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A7FM23 (PANC_YERP3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:YpsIP31758_3344
OrganismYersinia pseudotuberculosis serotype O:1b (strain IP 31758) [Complete proteome] [HAMAP]
Taxonomic identifier349747 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia ›

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.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP-Rule MF_00158

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: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000097132

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
A7FM23 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 77642582E034FA7F

FASTA28431,730
        10         20         30         40         50         60 
MLIIETLPLL RQQIRRWRQE GKRIALVPTM GNLHEGHMTL VDEAKTRADV VVVTIFVNPL 

        70         80         90        100        110        120 
QFERPDDLAH YPRTLQEDCE KLTRHGADLV FAPAAADIYP AGLEKQTYVD VPALSTILEG 

       130        140        150        160        170        180 
ASRPGHFRGV STIVSKLFNL IQPDVACFGE KDYQQLALIR KMVADMGYDI NIVGVPTVRA 

       190        200        210        220        230        240 
KDGLALSSRN GYLTEEERQI APQLSKIMWA LAEKMALGER QIDALLEDAA AQLLRAGFTP 

       250        260        270        280 
DELFIRDAET LQPLTVDSQQ AVILMAAWLG KARLIDNQLV DLRH

« Hide

References

[1]"The complete genome sequence of Yersinia pseudotuberculosis IP31758, the causative agent of Far East scarlet-like fever."
Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., Fayolle C., Lindler L.E., Carniel E., Ravel J.
PLoS Genet. 3:1508-1523(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP 31758.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000720 Genomic DNA. Translation: ABS47537.1.
RefSeqYP_001402301.1. NC_009708.1.

3D structure databases

ProteinModelPortalA7FM23.
SMRA7FM23. Positions 1-282.
ModBaseSearch...

Protein-protein interaction databases

STRING349747.YpsIP31758_3344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS47537; ABS47537; YpsIP31758_3344.
GeneID5385613.
KEGGypi:YpsIP31758_3344.
PATRIC18635857. VBIYerPse15693_3837.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHTIVSVF.
ProtClustDBPRK00380.

Enzyme and pathway databases

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_YERP3
AccessionPrimary (citable) accession number: A7FM23
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 11, 2007
Last modified: May 1, 2013
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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