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

Q1QSZ8 (PANC_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:Csal_3066
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

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_0000305425

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
Q1QSZ8 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: E05E18F84D6655BB

FASTA28330,602
        10         20         30         40         50         60 
MLTLSDIGEL RNHLHAARRD AKRIALVPTM GNLHAGHLAL VDAARRDADV VVATIFVNPL 

        70         80         90        100        110        120 
QFGANEDFAS YPRTLEADAQ ALASHGCDLV FTPRTDALYP HGLEAHTQVS VPDVSEGLCG 

       130        140        150        160        170        180 
ANRPGHFTGV ATVVSLLFNL VQPDAAYFGR KDYQQFMVIR KLVADLHFPI EIVGVPTQRA 

       190        200        210        220        230        240 
EDGLALSSRN GYLSAAERQR APALYRTLCQ VHDALRAGEA PPTALRDGLA ALAEQGFKPD 

       250        260        270        280 
YLELRRAQDL GPIAPDTQEA ILLVAAHLGT TRLIDNLAVS LPR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000285 Genomic DNA. Translation: ABE60410.1.
RefSeqYP_575109.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ1QSZ8.
SMRQ1QSZ8. Positions 1-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290398.Csal_3066.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE60410; ABE60410; Csal_3066.
GeneID4028870.
KEGGcsa:Csal_3066.
PATRIC21450006. VBIChrSal113723_3083.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAAYMGSTR.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

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_CHRSD
AccessionPrimary (citable) accession number: Q1QSZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 16, 2006
Last modified: May 14, 2014
This is version 52 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