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Reviewed, UniProtKB/Swiss-Prot Q2S8W3 (PANB2_HAHCH)

Last modified February 9, 2010. Version 30. 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 2
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase 2
      Short name=KPHMT 2
Gene names
Name: panB2
Ordered Locus Names: HCH_06264
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella

Protein attributes

Sequence length264 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 – 2642643-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156
PRO_0000297279

Regions

Region44 – 452Alpha-ketoisovalerate binding By similarity

Sites

Active site1801Proton acceptor By similarity
Metal binding441Magnesium By similarity
Metal binding831Magnesium By similarity
Metal binding1131Magnesium By similarity
Binding site831Alpha-ketoisovalerate By similarity
Binding site1111Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S8W3-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: F022E56C2A63411A

FASTA26428,050
        10         20         30         40         50         60 
MSITLSTLLD LKKKSEKFAV MTAYDATFAY EMDQAGVEVI LVGDSLGMVL QGHDSTIPVR 

        70         80         90        100        110        120 
LEDMVYHTAS VRRGARNAFI IADMPFMSYG TPDQAMAGAK QLMQAGAHMV KLEGGAWLCD 

       130        140        150        160        170        180 
AIAHLSRQGV PICAHLGLTP QSVNKFGGYK VQGKEASQAQ LMLDDAKALE QAGADILLLE 

       190        200        210        220        230        240 
CVPTKLAKQL TEEACAPVVG IGAGPYTDGQ VLVMHDLLGV GAGKKPKFVK NFLAGSDSIQ 

       250        260 
AAFKGYVEAV KSGAFPAEEH SFNI 

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000155 Genomic DNA. Translation: ABC32911.1.
RefSeqYP_437336.1.

3D structure databases

SMRQ2S8W3. Positions 2-263.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2S8W3.

Genome annotation databases

GeneID3839111.
GenomeReviewsGene locus HCH_06264 in contig CP000155_GR.
KEGGhch:HCH_06264.
NMPDRfig|349521.5.peg.5496.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYATPEQT.
PhylomeDBQ2S8W3.

Enzyme and pathway databases

BioCycHCHE349521:HCH_06264-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 namePANB2_HAHCH
AccessionPrimary (citable) accession number: Q2S8W3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: January 24, 2006
Last modified: February 9, 2010
This is version 30 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