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Q1I4P2 (PANB2_PSEE4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:PSEEN4735
OrganismPseudomonas entomophila (strain L48) [Complete proteome] [HAMAP]
Taxonomic identifier384676 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length266 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 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 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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2662663-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156
PRO_0000297336

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
Q1I4P2 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: FD24D0EC04089EC4

FASTA26627,752
        10         20         30         40         50         60 
MPEVTLTTLN GLKAKGEKIT MLTCYDATFA KAASEAGVEV LLVGDSLGMV LQGHDSTLPV 

        70         80         90        100        110        120 
SNDDMAYHTA SVKRGNNGAL ILTDLPFMAH ATPELAFTNA AQLMRAGAHM VKIEGAAWLA 

       130        140        150        160        170        180 
ETIRLLAERG VPVCAHMGLT PQTVNVLGGY KVQGRQEAQA RQMRADAIAL EQAGAAMLLL 

       190        200        210        220        230        240 
ECVPSELAAE ITQAVGIPVI GIGAGSATDG QVLVLHDMLG LSLSGRVPKF VKNFMAGQPD 

       250        260 
IQSALAAYVE AVKTVSFPAS EHGFSA 

« Hide

References

[1]"Complete genome sequence of the entomopathogenic and metabolically versatile soil bacterium Pseudomonas entomophila."
Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P., Weissenbach J., Lemaitre B., Medigue C., Boccard F.
Nat. Biotechnol. 24:673-679(2006) [PubMed: 16699499] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L48.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT573326 Genomic DNA. Translation: CAK17394.1.
RefSeqYP_610177.1. NC_008027.1.

3D structure databases

ProteinModelPortalQ1I4P2.
SMRQ1I4P2. Positions 4-265.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1I4P2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4085991.
GenomeReviewsGene locus PSEEN4735 in contig CT573326_GR.
KEGGpen:PSEEN4735.
NMPDRfig|384676.6.peg.4077.
PATRIC19867484. VBIPseEnt83862_4539.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYDATFAH.
PhylomeDBQ1I4P2.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycPENT384676:PSEEN4735-MONOMER.

Family and domain databases

HAMAPMF_00156. PanB.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK00606.
PANTHERPTHR20881. Pantoate_transf. 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 namePANB2_PSEE4
AccessionPrimary (citable) accession number: Q1I4P2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 13, 2006
Last modified: January 25, 2012
This is version 42 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