Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8FEH7 (PANB_BACP2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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
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:BPUM_1974
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length279 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 – 2792793-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000058181

Regions

Region43 – 442Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding431Magnesium By similarity
Metal binding821Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site821Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FEH7 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 0FA14141E5A8443E

FASTA27930,484
        10         20         30         40         50         60 
MKTKLDFFKM KEQNEPIVML TAYDYPSAKQ AEKAEVDMIL VGDSLGMVVL GLDSTIQVTI 

        70         80         90        100        110        120 
DDMIHHTKAV KRGAKDTFIV TDMPFMSYHY SLAETLKNAA RIMQESGADA LKLEGGDGVF 

       130        140        150        160        170        180 
ESIQALTRGG IPVVSHLGLT PQSVGVLGGY KVQGKDHESA QKLIEDSLKC EEAGAIALVL 

       190        200        210        220        230        240 
ECVPGELTKR ITDMLKIPVI GIGAGAEADG QVLVYHDVVG YGVSRTPKFV KQYAQIDTLL 

       250        260        270 
EEALIQYTKE VKAHTFPEDK HTFHIKEEVL DGLYGGIKK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000813 Genomic DNA. Translation: ABV62644.1.
RefSeqYP_001487204.1. NC_009848.1.

3D structure databases

ProteinModelPortalA8FEH7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FEH7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000063386; EBBACP00000061719; EBBACG00000063377.
GeneID5621243.
GenomeReviewsGene locus BPUM_1974 in contig CP000813_GR.
KEGGbpu:BPUM_1974.
PATRIC18967848. VBIBacPum16546_2020.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
GeneTreeEBGT00050000000505.
HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycBPUM315750:BPUM_1974-MONOMER.

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_BACP2
AccessionPrimary (citable) accession number: A8FEH7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 31 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents