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B6ELE1 (PANB_ALISL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:VSAL_I2609
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
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. 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.

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-methyl-2-oxobutanoate hydroxymethyltransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2642643-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000096937

Regions

Region45 – 462Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding451Magnesium By similarity
Metal binding841Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site841Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
B6ELE1 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 5A56A591AE8F334E

FASTA26428,720
        10         20         30         40         50         60 
MKKISIHDLM KWKQDGRKFA TVTAYDASFA QLFEQQDMPV LLVGDSLGMV LQGKSDTLPV 

        70         80         90        100        110        120 
TTEEIAYHTR CVRAGSPNSL LMADMPFMSY ATPEQACQNA AKLMQAGANM VKIEGGEWIA 

       130        140        150        160        170        180 
ETIKLLAERA VPVCAHLGLT PQSVNIFGGF RIQGRDETKA NQMVKDALTL EKAGAQIILL 

       190        200        210        220        230        240 
ECVPASLAER ITKACTVPVI GIGAGNVTDG QILVMHDMFG ISANYMPKFS KNFLAETGDM 

       250        260 
RTAVTKYIKD VELGVFPAAE HTFN 

« Hide

References

[1]"The complete genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238."
Hjerde E., Lorentzen M.S., Holden M.T.G., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.-P., Thomson N.R.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LFI1238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM178379 Genomic DNA. Translation: CAQ80293.1.
RefSeqYP_002263952.1. NC_011312.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB6ELE1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6988557.
GenomeReviewsGene locus VSAL_I2609 in contig FM178379_GR.
KEGGvsa:VSAL_I2609.
PATRIC20855691. VBIAliSal95923_2835.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBPRK00311.

Family and domain databases

HAMAPMF_00156. PanB.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK00606.
PANTHERPTHR20881. Pantoate_transf. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR00222. PanB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB_ALISL
AccessionPrimary (citable) accession number: B6ELE1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families