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Reviewed, UniProtKB/Swiss-Prot B0V5M5 (PANB_ACIBY)

Last modified November 3, 2009. Version 16. 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
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase
      Short name=KPHMT
Gene names
Name: panB
Ordered Locus Names: ABAYE3175
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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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 – 2692693-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000096935

Regions

Region43 – 442Alpha-ketoisovalerate binding By similarity

Sites

Active site1791Proton acceptor By similarity
Metal binding431Magnesium By similarity
Metal binding821Magnesium By similarity
Metal binding1121Magnesium By similarity
Binding site821Alpha-ketoisovalerate By similarity
Binding site1101Alpha-ketoisovalerate By similarity

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Sequences

Sequence LengthMass (Da)Tools
B0V5M5-1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: A92CEDA056752238

FASTA26928,976
        10         20         30         40         50         60 
MISLSDLRKF KAEGRKFSCL TCYDASMAKA MELAEIDTIL IGDSLGMAIQ GRDSTLPVTV 

        70         80         90        100        110        120 
EDMAYHTAAV RRGNQHALIM TDLPFMSYAT LNDALQNAKT VMQAGAQMIK IEGGAWLSET 

       130        140        150        160        170        180 
VQVLTRNGVP VCVHLGLTPQ SVHVFGGYKL QARTREAADQ LIADCTAVVE AGAAVLLLEC 

       190        200        210        220        230        240 
VPAQLGQEIA ELFPNTPVIG IGAGNATDGQ VLVVQDMLGL TFGRVARFVR NFMKEQSGET 

       250        260 
AILDAFKAFH AAVQDQSFPA KEHTFQVEL

« Hide

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References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CU459141 Genomic DNA. Translation: CAM87984.1.
RefSeqYP_001714956.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6003606.
GenomeReviewsGene locus ABAYE3175 in contig CU459141_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYATPEQT.

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...

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Entry information

Entry namePANB_ACIBY
AccessionPrimary (citable) accession number: B0V5M5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: November 3, 2009
This is version 16 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)

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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