Reviewed, UniProtKB/Swiss-Prot Q6HL16 (PANB_BACHK)

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:	BT9727_1421

Organism

Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]

Taxonomic identifier

180856 [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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding 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_0000184814
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)
	Q6HL16-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: BC891820D7C0D1D6	FASTA	279	30,535
	10 20 30 40 50 60 MKTKTDFLKM KEQGEPITML TAYDYPSAKL AEEAEVDMIL VGDSLGMVVL GYDSTVPVTV 70 80 90 100 110 120 EDMIHHTKAV RRGAKETFIV TDMPFMSYHV SLQDTMVNAR RIVQESGAHA LKVEGAGEVI 130 140 150 160 170 180 STIHYLTNAG IPVVAHLGLT PQSVGVLGGY KVQGKDAESA KKLIEDAKKC EEAGAIALVL 190 200 210 220 230 240 ECVPMQLAEL ISEQLTIPTI GIGAGQKVDG QVLVYHDLIS YGVNRVPKFV KQYTSVQEEI 250 260 270 VRGISQYVAE VKTRQFPEEK HSFTMKEEEC LALYGGKQS

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT59464.1.
RefSeq	YP_035755.1.
3D structure databases
SMR	Q6HL16. Positions 3-264.
ModBase	Search...
Genome annotation databases
GeneID	2855218.
GenomeReviews	Gene locus BT9727_1421 in contig AE017355_GR.
KEGG	btk:BT9727_1421.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299908.
OMA	YATPEQT.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_1421-MONOMER.
Family and domain databases
HAMAP	MF_00156. PanB. [Tree]
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PANTHER	PTHR20881. Pantoate_transf. 1 hit.
Pfam	PF02548. Pantoate_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
TIGRFAMs	TIGR00222. panB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANB_BACHK

Accession

Primary (citable) accession number: Q6HL16

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 36 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)