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Q8ZRR1 (PANC_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:STM0181
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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_0000128266

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

Secondary structure

1 .................................................. 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZRR1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 219D5B538BE37E1D

FASTA28431,858
        10         20         30         40         50         60 
MLIIETLPLL RQHIRRLRQE GKRVALVPTM GNLHDGHMKL VDEAKARADV VIVSIFVNPM 

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

       130        140        150        160        170        180 
ASRPGHFRGV STIVSKLFNL IQPDIACFGE KDFQQLALIR KMVADMSYDI 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 Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006468 Genomic DNA. Translation: AAL19145.1.
RefSeqNP_459186.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MUEX-ray2.70A/B/C/D1-284[»]
ProteinModelPortalQ8ZRR1.
SMRQ8ZRR1. Positions 1-282.
ModBaseSearch...

Protein-protein interaction databases

STRING99287.STM0181.

Proteomic databases

PaxDbQ8ZRR1.
PRIDEQ8ZRR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19145; AAL19145; STM0181.
GeneID1251699.
KEGGstm:STM0181.
PATRIC32378643. VBISalEnt20916_0191.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAHTIVSVF.
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...

Other

EvolutionaryTraceQ8ZRR1.

Entry information

Entry namePANC_SALTY
AccessionPrimary (citable) accession number: Q8ZRR1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 67 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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