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A1R5H8 (PANB_ARTAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. 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:AAur_1730
OrganismArthrobacter aurescens (strain TC1) [Complete proteome] [HAMAP]
Taxonomic identifier290340 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length301 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 – 3013013-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297216

Regions

Region82 – 832Alpha-ketoisovalerate binding By similarity

Sites

Active site2191Proton acceptor By similarity
Metal binding821Magnesium By similarity
Metal binding1211Magnesium By similarity
Metal binding1531Magnesium By similarity
Binding site1211Alpha-ketoisovalerate By similarity
Binding site1511Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1R5H8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: EA2F108E44BDA694

FASTA30131,540
        10         20         30         40         50         60 
MAPSNLPEST TPAEVPAPYG TGPAAAAQAA SAAGRKPISR VRIHHLQQAK DNGEHFAMLT 

        70         80         90        100        110        120 
AYEQYTAEIF DQAGIEVLLV GDSASNNVYG NETSLPVTVD ELLPLTRAVS RSAKRALIVA 

       130        140        150        160        170        180 
DLPFGSYEVS PGQAVATGVR FLKEGLAHAV KIEGTAYYAD TVRAMVQAGI PVMAHIGFTP 

       190        200        210        220        230        240 
QSEHSLGGYR VQGRGDDAQR LVDDAVALQD AGAFSVLMEM VPAETAAAVD AALRVPTVGI 

       250        260        270        280        290        300 
GAGKTTTGQV LVWQDMAGLR GGKMAKFVKQ YADLRTTLSD AAAAYGEDVR SGQFPGPEHS 


F 

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References

[1]"Secrets of soil survival revealed by the genome sequence of Arthrobacter aurescens TC1."
Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.
PLoS Genet. 2:2094-2106(2006) [PubMed: 17194220] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000474 Genomic DNA. Translation: ABM08191.1.
RefSeqYP_947490.1. NC_008711.1.

3D structure databases

ProteinModelPortalA1R5H8.
SMRA1R5H8. Positions 39-299.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1R5H8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4638844.
GenomeReviewsGene locus AAur_1730 in contig CP000474_GR.
KEGGaau:AAur_1730.
PATRIC20978860. VBIArtAur67810_1763.
TIGRAAur_1730.

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAQVLVWTD.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycAAUR290340:AAUR_1730-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_ARTAT
AccessionPrimary (citable) accession number: A1R5H8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 38 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