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Q0S8D5 (PANC_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:RHA1_ro04415
OrganismRhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]
Taxonomic identifier101510 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length312 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 – 312312Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305529

Regions

Nucleotide binding42 – 498ATP By similarity
Nucleotide binding159 – 1624ATP By similarity
Nucleotide binding196 – 1994ATP By similarity

Sites

Active site491Proton donor By similarity
Binding site731Beta-alanine By similarity
Binding site731Pantoate By similarity
Binding site1651Pantoate By similarity
Binding site1881ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0S8D5 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 9DF1D28D3313099C

FASTA31232,922
        10         20         30         40         50         60 
MSDLQGGYKR GELTVHHDPS VLTRVSKALR GVGRQVALVP TMGALHTGHL ELVRQAKLTG 

        70         80         90        100        110        120 
AVVIVSIFVN PLQFGAGEDL DAYPRTLDAD LELLREAGVE LAFVPTAATM YPAGPRTTIH 

       130        140        150        160        170        180 
PGPLGAELEG VSRPTHFAGM LTVVAKLLQI AAPNVAYFGE KDYQQLTLIR QMVTDLNFDV 

       190        200        210        220        230        240 
RIFGVPTVRE HDGLALSSRN RYLDEAQRSA ATALSAALIA GAHAAAGGAE AILATAREVL 

       250        260        270        280        290        300 
ASVPEVEVDY LEVRGVDLGP APERGDGRLL VAAKVGTTRL IDNVGVAVGT GFLERDAEPP 

       310 
SDASAADELL SR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000431 Genomic DNA. Translation: ABG96201.1.
RefSeqYP_704359.1. NC_008268.1.

3D structure databases

ProteinModelPortalQ0S8D5.
SMRQ0S8D5. Positions 7-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING101510.RHA1_ro04415.

Proteomic databases

PRIDEQ0S8D5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG96201; ABG96201; RHA1_ro04415.
GeneID4221966.
KEGGrha:RHA1_ro04415.
PATRIC23207719. VBIRhoJos26306_4444.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycRJOS101510:GJJ1-4412-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_RHOSR
AccessionPrimary (citable) accession number: Q0S8D5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 53 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