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Reviewed, UniProtKB/Swiss-Prot Q0BI15 (PANB1_BURCM)

Last modified November 3, 2009. Version 24. 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 1
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase 1
      Short name=KPHMT 1
Gene names
Name: panB1
Ordered Locus Names: Bamb_0649
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length271 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 – 2712713-methyl-2-oxobutanoate hydroxymethyltransferase 1 HAMAP MF_00156
PRO_0000297231

Regions

Region53 – 542Alpha-ketoisovalerate binding By similarity

Sites

Active site1891Proton acceptor By similarity
Metal binding531Magnesium By similarity
Metal binding921Magnesium By similarity
Metal binding1221Magnesium By similarity
Binding site921Alpha-ketoisovalerate By similarity
Binding site1201Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BI15-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 1C650F489D4B7D26

FASTA27128,740
        10         20         30         40         50         60 
MTYLQESSRP AVTVPKLQAM RDAGEKIAML TCYDASFAAL LDRSGVDVLL IGDSLGNVLQ 

        70         80         90        100        110        120 
GHTTTLPVSL DDIAYHTACV ARAQPRALII ADLPFGTYGT PAEAFASAVK LMRAGAQMIK 

       130        140        150        160        170        180 
LEGGEWLAET IRFLVERAVP VCAHVGLTPQ SVHAFGGFKV QGKTEAGAAQ LLRDARAVED 

       190        200        210        220        230        240 
AGAQLVVLEA VPTLVASEVT HMLKIPTIGI GAGTDCSGQV LVLHDMLGIF PGKRPRFVKD 

       250        260        270 
FMQGQPTIQA AVEAYVRAVK DSSFPGPEHS F 

« Hide

References

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

Cross-references

Sequence databases

CP000440 Genomic DNA. Translation: ABI86208.1.
RefSeqYP_772542.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BI15.

Genome annotation databases

GeneID4309296.
GenomeReviewsGene locus Bamb_0649 in contig CP000440_GR.
KEGGbam:Bamb_0649.
NMPDRfig|339670.3.peg.3159.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMSYLLDP.

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 namePANB1_BURCM
AccessionPrimary (citable) accession number: Q0BI15
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: October 17, 2006
Last modified: November 3, 2009
This is version 24 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