A7ZHM4 (PANB_ECO24) 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:	EcE24377A_0137

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	264 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-Rule MF_00156
Catalytic activity	5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP-Rule MF_00156
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00156
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP-Rule MF_00156
Subunit structure	Homodecamer; pentamer of dimers By similarity. HAMAP-Rule MF_00156
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00156.
Sequence similarities	Belongs to the PanB family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	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 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 – 264	264	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP-Rule MF_00156		PRO_1000058182
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)
	A7ZHM4 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 0EB08E5780F74B5D	FASTA	264	28,179
	10 20 30 40 50 60 MKPTTIASLQ KCKQDKKRFA TITAYDYSFA KLFADEGLNV MLVGDSLGMT VQGHDSTLPV 70 80 90 100 110 120 TVEDIAYHTA AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV 130 140 150 160 170 180 ETVKMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAG DQLLSDALAL EAAGAQLLVL 190 200 210 220 230 240 ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI 250 260 RAAVRQYMAE VESGVYPGEE HSFH

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E24377A / ETEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000800 Genomic DNA. Translation: ABV20645.1.
RefSeq	YP_001461303.1. NC_009801.1.
3D structure databases
ProteinModelPortal	A7ZHM4.
SMR	A7ZHM4. Positions 3-264.
ModBase	Search...
Protein-protein interaction databases
STRING	331111.EcE24377A_0137.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV20645; ABV20645; EcE24377A_0137.
GeneID	5590338.
KEGG	ecw:EcE24377A_0137.
PATRIC	18289553. VBIEscCol31211_0467.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HOG000078427.
KO	K00606.
OMA	CYDASFA.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	ECOL331111:GH7P-136-MONOMER.
UniPathway	UPA00028; UER00003.
Family and domain databases
Gene3D	3.20.20.60. 1 hit.
HAMAP	MF_00156. PanB.
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. [Graphical view]
PANTHER	PTHR20881. PTHR20881. 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_ECO24

Accession

Primary (citable) accession number: A7ZHM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	May 29, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program