Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P31663 (PANC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantothenate synthetase

Short name=PS
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene names
Name:panC
Ordered Locus Names:b0133, JW0129
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Ref.4

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

Enzyme regulation

Activation requires a combination of a divalent cation, magnesium or manganese, and a monovalent cation, potassium or ammonium. Above the optimum concentration for activation, magnesium and manganese are rather inhibitory. Also activated by 2-mercaptoethanol, dithiothreitol, cysteine and glutathione. Inhibited by divalent cations (mercury, cobalt, zinc, copper, silver), chelating agents (EDTA, EGTA and o-phenanthroline), and analogs of beta-alanine (taurine, gamma-aminobutyrate, gamma-amino-beta-hydroxybutyrate). Ref.4

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism.

Sequence similarities

Belongs to the pantothenate synthetase family.

Biophysicochemical properties

Kinetic parameters:

KM=63 µM for pantoate Ref.4

KM=100 µM for ATP

KM=150 µM for beta-alanine

KM=2000 µM for magnesium

KM=5500 µM for manganese

pH dependence:

Optimum pH is 10. Stable from pH 5.0 to 11.0.

Temperature dependence:

Optimum temperature is 30 degrees Celsius. Stable up to 37 degrees Celsius and loses activity almost completely when incubated at 60 degrees Celsius for 10 minutes.

Mass spectrometry

Molecular mass is 31601.2±3.4 Da from positions 1 - 283. Determined by ESI. Ref.5

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-545354,EBI-545354
yfcDP655565EBI-545354,EBI-545346

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128229

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding149 – 1524ATP By similarity
Nucleotide binding186 – 1894ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1551Pantoate By similarity
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

.................................................. 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31663 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 4246647C6FDAFB20

FASTA28331,598
        10         20         30         40         50         60 
MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV VVVSIFVNPM 

        70         80         90        100        110        120 
QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP NGTETHTYVD VPGLSTMLEG 

       130        140        150        160        170        180 
ASRPGHFRGV STIVSKLFNL VQPDIACFGE KDFQQLALIR KMVADMGFDI EIVGVPIMRA 

       190        200        210        220        230        240 
KDGLALSSRN GYLTAEQRKI APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA 

       250        260        270        280 
DDIQIRDADT LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and sequence of the Escherichia coli panBCD gene cluster."
Merkel W.K., Nichols B.P.
FEMS Microbiol. Lett. 143:247-252(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Enzymological properties of pantothenate synthetase from Escherichia coli B."
Miyatake K., Nakano Y., Kitaoka S.
J. Nutr. Sci. Vitaminol. 24:243-253(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ENZYME REGULATION.
Strain: B.
[5]"The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily."
von Delft F., Lewendon A., Dhanaraj V., Blundell T.L., Abell C., Smith A.G.
Structure 9:439-450(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MASS SPECTROMETRY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L17086 Genomic DNA. Translation: AAA24272.1.
U00096 Genomic DNA. Translation: AAC73244.1.
AP009048 Genomic DNA. Translation: BAE76042.1.
PIRE64736.
RefSeqNP_414675.1. NC_000913.3.
YP_488436.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHOX-ray1.70A/B1-283[»]
3GUZX-ray1.67A/B1-176[»]
ProteinModelPortalP31663.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10437N.
IntActP31663. 11 interactions.
MINTMINT-1249237.
STRING511145.b0133.

2D gel databases

SWISS-2DPAGEP31663.

Proteomic databases

PaxDbP31663.
PRIDEP31663.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73244; AAC73244; b0133.
BAE76042; BAE76042; BAE76042.
GeneID12932172.
944958.
KEGGecj:Y75_p0130.
eco:b0133.
PATRIC32115371. VBIEscCol129921_0137.

Organism-specific databases

EchoBASEEB1696.
EcoGeneEG11746. panC.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAECPIVRE.
OrthoDBEOG6Z6FZ4.
PhylomeDBP31663.

Enzyme and pathway databases

BioCycEcoCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
ECOL316407:JW0129-MONOMER.
MetaCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
UniPathwayUPA00028; UER00005.

Gene expression databases

GenevestigatorP31663.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP31663.
PROP31663.

Entry information

Entry namePANC_ECOLI
AccessionPrimary (citable) accession number: P31663
Secondary accession number(s): Q2MCG4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 11, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene