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

Q8Z9D3 (PANC_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. 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:STY0199, t0182
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length284 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 – 284284Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128265

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
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Z9D3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 59827C75052ADD61

FASTA28431,849
        10         20         30         40         50         60 
MLIIETLPLL RQHIRRLRQE GKRVALVPTM GNLHDGHMKL VDEAKARADV VIVSIFVNPM 

        70         80         90        100        110        120 
QFDRPDDLVR YPRTLQEDCE KLNKRKVDYV FAPAVEEIYP QGLEGQTYVD VPGLSTMLEG 

       130        140        150        160        170        180 
TSRPGHFRGV STIVSKLFNL IQPDIACFGE KDFQQLALIR KMVADMGYDI EIVGVPIIRA 

       190        200        210        220        230        240 
KDGLALSSRN AYLTAEQRKI APGLYNVMNS IAEKLIAGNR ELQEIIAIAE QELNEKGFRA 

       250        260        270        280 
DDIQIRDADT LLELTETSKR AVILAAAWLG QARLIDNQSV TLAQ 

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513382 Genomic DNA. Translation: CAD01335.1.
AE014613 Genomic DNA. Translation: AAO67914.1.
RefSeqNP_454790.1. NC_003198.1.
NP_804065.1. NC_004631.1.

3D structure databases

ProteinModelPortalQ8Z9D3.
SMRQ8Z9D3. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220341.STY0199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO67914; AAO67914; t0182.
CAD01335; CAD01335; CAD01335.
GeneID1246693.
PATRIC18538220. VBISalEnt120419_0202.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAQKDAQQF.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

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_SALTI
AccessionPrimary (citable) accession number: Q8Z9D3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 77 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