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Reviewed, UniProtKB/Swiss-Prot Q57F29 (PANB_BRUAB)

Last modified November 24, 2009. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: BruAb1_0356
OrganismBrucella abortus [Complete proteome] [HAMAP]
Taxonomic identifier235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length275 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 – 2752753-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297226

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
Q57F29-1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: F73117B84258FE26

FASTA27529,418
        10         20         30         40         50         60 
MSAPVTRKRL TPKVIQAMKG ECPIVSLTAY TTPVARLLDP HCDLLLVGDS LGMVLYGMES 

        70         80         90        100        110        120 
TLAVTLDMMI MHGQAVMRGT SHACVIVDMP FGSYQESKEQ AFRNAARVMQ ETGCDGVKLE 

       130        140        150        160        170        180 
GGEEMAETVA FLVRRGIPVF GHVGLMPQQV NTVGGFRSLG RGDDEAGKIR RDAQAIAQAG 

       190        200        210        220        230        240 
AFAVVIEGTV EPLAREITAL IDIPTVGIGA SSACDGQVLV SDDMLGLFQD FTPRFVKRFA 

       250        260        270 
HLAPQVSQAA EAYAEEVRAR RFPGPEHVFG AKPGA 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941 / Biovar 1.

Cross-references

Sequence databases

AE017223 Genomic DNA. Translation: AAX73755.1.
RefSeqYP_221116.1.

3D structure databases

HSSPHSSP built from PDB template 1O66 based on UniProtKB Q9JZW6.
ModBaseSearch...

Genome annotation databases

GeneID3339160.
GenomeReviewsGene locus BruAb1_0356 in contig AE017223_GR.
KEGGbmb:BruAb1_0356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ57F29.
OMADMMIAHG

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_0356-MON.
BRENDA2.1.2.11. 575.

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_BRUAB
AccessionPrimary (citable) accession number: Q57F29
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: May 10, 2005
Last modified: November 24, 2009
This is version 29 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

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

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