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Reviewed, UniProtKB/Swiss-Prot Q2IFU2 (PANB_ANADE)

Last modified February 9, 2010. Version 29. 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
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase
      Short name=KPHMT
Gene names
Name: panB
Ordered Locus Names: Adeh_3682
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length305 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 – 3053053-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297214

Regions

Region52 – 532Alpha-ketoisovalerate binding By similarity

Sites

Active site1941Proton acceptor By similarity
Metal binding521Magnesium By similarity
Metal binding951Magnesium By similarity
Metal binding1271Magnesium By similarity
Binding site951Alpha-ketoisovalerate By similarity
Binding site1251Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IFU2-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 6466692963670454

FASTA30532,132
        10         20         30         40         50         60 
MSSHPPPRKH VNIHELRRMK EAGERIAMVT AYDATAARLV AAAGVDAVLV GDSLGMAVQG 

        70         80         90        100        110        120 
HESTLPVTLD QMVYHSAMVR RGLARGDGRA HLVADMSFGS YQASADEAVK AAMRLVAEGG 

       130        140        150        160        170        180 
AEAVKLEGGA EFGDVIRRIV RAGVPVMGHI GLTPQSVHKM GGYVVQGKDS EKAQQILRDA 

       190        200        210        220        230        240 
RALEAAGCYA LVLECIPSEL ARIVTSQLRI PTIGIGAGPH CDGQVLVLND LLGLDASFTP 

       250        260        270        280        290        300 
KFVKRFGELG AAVEGAVGAY VGEVKARAFP DDAHSFHSAS VRLVPVERHA EEAEEEPPDA 


IGAPI 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC83448.1.
RefSeqYP_466885.1.

3D structure databases

SMRQ2IFU2. Positions 11-274.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IFU2.

Genome annotation databases

GeneID3886457.
GenomeReviewsGene locus Adeh_3682 in contig CP000251_GR.
KEGGade:Adeh_3682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYATPEQT.
PhylomeDBQ2IFU2.

Enzyme and pathway databases

BioCycADEH290397:ADEH_3682-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 namePANB_ANADE
AccessionPrimary (citable) accession number: Q2IFU2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: March 7, 2006
Last modified: February 9, 2010
This is version 29 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