[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1006/bbrc.1998.9343; PubMed=9753662 [NCBI, ExPASy, EBI, Israel, Japan] Vaz F.M., van Gool S., Ofman R., Ijlst L., Wanders R.J.A.; "Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase."; Biochem. Biophys. Res. Commun. 250:506-510(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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: Iron.
COFACTOR: Ascorbate.
PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Highly expressed in kidney; moderately expressed in liver; very low expression in brain.
SIMILARITY: Belongs to the gamma-BBH/TMLD family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF082868; AAC64066.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456812; CAG33093.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011034; AAH11034.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JE0360; JE0360.

NP_003977.1; -.

3D structure databases

ModBase

O75936.

Protein-protein interaction databases

IntAct

O75936; 1.

PTM databases

PhosphoSite

O75936; -.

Enzyme and pathway databases

Reactome

REACT_13; Metabolism of amino acids.

Organism-specific databases

GC11P027019; -.

HIX0009515; -.

HGNC:964; BBOX1.

HPA007600; -.

603312; gene. [NCBI / EBI]

PharmGKB

PA25274; -.

GeneCards

O75936.

Gene expression databases

ArrayExpress

O75936; -.

CleanEx

HS_BBOX1; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008336;	Molecular function: gamma-butyrobetaine dioxygenase activity (inferred from direct assay from UniProtKB).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0045329;	Biological process: carnitine biosynthetic process (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR012775; 2-oxoglut_dOase.
IPR003819; Taurine_dOase.
Graphical view of domain structure.

Pfam

PF02668; TauD; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02409; carnitine_bodg; 1.

Proteomics databases

PRIDE

O75936; -.

Genome annotation databases

Ensembl

ENSG00000129151; Homo sapiens. [Contig view]

GeneID

8424; -.

KEGG

hsa:8424; -.

Phylogenomic databases

HOGENOM

O75936; -.

HOVERGEN

O75936; -.

Other

DrugBank

DB00139; Succinic acid.
DB00126; Vitamin C.

31520; -.

BBOX1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carnitine biosynthesis; Cytoplasm; Dioxygenase; Iron; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 387`	`387`		`Gamma-butyrobetaine dioxygenase.`	`PRO_0000207085`

Sequence information

Length: 387 AA [This is the length of the unprocessed precursor]

Molecular weight: 44715 Da [This is the MW of the unprocessed precursor]

CRC64: A3BA3F9FA9355DB3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MACTIQKAEA LDGAHLMQIL WYDEEESLYP AVWLRDNCPC SDCYLDSAKA RKLLVEALDV 

        70         80         90        100        110        120 
NIGIKGLIFD RKKVYITWPD EHYSEFQADW LKKRCFSKQA RAKLQRELFF PECQYWGSEL 

       130        140        150        160        170        180 
QLPTLDFEDV LRYDEHAYKW LSTLKKVGIV RLTGASDKPG EVSKLGKRMG FLYLTFYGHT 

       190        200        210        220        230        240 
WQVQDKIDAN NVAYTTGKLS FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK 

       250        260        270        280        290        300 
LKKNNPQAFQ ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRIN FNNATRDTIF 

       310        320        330        340        350        360 
DVPVERVQPF YAALKEFVDL MNSKESKFTF KMNPGDVITF DNWRLLHGRR SYEAGTEISR 

       370        380 
HLEGAYADWD VVMSRLRILR QRVENGN

O75936 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools