Reviewed, UniProtKB/Swiss-Prot P80193 (BODG_PSESK)

Names and origin

Protein names	Recommended name:     Gamma-butyrobetaine dioxygenase     EC=1.14.11.1 Alternative name(s):     Gamma-butyrobetaine,2-oxoglutarate dioxygenase     Gamma-butyrobetaine hydroxylase       Short name=Gamma-BBH
Organism	Pseudomonas sp. (strain AK-1)
Taxonomic identifier	29440 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 + O(2) = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO(2).
Cofactor	Iron. Ascorbate.
Pathway	Amine and polyamine biosynthesis; carnitine biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the gamma-BBH/TMLD family.

Ontologies

Keywords
Biological process	Carnitine biosynthesis
Cellular component	Cytoplasm
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	gamma-butyrobetaine dioxygenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 383	383	Gamma-butyrobetaine dioxygenase		PRO_0000207089
Natural variations
	Natural variant	1	1	Missing in 50% of the chains.

Sequences

	Sequence		Length	Mass (Da)
	P80193-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 1A16205902C92DB9	FASTA	383	43,322
	10 20 30 40 50 60 NAIADYRTFP LISPLASAAS FASGVSVTWA DGRVSPFHNL WLRDNCPCGD CVYEVTREQV 70 80 90 100 110 120 FLVADVPEDI QVQAVTIGDD GRLVVQWDDG HASAYHPGWL RAHAYDAQSL AEREAARPHK 130 140 150 160 170 180 HRWMQGLSLP VYDHGAVMQD DDTLLEWLLA VRDVGLTQLH GVPTEPGALI PLAKRISFIR 190 200 210 220 230 240 ESNFGVLFDV RSKADADSNA YTAFNLPLHT DLPTRELQPG LQFLHCLVND ATGGNSTFVD 250 260 270 280 290 300 GFAIAEALRI EAPAAYRLLC ETPVEFRNKD RHSDYRCTAP VIALDSSGEV REIRLANFLR 310 320 330 340 350 360 APFQMDAQRM PDYYLAYRRF IQMTREPRFC FTRRLEAGQL WCFDNRRVLH ARDAFDPASG 370 380 DRHFQGCYVD RDELLSRILV LQR

References

[1]	"Gamma-butyrobetaine hydroxylase. Structural characterization of the Pseudomonas enzyme." Rueetschi U., Nordin I., Odelhoeg B., Joernvall H., Lindstedt S. Eur. J. Biochem. 213:1075-1080(1993) [PubMed: 8504802] [Abstract] Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-8461.
Family and domain databases
InterPro	IPR012775. 2-oxoglut_dOase. IPR003819. Taurine_dOase. [Graphical view]
Pfam	PF02668. TauD. 1 hit. [Graphical view]
TIGRFAMs	TIGR02409. carnitine_bodg. 1 hit.
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

BODG_PSESK

Accession

Primary (citable) accession number: P80193

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 4, 2008
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)