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Q2S2P6 (PANC_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:SRU_1411
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP]
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length295 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
Reference 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 – 295295Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305543

Regions

Nucleotide binding154 – 1574ATP By similarity
Nucleotide binding191 – 1944ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1601Pantoate By similarity
Binding site1831ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S2P6 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 94B96E99F9190ABC

FASTA29532,106
        10         20         30         40         50         60 
MELLRTVDAM QAQADAARAE GQTLALVPTL GALHEGHLAL VRRALNEADH VTVSVFVNPT 

        70         80         90        100        110        120 
QFGPGEDYDD YPRDLEGDRE TLEALDVDAM FAPSVEEMYP YADDEALPGP LAWVDVERLD 

       130        140        150        160        170        180 
EHLCGAYREG HFRGVTTVVT KLFHACKPDV AVFGRKDAQQ YVILQRLVED LLFDIEIVGV 

       190        200        210        220        230        240 
PTVREPDGLA QSSRNEYLDP EEREQATVLY AAVTAAEEAI EGGEQAAEGV VGAMENELAA 

       250        260        270        280        290 
APDADVQYAE VVDAHTLQPV DHLVPGQEVL AAVAVFFGET RLIDNTFVQV PPAQA 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC43779.1.
RefSeqYP_445535.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S2P6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_1411.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC43779; ABC43779; SRU_1411.
GeneID3850341.
KEGGsru:SRU_1411.
PATRIC23425253. VBISalRub86502_1466.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHLGHITL.
OrthoDBEOG6Z6FZ4.
PhylomeDBQ2S2P6.
ProtClustDBCLSK2773634.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-1408-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_SALRD
AccessionPrimary (citable) accession number: Q2S2P6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 57 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