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A7FM22 (PANB_YERP3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:YpsIP31758_3343
OrganismYersinia pseudotuberculosis serotype O:1b (strain IP 31758) [Complete proteome] [HAMAP]
Taxonomic identifier349747 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Protein existenceInferred 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.

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.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00156.

Sequence similarities

Belongs to the PanB family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2652653-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP-Rule MF_00156
PRO_1000058187

Regions

Region45 – 462Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding451Magnesium By similarity
Metal binding841Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site841Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7FM22 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 3F3004286B15D99A

FASTA26528,695
        10         20         30         40         50         60 
MKTTTMSQLR QWKQEKRKFA TLTAYDASFA QLFAEQGIQV LLVGDSLGMT LQGFDSTLPV 

        70         80         90        100        110        120 
TVADVAYHTR AVRRGAPHCL LLADMPFMSY ATPELAFTHA AELMRAGANM VKLEGGSWLC 

       130        140        150        160        170        180 
DTIRMLAERA VPVCGHLGLT PQSVNIFGGY KVQGREEVAA NQLLQDAIVL EQAGAQLLVL 

       190        200        210        220        230        240 
ECVPVELAQR VTEELTIPVI GIGAGNVTDG QILVMHDALG ITGGHTPKFS KNFLAHSAGD 

       250        260 
IRAAIKLYIE EVEGGIYPAE EHTFQ 

« Hide

References

[1]"The complete genome sequence of Yersinia pseudotuberculosis IP31758, the causative agent of Far East scarlet-like fever."
Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., Fayolle C., Lindler L.E., Carniel E., Ravel J.
PLoS Genet. 3:1508-1523(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP 31758.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000720 Genomic DNA. Translation: ABS47724.1.
RefSeqYP_001402300.1. NC_009708.1.

3D structure databases

ProteinModelPortalA7FM22.
SMRA7FM22. Positions 4-265.
ModBaseSearch...

Protein-protein interaction databases

STRING349747.YpsIP31758_3343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS47724; ABS47724; YpsIP31758_3343.
GeneID5386444.
KEGGypi:YpsIP31758_3343.
PATRIC18635855. VBIYerPse15693_3836.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHOG000078427.
KOK00606.
OMAGINVLLV.
ProtClustDBPRK00311.

Enzyme and pathway databases

UniPathwayUPA00028; UER00003.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
HAMAPMF_00156. PanB.
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
PANTHERPTHR20881. PTHR20881. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR00222. panB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB_YERP3
AccessionPrimary (citable) accession number: A7FM22
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 11, 2007
Last modified: May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families