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B5YZH0 (PANC_ECO5E) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:
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:ECH74115_0142
OrganismEscherichia coli O157:H7 (strain EC4115 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier444450 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP-Rule MF_00158

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00158

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

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

Sequence similarities

Belongs to the pantothenate synthetase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantoate-beta-alanine ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000097060

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

Sequences

Sequence LengthMass (Da)Tools
B5YZH0 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 575364697ADAFB20

FASTA28331,568
        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 DLDEIIAIAG QELNEKGFRA 

       250        260        270        280 
DDIQIRDADT LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA 

« Hide

References

[1]"Complete genome sequence of Escherichia coli O157:H7 str. EC4115."
Eppinger M., Sebastian Y., Ravel J.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EC4115 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001164 Genomic DNA. Translation: ACI37358.1.
RefSeqYP_002268742.1. NC_011353.1.

3D structure databases

ProteinModelPortalB5YZH0.
SMRB5YZH0. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444450.ECH74115_0142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI37358; ACI37358; ECH74115_0142.
GeneID6969266.
KEGGecf:ECH74115_0142.
PATRIC18361128. VBIEscCol74651_0279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAIRELRAW.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycECOL444450:GHOB-139-MONOMER.
UniPathwayUPA00028; UER00005.

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...

Entry information

Entry namePANC_ECO5E
AccessionPrimary (citable) accession number: B5YZH0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: February 19, 2014
This is version 41 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

PATHWAY comments

Index of metabolic and biosynthesis pathways