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Q14GL0 (PANC_FRAT1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:FTF1390
OrganismFrancisella tularensis subsp. tularensis (strain FSC 198) [Complete proteome] [HAMAP]
Taxonomic identifier393115 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length261 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 – 261261Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305451

Regions

Nucleotide binding29 – 368ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site361Proton donor By similarity
Binding site601Beta-alanine By similarity
Binding site601Pantoate By similarity
Binding site1531Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q14GL0 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 9EF115B43EDC2FDE

FASTA26129,715
        10         20         30         40         50         60 
MIIADNIKQF HSIRNSLIKQ QKIGFVPTMG ALHNGHISLI KKAKSENDVV IVSIFVNPTQ 

        70         80         90        100        110        120 
FNNPNDYQTY PNQLQQDIQI LASLDVDVLF NPSEKDIYPD GNLLRIEPKL EIANILEGKS 

       130        140        150        160        170        180 
RPGHFSGMLT VVLKLLQITK PNNLYLGEKD YQQVMLIKQL VKDFFINTKI IVCPTQRQPS 

       190        200        210        220        230        240 
GLPLSSRNKN LTSTDIEIAN KIYEILRQDD FSNLEELTNK INSTGAKLQY IQKLNNRIFL 

       250        260 
AFYIGKVRLI DNFLKETGPS C 

« Hide

References

[1]"Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FSC 198.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286280 Genomic DNA. Translation: CAL09406.1.
RefSeqYP_667467.1. NC_008245.1.

3D structure databases

ProteinModelPortalQ14GL0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393115.FTF1390.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL09406; CAL09406; FTF1390.
GeneID4200091.
KEGGftf:FTF1390.
PATRIC17961902. VBIFraTul133500_1599.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAAYMGSTR.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycFTUL393115:GJUT-1421-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_FRAT1
AccessionPrimary (citable) accession number: Q14GL0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 55 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