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C5CWV0 (PANC_VARPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 32. 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:Vapar_4094
OrganismVariovorax paradoxus (strain S110) [Complete proteome] [HAMAP]
Taxonomic identifier543728 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVariovorax

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_1000203498

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding144 – 1474ATP By similarity
Nucleotide binding181 – 1844ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1501Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
C5CWV0 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: A02D1089C32DFF8C

FASTA28331,266
        10         20         30         40         50         60 
MYIAHTIDEL RSHLAAFRRP AFVPTMGNLH EGHLALVKQA KPLGDVTVAS IFVNRLQFLP 

        70         80         90        100        110        120 
HEDFDTYPRT WDSDCEKLRT AGCGVLFAPD EKALYPEPQT CKVHPDPALA DILEGHFRPG 

       130        140        150        160        170        180 
FFVGVCTVVM KLFQCVQPRV AVFGKKDYQQ LMMIRHMVRQ FALPIEIVGS ETFRADDGLA 

       190        200        210        220        230        240 
LSSRNGYLSE AERAEAVQLS KALKAMAQAV QAGERDLAAI EARAMQALAQ RGWQPDYLVL 

       250        260        270        280 
RRRSDLQAPS SANLAGEPLV ALAAARLGGT RLIDNLEIDA MPS 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile plant growth-promoting endophyte, Variovorax paradoxus S110."
Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G., O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C., Ovchinnikova G., Goodwin L., Han C.
J. Bacteriol. 193:1183-1190(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001635 Genomic DNA. Translation: ACS20707.1.
RefSeqYP_002945973.1. NC_012791.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING543728.Vapar_4094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS20707; ACS20707; Vapar_4094.
GeneID7974416.
KEGGvap:Vapar_4094.
PATRIC24008677. VBIVarPar36677_4119.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHLGHITL.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycVPAR543728:GHLL-4132-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_VARPS
AccessionPrimary (citable) accession number: C5CWV0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 32 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