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Reviewed, UniProtKB/Swiss-Prot A1WBI7 (PANB_ACISJ)

Last modified November 3, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Ajs_3499
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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.

Subcellular location

Cytoplasm Potential.

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

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2932933-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297207

Regions

Region67 – 682Alpha-ketoisovalerate binding By similarity

Sites

Active site2081Proton acceptor By similarity
Metal binding671Magnesium By similarity
Metal binding1101Magnesium By similarity
Metal binding1411Magnesium By similarity
Binding site1101Alpha-ketoisovalerate By similarity
Binding site1391Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WBI7-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 7E8EC06100334083

FASTA29331,009
        10         20         30         40         50         60 
MTDSPTAGTP YGTLPPASPL PQRRPVSLPR LAQMREAGEK ITMLTAYDAT FAAVADAAGV 

        70         80         90        100        110        120 
ECILVGDSLG MVCQGLPSTV GVTLEHMAYH TASVARGLHR VQGTAWLIAD LPYGSYAESR 

       130        140        150        160        170        180 
EQALRSACQL MQAGAHMVKL EGGGWTAPTV QFLVERGVPV CAHLGLTPQT VHALGGYRVQ 

       190        200        210        220        230        240 
GKGDQAAQQL RRQALELQDA GAAMLVLEMV PTPLARDLTQ ALPRCHTIGI GAGSGTAGQV 

       250        260        270        280        290 
LVMHDMLGIN LGKNPKFVHD FMRDAGSVRG AIEAYVQAVK QGRFPDDALH AWN 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000539 Genomic DNA. Translation: ABM43612.1.
RefSeqYP_987688.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1WBI7.

Genome annotation databases

GeneID4672727.
GenomeReviewsGene locus Ajs_3499 in contig CP000539_GR.
KEGGajs:Ajs_3499.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYATPEQT.

Family and domain databases

HAMAPMF_00156.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PANTHERPTHR20881. Pantoate_transf. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
TIGRFAMsTIGR00222. panB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB_ACISJ
AccessionPrimary (citable) accession number: A1WBI7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents