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P31663

- PANC_ECOLI

UniProt

P31663 - PANC_ECOLI

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Protein

Pantothenate synthetase

Gene

panC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.1 Publication

Catalytic activityi

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

Enzyme regulationi

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).1 Publication

Kineticsi

  1. KM=63 µM for pantoate1 Publication
  2. KM=100 µM for ATP1 Publication
  3. KM=150 µM for beta-alanine1 Publication
  4. KM=2000 µM for magnesium1 Publication
  5. KM=5500 µM for manganese1 Publication

pH dependencei

Optimum pH is 10. Stable from pH 5.0 to 11.0.1 Publication

Temperature dependencei

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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371Proton donorBy similarity
Binding sitei61 – 611Beta-alanineBy similarity
Binding sitei61 – 611PantoateBy similarity
Binding sitei155 – 1551PantoateBy similarity
Binding sitei178 – 1781ATP; via amide nitrogen and carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378ATPBy similarity
Nucleotide bindingi149 – 1524ATPBy similarity
Nucleotide bindingi186 – 1894ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. pantoate-beta-alanine ligase activity Source: EcoCyc

GO - Biological processi

  1. pantothenate biosynthetic process from valine Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
ECOL316407:JW0129-MONOMER.
MetaCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate synthetase (EC:6.3.2.1)
Short name:
PS
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene namesi
Name:panC
Ordered Locus Names:b0133, JW0129
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11746. panC.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283Pantothenate synthetasePRO_0000128229Add
BLAST

Proteomic databases

PaxDbiP31663.
PRIDEiP31663.

2D gel databases

SWISS-2DPAGEP31663.

Expressioni

Gene expression databases

GenevestigatoriP31663.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-545354,EBI-545354
yfcDP655565EBI-545354,EBI-545346

Protein-protein interaction databases

DIPiDIP-10437N.
IntActiP31663. 11 interactions.
MINTiMINT-1249237.
STRINGi511145.b0133.

Structurei

Secondary structure

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43
Helixi7 – 1913
Beta strandi24 – 296
Helixi35 – 373
Helixi38 – 469
Beta strandi49 – 557
Helixi59 – 613
Helixi65 – 706
Helixi75 – 8410
Beta strandi89 – 913
Helixi95 – 984
Beta strandi108 – 1103
Helixi114 – 1163
Helixi119 – 1224
Helixi126 – 14116
Beta strandi144 – 1529
Helixi153 – 16614
Beta strandi171 – 1755
Helixi188 – 1925
Helixi195 – 2006
Helixi203 – 21614
Helixi222 – 23615
Beta strandi239 – 2479
Turni248 – 2503
Beta strandi260 – 26910
Beta strandi272 – 28110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHOX-ray1.70A/B1-283[»]
3GUZX-ray1.67A/B1-176[»]
ProteinModelPortaliP31663.
SMRiP31663. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31663.

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175517.
InParanoidiP31663.
KOiK01918.
OMAiECPIVRE.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP31663.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

P31663 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV
60 70 80 90 100
VVVSIFVNPM QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP
110 120 130 140 150
NGTETHTYVD VPGLSTMLEG ASRPGHFRGV STIVSKLFNL VQPDIACFGE
160 170 180 190 200
KDFQQLALIR KMVADMGFDI EIVGVPIMRA KDGLALSSRN GYLTAEQRKI
210 220 230 240 250
APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA DDIQIRDADT
260 270 280
LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA
Length:283
Mass (Da):31,598
Last modified:July 1, 1993 - v1
Checksum:i4246647C6FDAFB20
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L17086 Genomic DNA. Translation: AAA24272.1.
U00096 Genomic DNA. Translation: AAC73244.1.
AP009048 Genomic DNA. Translation: BAE76042.1.
PIRiE64736.
RefSeqiNP_414675.1. NC_000913.3.
YP_488436.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73244; AAC73244; b0133.
BAE76042; BAE76042; BAE76042.
GeneIDi12932172.
944958.
KEGGiecj:Y75_p0130.
eco:b0133.
PATRICi32115371. VBIEscCol129921_0137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L17086 Genomic DNA. Translation: AAA24272.1 .
U00096 Genomic DNA. Translation: AAC73244.1 .
AP009048 Genomic DNA. Translation: BAE76042.1 .
PIRi E64736.
RefSeqi NP_414675.1. NC_000913.3.
YP_488436.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IHO X-ray 1.70 A/B 1-283 [» ]
3GUZ X-ray 1.67 A/B 1-176 [» ]
ProteinModelPortali P31663.
SMRi P31663. Positions 1-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10437N.
IntActi P31663. 11 interactions.
MINTi MINT-1249237.
STRINGi 511145.b0133.

2D gel databases

SWISS-2DPAGE P31663.

Proteomic databases

PaxDbi P31663.
PRIDEi P31663.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73244 ; AAC73244 ; b0133 .
BAE76042 ; BAE76042 ; BAE76042 .
GeneIDi 12932172.
944958.
KEGGi ecj:Y75_p0130.
eco:b0133.
PATRICi 32115371. VBIEscCol129921_0137.

Organism-specific databases

EchoBASEi EB1696.
EcoGenei EG11746. panC.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175517.
InParanoidi P31663.
KOi K01918.
OMAi ECPIVRE.
OrthoDBi EOG6Z6FZ4.
PhylomeDBi P31663.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci EcoCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
ECOL316407:JW0129-MONOMER.
MetaCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.

Miscellaneous databases

EvolutionaryTracei P31663.
PROi P31663.

Gene expression databases

Genevestigatori P31663.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi IPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR21299:SF1. PTHR21299:SF1. 1 hit.
Pfami PF02569. Pantoate_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPANC_ECOLI
AccessioniPrimary (citable) accession number: P31663
Secondary accession number(s): Q2MCG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3