Reviewed, UniProtKB/Swiss-Prot Q81ST3 (PANB_BACAN)

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:	BA_1562, GBAA_1562, BAS1449

Organism

Bacillus anthracis [Complete proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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.
Subcellular location	Cytoplasm Potential.
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_0000184808
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)
	Q81ST3-1 [UniParc]. Last modified June 1, 2003. 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]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016879 Genomic DNA. Translation: AAP25498.1. AE017334 Genomic DNA. Translation: AAT30659.2. AE017225 Genomic DNA. Translation: AAT53769.1.
RefSeq	NP_844012.1. YP_018184.2. YP_027718.1.
3D structure databases
HSSP	HSSP built from PDB template 1OY0 based on UniProtKB Q10505.
ModBase	Search...
Genome annotation databases
GeneID	1084235. 2815634. 2850864.
GenomeReviews	Gene locus BA_1562 in contig AE016879_GR. Gene locus BAS1449 in contig AE017225_GR. Gene locus GBAA_1562 in contig AE017334_GR.
KEGG	ban:BA1562. bar:GBAA1562. bat:BAS1449.
TIGR	BA_1562. GBAA_1562.
Phylogenomic databases
HOGENOM	Q81ST3.
OMA	YATPEQT.
Enzyme and pathway databases
BioCyc	BANT260799:BAS1449-MON. BANT261594:GBAA1562-MON.
BRENDA	2.1.2.11. 267517.
Family and domain databases
HAMAP	MF_00156. [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_BACAN

Accession

Primary (citable) accession number: Q81ST3
Secondary accession number(s): Q6I113, Q6KUW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 46 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)