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Reviewed, UniProtKB/Swiss-Prot A0AXR0 (PANB2_BURCH)

Last modified November 3, 2009. Version 21. 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 2
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase 2
      Short name=KPHMT 2
Gene names
Name: panB2
Ordered Locus Names: Bcen2424_3447
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length284 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 – 2842843-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156
PRO_0000297230

Regions

Region49 – 502Alpha-ketoisovalerate binding By similarity

Sites

Active site1871Proton acceptor By similarity
Metal binding491Magnesium By similarity
Metal binding881Magnesium By similarity
Metal binding1201Magnesium By similarity
Binding site881Alpha-ketoisovalerate By similarity
Binding site1181Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0AXR0-1 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 1C27E26A77B57D16

FASTA28429,919
        10         20         30         40         50         60 
MSAHTRITRK TVTAIRSTKG IGSLVSLTAY SAPMAKLVDE VADVIIVGDS VGMVLYGMPD 

        70         80         90        100        110        120 
TLRVTLDMMI AHGAAVVRGA AQACVVVDLP FSTFQESPAQ AYRSAARLLA ETGAQAVKLE 

       130        140        150        160        170        180 
GGCEMTDTIR FLTDRGIPVM AHVGLMPQQA NAAGGFRAQG MDPRSAAQVF DAACAAERAG 

       190        200        210        220        230        240 
AFSVVIEGTA EALARHLTET LTIPTIGIGA SPACDGQVLV TEDMIGAFDA YTPRFVKRYA 

       250        260        270        280 
DANAVMRDAI RQYAHDVRQR VFPEPAHCFG YGKPLQLADA ATAA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000459 Genomic DNA. Translation: ABK10186.1.
RefSeqYP_837079.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0AXR0.

Genome annotation databases

GeneID4451510.
GenomeReviewsGene locus Bcen2424_3447 in contig CP000459_GR.
KEGGbch:Bcen2424_3447.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMA0AXR0.
OMALVVVDMP.

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 namePANB2_BURCH
AccessionPrimary (citable) accession number: A0AXR0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: November 28, 2006
Last modified: November 3, 2009
This is version 21 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