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A1KAA5 (PANB_AZOSB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. 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:azo3144
OrganismAzoarcus sp. (strain BH72) [Complete proteome] [HAMAP]
Taxonomic identifier62928 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length271 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 – 2712713-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297218

Regions

Region51 – 522Alpha-ketoisovalerate binding By similarity

Sites

Active site1881Proton acceptor By similarity
Metal binding511Magnesium By similarity
Metal binding901Magnesium By similarity
Metal binding1211Magnesium By similarity
Binding site901Alpha-ketoisovalerate By similarity
Binding site1191Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KAA5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 3512F64C9877D563

FASTA27128,665
        10         20         30         40         50         60 
MSYLQDDKPV TLFELGKMRA EGRKIAMLTC YDASFAALLE RNGVDVLLVG DSLGNVLQGQ 

        70         80         90        100        110        120 
KSTLPVTLEQ MAYHTECVVR GSSRPFVVTD MPFGSYQESP EQAMRNAARL MAAGAEMVKL 

       130        140        150        160        170        180 
EGGAFMAETV RFLVERGVPV CAHIGLTPQS VHQLGGYRVQ GRSEEGAARL KADALALEQA 

       190        200        210        220        230        240 
GAALVVLEMV PAAVASDITR SLSTMATIGI GAGADCSGQV LVLHDMIGVY PGKKARFVKN 

       250        260        270 
FMEGAASIDA AVAAYVAAVK DGSFPAAEHC Y 

« Hide

References

[1]"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. expand/collapse author list , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BH72.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM406670 Genomic DNA. Translation: CAL95761.1.
RefSeqYP_934647.1. NC_008702.1.

3D structure databases

ProteinModelPortalA1KAA5.
SMRA1KAA5. Positions 10-271.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1KAA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4607817.
GenomeReviewsGene locus azo3144 in contig AM406670_GR.
KEGGazo:azo3144.
PATRIC21014724. VBIAzoSp26047_3190.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYDATFAH.
PhylomeDBA1KAA5.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycASP62928:AZO3144-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_AZOSB
AccessionPrimary (citable) accession number: A1KAA5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 37 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