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Reviewed, UniProtKB/Swiss-Prot A2SEX8 (PANB2_METPP)

Last modified February 9, 2010. Version 26. 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

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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: Mpe_A1156
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Methylibium

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Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2792793-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156
PRO_0000297296

Regions

Region58 – 592Alpha-ketoisovalerate binding By similarity

Sites

Active site1951Proton acceptor By similarity
Metal binding581Magnesium By similarity
Metal binding971Magnesium By similarity
Metal binding1281Magnesium By similarity
Binding site971Alpha-ketoisovalerate By similarity
Binding site1261Alpha-ketoisovalerate By similarity

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Sequences

Sequence LengthMass (Da)Tools
A2SEX8-1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 7F792CF1667D6D06

FASTA27929,450
        10         20         30         40         50         60 
MSSHSSPADT PSARKPVTLH TLREMHARGE KIAMITAYDA SFAALVDTAG VDCILVGDSL 

        70         80         90        100        110        120 
GMVLKGQSST LSVTMEQIGY HTRSTSRGTK AAFLIADMPF GSYQENPVQA LRNAGTLMAA 

       130        140        150        160        170        180 
GAQMVKLEGG GWTPETVNFL VERGVPVCAH LGLTPQSVHA LGGYRIQGKD EAGAATLRRH 

       190        200        210        220        230        240 
AKALADAGAA MMVLELMPSR VAREVQADNP GLMTIGIGAG AGTAGQVLVL HDMLGVTRGR 

       250        260        270 
LPRFVRNFMD SATSIEDAVR RYVAAVKDGS FPDETLHAY

« Hide

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References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed: 17158667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000555 Genomic DNA. Translation: ABM94117.1. Different initiation.
RefSeqYP_001020352.1.

3D structure databases

SMRA2SEX8. Positions 17-275.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2SEX8.

Genome annotation databases

GeneID4785731.
GenomeReviewsGene locus Mpe_A1156 in contig CP000555_GR.
KEGGmpt:Mpe_A1156.
NMPDRfig|279263.3.peg.685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.

Family and domain databases

HAMAPMF_00156. PanB.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[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...

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Entry information

Entry namePANB2_METPP
AccessionPrimary (citable) accession number: A2SEX8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: February 9, 2010
This is version 26 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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