM_022629.1.
UniGene	Rn.16333.
3D structure databases
ProteinModelPortal	Q9QZU7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QZU7.
PTM databases
PhosphoSite	Q9QZU7.
Proteomic databases
PRIDE	Q9QZU7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000006197; ENSRNOP00000006197; ENSRNOG00000004536.
GeneID	64564.
KEGG	rno:64564.
Organism-specific databases
CTD	8424.
RGD	619756. Bbox1.
Phylogenomic databases
eggNOG	roNOG11179.
GeneTree	ENSGT00530000063582.
HOVERGEN	HBG031125.
InParanoid	Q9QZU7.
OMA	IQKAEVL.
OrthoDB	EOG4SXNCM.
PhylomeDB	Q9QZU7.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14431.
Gene expression databases
ArrayExpress	Q9QZU7.
Genevestigator	Q9QZU7.
GermOnline	ENSRNOG00000004536. Rattus norvegicus.
Family and domain databases
InterPro	IPR012775. 2-oxoglut_dOase. IPR010376. DUF971. IPR003819. Taurine_dOase. [Graphical view]
KO	K00471.
Pfam	PF06155. DUF971. 1 hit. PF02668. TauD. 1 hit. [Graphical view]
TIGRFAMs	TIGR02409. Carnitine_bodg. 1 hit.
ProtoNet	Search...
Other
NextBio	613498.

Entry information

Entry name

BODG_RAT

Accession

Primary (citable) accession number: Q9QZU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	May 1, 2000
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program