Q9AMS0 (PANB2_BRAJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Ketopantoate hydroxymethyltransferase 2
Short name=KPHMT 2

Gene names

Name:	panB2
Ordered Locus Names:	blr2101
ORF Names:	id910

Organism

Bradyrhizobium japonicum

Taxonomic identifier

375 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length	292 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.
Sequence caution	The sequence AAG61077.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC47366.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference 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 – 292	292	3-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156		PRO_0000184824
Regions
	Region	52 – 53	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	189	1	Proton acceptor By similarity
	Metal binding	52	1	Magnesium By similarity
	Metal binding	91	1	Magnesium By similarity
	Metal binding	122	1	Magnesium By similarity
	Binding site	91	1	Alpha-ketoisovalerate By similarity
	Binding site	120	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9AMS0 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 439C07685557F503	FASTA	292	31,515
	10 20 30 40 50 60 MSHSSEQPLE RVTIPALQQW KDKGRRVVMT TAYDAVAARI ADPIVDIILV GDSVGNVCLG 70 80 90 100 110 120 FDNTLPVSVA MMNHHLEAVA RTRPHALLVA DMPFLSFHVG SEDTIRNAGG FLQRGADAVK 130 140 150 160 170 180 LEGGAKRIEM VRALVDCDIP VMGHLGLTPQ SVNVMGGFKV QGRTTDTALR LLDDAHRLQE 190 200 210 220 230 240 AGCFALVLEG IPAELAARAT ESLTIPTIGI GAGADCSGQV LVFHDVLGLT EGHRPKFVRA 250 260 270 280 290 YTNGFQLFQE ALSRWAADIR KGAFPGSEEC YRLPDQLRHA VANWVPSSST SR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA region of the Bradyrhizobium japonicum chromosome." Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R., Hennecke H. J. Bacteriol. 183:1405-1412(2001) [PubMed: 11157954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: USDA 110spc4.
[2]	"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USDA 110.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF322013 Genomic DNA. Translation: AAG61077.1. Different initiation. BA000040 Genomic DNA. Translation: BAC47366.1. Different initiation.
RefSeq	NP_768741.1. NC_004463.1.
3D structure databases
ProteinModelPortal	Q9AMS0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1055446.
GenomeReviews	Gene locus blr2101 in contig BA000040_GR.
KEGG	bja:blr2101.
NMPDR	fig|224911.1.peg.2101.
Phylogenomic databases
HOGENOM	HBG299908.
OMA	SCAAAVK.
PhylomeDB	Q9AMS0.
ProtClustDB	CLSK254121.
Enzyme and pathway databases
BioCyc	BJAP224911:BLR2101-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

PANB2_BRAJA

Accession

Primary (citable) accession number: Q9AMS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2004
Last modified:	November 16, 2011
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program