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Reviewed, UniProtKB/Swiss-Prot Q0AB69 (PANB_ALHEH)

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: Mlg_0564
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length277 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 – 2772773-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297212

Regions

Region54 – 552Alpha-ketoisovalerate binding By similarity

Sites

Active site1911Proton acceptor By similarity
Metal binding541Magnesium By similarity
Metal binding931Magnesium By similarity
Metal binding1241Magnesium By similarity
Binding site931Alpha-ketoisovalerate By similarity
Binding site1221Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AB69-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 5DC34BA88EDF06AF

FASTA27729,131
        10         20         30         40         50         60 
MYTGDPPQTR RPVTVGRLQR MKADGQKVVA LTAYDYTFAV AEDQAGVDVI LVGDSLGMVV 

        70         80         90        100        110        120 
QGRDTTVPVT VEEMVYHTRC VTAARPSALV MADMPFMSYA TLEDGLRNAA RLMQEGGAQM 

       130        140        150        160        170        180 
IKLEGAGEQA ELVARLARAG IPVCAHLGLQ PQLVHKLGGY RVQGRESAAA DAMLADAQAL 

       190        200        210        220        230        240 
EAAGADLLLL ECVPAELGRR ISQGLEIPVI GIGAGPDCDG QILVLQDILG VTPGRIPRFS 

       250        260        270 
KNFMNGAGSI QCALQAYVQA VRSGAFPDAA HSFGGQG 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI55918.1.
RefSeqYP_741408.1.

3D structure databases

SMRQ0AB69. Positions 12-274.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0AB69.

Genome annotation databases

GeneID4270894.
GenomeReviewsGene locus Mlg_0564 in contig CP000453_GR.
KEGGaeh:Mlg_0564.
NMPDRfig|187272.6.peg.537.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYATPEQT.
PhylomeDBQ0AB69.

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_ALHEH
AccessionPrimary (citable) accession number: Q0AB69
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: October 17, 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