Q6G5H3 (PANB_BARHE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-methyl-2-oxobutanoate hydroxymethyltransferase
EC=2.1.2.11

Alternative name(s):
Ketopantoate hydroxymethyltransferase
Short name=KPHMT

Gene names

Name:	panB
Ordered Locus Names:	BH05130

Organism

Bartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]

Taxonomic identifier

283166 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate By similarity. HAMAP MF_00156
Catalytic activity	5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP MF_00156
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00156
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP MF_00156
Subunit structure	Homodecamer; pentamer of dimers By similarity. HAMAP MF_00156
Subcellular location	Cytoplasm Potential HAMAP MF_00156.
Sequence similarities	Belongs to the PanB family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methyltransferase activity 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 – 275	275	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184818
Regions
	Region	49 – 50	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	187	1	Proton acceptor By similarity
	Metal binding	49	1	Magnesium By similarity
	Metal binding	88	1	Magnesium By similarity
	Metal binding	120	1	Magnesium By similarity
	Binding site	88	1	Alpha-ketoisovalerate By similarity
	Binding site	118	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G5H3 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 3625E8828CE05BDE	FASTA	275	29,976
	10 20 30 40 50 60 MTIHKAVKRI TASEIRSRKG QEPIVSLTAY QAYSARIADP YCDLLLVGDS VGMVVHGFET 70 80 90 100 110 120 TLPVSLDMMI LHGQAVMRGS KRALVVVDMP FGSYEESPEQ AFSNASRILA ETGCSAVKLE 130 140 150 160 170 180 GGVYIAETID FLCKRGIPVM SHVGLTPQAV NRFGGFKTQG RNESNWQQIE ADAAAIEKAG 190 200 210 220 230 240 AFAVVVEGVV EPLAVKLTQM LSIPTIGIGA SSQCDGQILV MEDMLGYGTW VPKFVRRYGV 250 260 270 LEQEMEKAIK SYADDVKSRT FPSDEEIYKL KQKSG

References

[1]

"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX897699 Genomic DNA. Translation: CAF27321.1.
RefSeq	YP_033349.1. NC_005956.1.
3D structure databases
ProteinModelPortal	Q6G5H3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2864996.
GenomeReviews	Gene locus BH05130 in contig BX897699_GR.
KEGG	bhe:BH05130.
NMPDR	fig|283166.1.peg.477.
PATRIC	20544809. VBIBarHen29080_0557.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299908.
OMA	DPIVMLT.
PhylomeDB	Q6G5H3.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	BHEN283166:BH05130-MONOMER.
Family and domain databases
HAMAP	MF_00156. PanB. [Tree]
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KO	K00606.
PANTHER	PTHR20881. Pantoate_transf. 1 hit.
Pfam	PF02548. Pantoate_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR00222. PanB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANB_BARHE

Accession

Primary (citable) accession number: Q6G5H3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program