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A5IAR4 (PANC_LEGPC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:LPC_0477
OrganismLegionella pneumophila (strain Corby) [Complete proteome] [HAMAP]
Taxonomic identifier400673 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length252 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 – 252252Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000011431

Regions

Nucleotide binding29 – 368ATP By similarity
Nucleotide binding146 – 1494ATP By similarity
Nucleotide binding183 – 1864ATP By similarity

Sites

Active site361Proton donor By similarity
Binding site601Beta-alanine By similarity
Binding site601Pantoate By similarity
Binding site1521Pantoate By similarity
Binding site1751ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IAR4 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 492DBA4FF7377648

FASTA25228,832
        10         20         30         40         50         60 
MQIFHNLNEW IRFRNTLSPD LSLGFAPTMG NLHAGHASLF LASSKENHYT VSSLFVNPTQ 

        70         80         90        100        110        120 
FNNPDDYKHY PRTVDADLEL MTQNGVDFCI LPNENEIYTD GYAYQVQENR LGQLMEGKHR 

       130        140        150        160        170        180 
PGHFNGVLTI VMKLFNLVKP TRAYFGEKDY QQLLLIQGMV KALFMDIEIK SCPTVREKSG 

       190        200        210        220        230        240 
LACSSRNNRL TPSQREIADE FAKIFHQNKS SAMISKELEA LGITVEYIEE FQGRRFAAVK 

       250 
IGDIRLIDNY LL 

« Hide

References

[1]"Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Corby.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000675 Genomic DNA. Translation: ABQ54464.1.
RefSeqYP_001249810.1. NC_009494.2.

3D structure databases

ProteinModelPortalA5IAR4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400673.LPC_0477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ54464; ABQ54464; LPC_0477.
GeneID5182274.
KEGGlpc:LPC_0477.
PATRIC22307317. VBILegPne45588_0496.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAASSKENH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycLPNE400673:GCIT-2883-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_LEGPC
AccessionPrimary (citable) accession number: A5IAR4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 44 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