A7GN76 (PANB_BACCN) 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:	Bcer98_1262

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	279 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 – 279	279	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_1000076815
Regions
	Region	43 – 44	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	181	1	Proton acceptor By similarity
	Metal binding	43	1	Magnesium By similarity
	Metal binding	82	1	Magnesium By similarity
	Metal binding	114	1	Magnesium By similarity
	Binding site	82	1	Alpha-ketoisovalerate By similarity
	Binding site	112	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GN76 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 8535BCB00EA0F8AD	FASTA	279	30,463
	10 20 30 40 50 60 MKTKTDFLRM KQKGEPITML TAYDYPSAKL VEEAEVDMIL VGDSLGMVVL GYDSTVPVTV 70 80 90 100 110 120 EDMIHHTKAV RRGAKDTFVV TDMPFMSYHV SLAETMHHAR RIVQEGGAHA LKVEGAGEVI 130 140 150 160 170 180 STIHYLTNAG IPVVAHLGLT PQSVGILGGY KVQGKDAESA KQLIADAKKC EDAGAIALVL 190 200 210 220 230 240 ECVPMQLAKI ISDELTIPTI GIGAGKDVDG QVLVYHDLIS YGVNRVPKFV KQYTAVQDEI 250 260 270 VRGISQYVAE VKTRQFPEDQ YSFTMKEEEY VALYGGKQG

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000764 Genomic DNA. Translation: ABS21584.1.
RefSeq	YP_001374579.1. NC_009674.1.
3D structure databases
ProteinModelPortal	A7GN76.
ModBase	Search...
Protein-protein interaction databases
STRING	A7GN76.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000038497; EBBACP00000037548; EBBACG00000038488.
GeneID	5346020.
GenomeReviews	Gene locus Bcer98_1262 in contig CP000764_GR.
KEGG	bcy:Bcer98_1262.
PATRIC	18930978. VBIBacCyt128034_1333.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
GeneTree	EBGT00050000000505.
HOGENOM	HBG299908.
OMA	YDATFAH.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	BCER315749:BCER98_1262-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_BACCN

Accession

Primary (citable) accession number: A7GN76

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 11, 2007
Last modified:	December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program