Skip Header

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

Q5NXQ3 (PANB_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:AZOSEA40360
ORF Names:ebA7119
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

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_0000297219

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
Q5NXQ3 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: EEBD7950BD7C134D

FASTA27128,881
        10         20         30         40         50         60 
MSYLQDDKPV TLFEIGKMRA EGRKISMLTC YDASFASLLE RAGVDILLVG DSLGNVVQGQ 

        70         80         90        100        110        120 
KSTLPVTLEH MIYHTECVVR GSTRPFIVTD MPFGAYHESP SQAMHNAASL LAAGAQMVKL 

       130        140        150        160        170        180 
EGGTFMAETV RFLVERGIPV CAHIGLTPQS VHQLGGYRVQ GRSEAAAAQL KGDALALEQA 

       190        200        210        220        230        240 
GAALMVMEMV PAALAREVTA SLASMATIGI GAGPDCDGQV LVLHDMIGVY PGKKARFVRN 

       250        260        270 
FMTGKTDIDE AVASYVQAVR DGSFPAAEHC Y 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI10161.1.
RefSeqYP_161062.1. NC_006513.1.

3D structure databases

HSSPHSSP built from PDB template 1O66 based on UniProtKB Q9JZW6.
ProteinModelPortalQ5NXQ3.
SMRQ5NXQ3. Positions 10-271.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5NXQ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3181660.
GenomeReviewsGene locus AZOSEA40360 in contig CR555306_GR.
KEGGeba:ebA7119.
NMPDRfig|76114.4.peg.4052.
PATRIC20974317. VBIAroAro98752_4072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycASP76114:EBA7119-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_AROAE
AccessionPrimary (citable) accession number: Q5NXQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 49 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