Q65I56 (PANB_BACLD) 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:	BLi02378, BL02752

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	277 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 – 277	277	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297220
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)
	Q65I56 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 19587BBB94815AB7	FASTA	277	29,519
	10 20 30 40 50 60 MKTKTDFLKM KQEGEPIVML TAYDYPAAKL AEQAGVDMIL VGDSLGMVVL GLDSTVSVTV 70 80 90 100 110 120 ADMIHHTKAV KRGAKDTFVV TDMPFMSYHC SLESALKNAA AIVQESGADA LKLEGGDGVF 130 140 150 160 170 180 ETITALTRGG IPVVSHLGLT PQSVGVLGGY KVQGKDEESA GKLIEDSRRC EEAGAMALVL 190 200 210 220 230 240 ECVPAALAER ISKELTIPVI GIGAGAGTDG QVLVYHDVVG HGVSRTPKFV KQYAQIDQPL 250 260 270 EQALRGYVED VRSRVFPEDA HSFRIDQQVL EGLYGGK

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU23904.1. AE017333 Genomic DNA. Translation: AAU41258.1.
RefSeq	YP_079542.1. NC_006270.3. YP_091951.1. NC_006322.1.
3D structure databases
HSSP	HSSP built from PDB template 1M3U based on UniProtKB P31057.
ProteinModelPortal	Q65I56.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65I56.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000056450; EBBACP00000054981; EBBACG00000056441. EBBACT00000062437; EBBACP00000060870; EBBACG00000062428.
GeneID	3027472. 3100431.
GenomeReviews	Gene locus BLi02378 in contig AE017333_GR. Gene locus BL02752 in contig CP000002_GR.
KEGG	bld:BLi02378. bli:BL02752.
NMPDR	fig|279010.5.peg.228.
PATRIC	18950414. VBIBacLic203714_2409.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
GeneTree	EBGT00050000000505.
HOGENOM	HBG299908.
OMA	YDATFAH.
PhylomeDB	Q65I56.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI02378-MONOMER. BLIC279010:BL02752-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_BACLD

Accession

Primary (citable) accession number: Q65I56
Secondary accession number(s): Q62TK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program