Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A6L3Y2 (PANB_BACV8)

Last modified November 3, 2009. Version 23. 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

Hide | Top

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: BVU_2746
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Hide | Top

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2732733-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000011362

Regions

Region53 – 542Alpha-ketoisovalerate binding By similarity

Sites

Active site1911Proton acceptor By similarity
Metal binding531Magnesium By similarity
Metal binding921Magnesium By similarity
Metal binding1241Magnesium By similarity
Binding site921Alpha-ketoisovalerate By similarity
Binding site1221Alpha-ketoisovalerate By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
A6L3Y2-1 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: EA5A0AE83A3A2DA0

FASTA27329,579
        10         20         30         40         50         60 
MAGYISGDTR KVTTHRLVEM KQRGEKISML TSYDYTTAQI VDGAGIDVIL VGDSASNVMA 

        70         80         90        100        110        120 
GNVTTLPITL DQMIYHGKSV VRGVKRALVV VDLPFGTYQT SEYEAVTNAI KVMKITHADA 

       130        140        150        160        170        180 
LKLEGGVEII DAVKKIIAAG IPIMGHLGLM PQSINKYGTY TVRAKDEEEA EKLLSDAHLL 

       190        200        210        220        230        240 
EETGCFALVL EKIPASLAER VARELTIPVI GIGAGGAVDG QVLVVSDMLG MTNGFSPRFL 

       250        260        270 
RRYADLHTVM TGAIQQYVDD VKKGDFPNED EQY

« Hide

Hide | Top

References

[1]"Evolution of symbiotic bacteria in the distal human intestine."
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.
PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

CP000139 Genomic DNA. Translation: ABR40396.1.
RefSeqYP_001300018.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6L3Y2.

Genome annotation databases

GeneID5303709.
GenomeReviewsGene locus BVU_2746 in contig CP000139_GR.
KEGGbvu:BVU_2746.
NMPDRfig|435590.6.peg.2582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMALVVVDMP.

Family and domain databases

HAMAPMF_00156.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
[Graphical view]
PANTHERPTHR20881. Pantoate_transf. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
TIGRFAMsTIGR00222. panB. 1 hit.
ProtoNetSearch...

Hide | Top

Entry information

Entry namePANB_BACV8
AccessionPrimary (citable) accession number: A6L3Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: November 3, 2009
This is version 23 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)

Hide | Top

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