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B7JBM8 (PANB_ACIF2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:AFE_1771
OrganismAcidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) [Complete proteome] [HAMAP]
Taxonomic identifier243159 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length261 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 – 2612613-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000118113

Regions

Region44 – 452Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding441Magnesium By similarity
Metal binding831Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site831Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
B7JBM8 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: E6E871642D07AC9E

FASTA26127,743
        10         20         30         40         50         60 
MHKKIARWVQ DKKSGIKRAV VTAYDYPFAR LAAEAGVHGI LVGDSLGMVV GGGSDTLGVT 

        70         80         90        100        110        120 
LEQMAYHTGM VVRGAGDCLV FADLPFGSYE KGPEQAWAAA VTLLRAGADV VKLEGGAEMA 

       130        140        150        160        170        180 
STVAFCTERG INICAHIGLT PQRVRQWGSF QRQGTDADSA RRLQADAGAL AEAGARFLVL 

       190        200        210        220        230        240 
EAVPDALAAN ITRDIAIPTI GIGAGPDTDA QVLVIHDLLG LGTESPPFAR RYIEGGRIMR 

       250        260 
DALAEYVREV GNSEFPPRRK R 

« Hide

References

[1]"Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications."
Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S.
BMC Genomics 9:597-597(2008) [PubMed: 19077236] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23270 / DSM 14882 / NCIB 8455.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001219 Genomic DNA. Translation: ACK80864.1.
RefSeqYP_002426190.1. NC_011761.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB7JBM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7135434.
GenomeReviewsGene locus AFE_1771 in contig CP001219_GR.
KEGGafr:AFE_1771.
PATRIC20654679. VBIAciFer29821_1611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBCLSK2400173.

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_ACIF2
AccessionPrimary (citable) accession number: B7JBM8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 27 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