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Reviewed, UniProtKB/Swiss-Prot A0KP07 (PANB_AERHH)

Last modified November 3, 2009. Version 22. 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: AHA_3538
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

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Protein attributes

Sequence length264 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 – 2642643-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297209

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

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Sequences

Sequence LengthMass (Da)Tools
A0KP07-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 00DCE8E750327A8E

FASTA26428,702
        10         20         30         40         50         60 
MSKITTTNLL KMKQEGQRIT AITAYDATFA KLFDDEGAHV LLIGDSLGMV LQGGQDTLGV 

        70         80         90        100        110        120 
SMDEMVYHTR CVVRGTTNAL VVTDMPFMSY ATPEQTYQNA ARLMAAGARM VKMEGGDWLC 

       130        140        150        160        170        180 
DSIRHLTRNG VPVCGHLGLT PQSVHVFGGF KVQGRDEFQA QEIYRQALEL QAAGIQLLVL 

       190        200        210        220        230        240 
ECVPTSLAER ISKALRIPVI GIGAGPATDG QILVMHDAFG ITSGYVPKFT KNFLAETGDM 

       250        260 
RAAIRLYVKQ VSEGTFPGPE HCFN

« Hide

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References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000462 Genomic DNA. Translation: ABK37379.1.
RefSeqYP_858008.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0KP07.

Genome annotation databases

GeneID4488710.
GenomeReviewsGene locus AHA_3538 in contig CP000462_GR.
KEGGaha:AHA_3538.
TIGRAHA_3538.

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_AERHH
AccessionPrimary (citable) accession number: A0KP07
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 22 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