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

Q0T868 (PANC_SHIF8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:SFV_0123
OrganismShigella flexneri serotype 5b (strain 8401) [Complete proteome] [HAMAP]
Taxonomic identifier373384 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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_0000305553

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

Sequences

Sequence LengthMass (Da)Tools
Q0T868 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 40E4647C6B3AFB20

FASTA28331,597
        10         20         30         40         50         60 
MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHNGHMKL VDEAKARADV VVVSIFVNPM 

        70         80         90        100        110        120 
QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP NGTETHTYVD VPGLSTMLEG 

       130        140        150        160        170        180 
ASRPGHFRGV STIVSKLFNL VQPDIACFGE KDFQQLALIR KMVADMGFDI EIVGVPIMRA 

       190        200        210        220        230        240 
KDGLALSSRN GYLTAEQRKI APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA 

       250        260        270        280 
DDIQIRDADT LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA 

« Hide

References

[1]"Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a."
Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.
BMC Genomics 7:173-173(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8401.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000266 Genomic DNA. Translation: ABF02408.1.
RefSeqYP_687713.1. NC_008258.1.

3D structure databases

ProteinModelPortalQ0T868.
SMRQ0T868. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING373384.SFV_0123.

Proteomic databases

PRIDEQ0T868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF02408; ABF02408; SFV_0123.
GeneID4210145.
KEGGsfv:SFV_0123.
PATRIC18723172. VBIShiFle33408_0143.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAECPIVRE.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycSFLE373384:GHZM-122-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_SHIF8
AccessionPrimary (citable) accession number: Q0T868
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 54 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