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Reviewed, UniProtKB/Swiss-Prot Q5E2T2 (PANB1_VIBF1)

Last modified February 9, 2010. Version 33. 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: VF_2169
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Complete proteome] [HAMAP]
Taxonomic identifier312309 [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: 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 – 2642643-methyl-2-oxobutanoate hydroxymethyltransferase 1 HAMAP MF_00156
PRO_0000297408

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
Q5E2T2-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 7BB66C286AAA3F94

FASTA26428,673
        10         20         30         40         50         60 
MKKISIHDLM KWKQEGKKFA TVTAYDASFA QLFEQQEVPV LLVGDSLGMV LQGKSDTLPV 

        70         80         90        100        110        120 
TTEEIAYHTR CVRAGSPNSL LMADMPFMSY ATPEQACENA GKLMQAGANM VKIEGGEWIA 

       130        140        150        160        170        180 
ETVRVLAERA VPVCAHLGLT PQSVNIFGGF RIQGRDEAKA EQMVKDALTL EAAGAQIILL 

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

       250        260 
RKAVTKYIQD VEQGVFPVAE HTFN 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed: 15703294] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW86664.1.
RefSeqYP_205552.1.

3D structure databases

HSSPHSSP built from PDB template 1M3U based on UniProtKB P31057.
SMRQ5E2T2. Positions 5-264.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5E2T2.

Genome annotation databases

GeneID3279367.
GenomeReviewsGene locus VF_2169 in contig CP000020_GR.
KEGGvfi:VF_2169.
NMPDRfig|312309.3.peg.2169.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYATPEQT.
PhylomeDBQ5E2T2.

Enzyme and pathway databases

BioCycVFIS312309:VF2169-MONOMER.

Family and domain databases

HAMAPMF_00156. PanB.
[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_VIBF1
AccessionPrimary (citable) accession number: Q5E2T2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: March 15, 2005
Last modified: February 9, 2010
This is version 33 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