P57293 (PANB_BUCAI) 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:	BU197

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	263 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 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 – 263	263	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184828
Regions
	Region	45 – 46	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	181	1	Proton acceptor By similarity
	Metal binding	45	1	Magnesium By similarity
	Metal binding	84	1	Magnesium By similarity
	Metal binding	114	1	Magnesium By similarity
	Binding site	84	1	Alpha-ketoisovalerate By similarity
	Binding site	112	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57293 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 2FDA6D9D963B9098	FASTA	263	29,353
	10 20 30 40 50 60 MESITISQLK NWKINKKKFA AITAYDFSFS RLFSNCGIPV ILIGDSLGMT IQGHTSTLPV 70 80 90 100 110 120 KIEDIAYHTK AVRKGAPNTF LISDLPFMSY YDTKQALKNT AKIIRSGANM IKMEGGKWLI 130 140 150 160 170 180 EIIRELSNRL ILICGHIGLI PQSFHYLGGY KVQGRKENDA NKLIDEALLL EESGINMLIL 190 200 210 220 230 240 ECIPEKLAKK ITESLSIPVI GIGSGKNTDG QILVMHDLLG ITEGKTPSFT KNFLSESDSI 250 260 QKAIQKYIYE VEHSIYPSKK HSF

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12914.1.
RefSeq	NP_240028.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57293.
SMR	P57293. Positions 3-263.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002969; EBBUCP00000002745; EBBUCG00000002969.
GeneID	1109640.
GenomeReviews	Gene locus BU197 in contig BA000003_GR.
KEGG	buc:BU197.
PATRIC	21243912. VBIBucAph127364_0208.
Phylogenomic databases
GeneTree	EBGT00050000008082.
HOGENOM	HBG299908.
OMA	YDATFAH.
PhylomeDB	P57293.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	BSP107806:BU197-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_BUCAI

Accession

Primary (citable) accession number: P57293

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program