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A0Q7L3 (PANC_FRATN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:FTN_1353
OrganismFrancisella tularensis subsp. novicida (strain U112) [Complete proteome] [HAMAP]
Taxonomic identifier401614 [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_0000305449

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
A0Q7L3 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: A9F111B587AF37A8

FASTA26129,709
        10         20         30         40         50         60 
MIIADNIKQL HSIRNSLIKQ QKIGFVPTMG ALHNGHISLI KKAKSENDVV IVSIFVNPTQ 

        70         80         90        100        110        120 
FNNPNDYQTY PNQLQQDIQI LESLDVDVLF 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 INSAGAKLQY IQKLNNRIFL 

       250        260 
AFYIGKVRLI DNFLKETGPS C 

« Hide

References

[1]"Comparison of Francisella tularensis genomes reveals evolutionary events associated with the emergence of human pathogenic strains."
Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y. expand/collapse author list , Chang J., Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.
Genome Biol. 8:R102.1-R102.16(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: U112.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000439 Genomic DNA. Translation: ABK90228.1.
RefSeqYP_898982.1. NC_008601.1.

3D structure databases

ProteinModelPortalA0Q7L3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING401614.FTN_1353.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK90228; ABK90228; FTN_1353.
GeneID4547910.
KEGGftn:FTN_1353.
PATRIC17935863. VBIFraNov128299_1388.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAKNIEQFN.
OrthoDBEOG6Z6FZ4.
ProtClustDBCLSK935002.

Enzyme and pathway databases

BioCycFNOV401614:GC4M-1352-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_FRATN
AccessionPrimary (citable) accession number: A0Q7L3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 47 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