Q8X929 (PANB_ECO57) 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:	Z0145, ECs0138

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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_0000184843
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)
	Q8X929 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: D93FF23EBEF8D090	FASTA	264	28,310
	10 20 30 40 50 60 MKPTTIASLQ KCKQEKKRFA TITAYDYSFA KLFAEEGLNV MLVGDSLGMT VQGHESTLPV 70 80 90 100 110 120 TVEDIAYHTT AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV 130 140 150 160 170 180 ETVKMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAS DRLLSDALAL EAAGAQLLVL 190 200 210 220 230 240 ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI 250 260 RAAVRQYMAE VESGVYPGEE HSFH

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG54438.1. BA000007 Genomic DNA. Translation: BAB33561.1.
PIR	B85497. B90646.
RefSeq	NP_285830.1. NC_002655.2. NP_308165.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X929.
SMR	Q8X929. Positions 3-264.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z0145.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG54438; AAG54438; Z0145. BAB33561; BAB33561; BAB33561.
GeneID	913736. 956841.
KEGG	ece:Z0145. ecs:ECs0138.
PATRIC	18349218. VBIEscCol44059_0139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HOG000078427.
KO	K00606.
OMA	CYDASFA.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-135-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_ECO57

Accession

Primary (citable) accession number: Q8X929

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	March 1, 2002
Last modified:	May 29, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program