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Q211R2 (PANC_RHOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. 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:RPC_3332
OrganismRhodopseudomonas palustris (strain BisB18) [Complete proteome] [HAMAP]
Taxonomic identifier316056 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

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.

Sequence caution

The sequence ABD88874.1 differs from that shown. Reason: Erroneous initiation.

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_0000305534

Regions

Nucleotide binding34 – 418ATP By similarity
Nucleotide binding152 – 1554ATP By similarity
Nucleotide binding189 – 1924ATP By similarity

Sites

Active site411Proton donor By similarity
Binding site651Beta-alanine By similarity
Binding site651Pantoate By similarity
Binding site1581Pantoate By similarity
Binding site1811ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q211R2 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 58A71EB5E1FB446E

FASTA28330,673
        10         20         30         40         50         60 
MSRSPVIVRT LPALRRALDT LRARNASLAL VPTMGALHDG HVSLVRLAKR RASKVAVSIF 

        70         80         90        100        110        120 
INPAQFAPNE DFAAYPRTWK ADLARLTAEK VDLIWNPDAK TMYPAGFASK ILTEGPALAG 

       130        140        150        160        170        180 
LEDRFRPQFF GGVTTVVGKL FAQVRPDLAL FGEKDFQQLR VVARMARDLD LGVKVVGAQI 

       190        200        210        220        230        240 
VRERDGLAMS SRNRYLSPEH RESATALCRG LKEAAKRIRA GEAIEAALAG SAALITAAGF 

       250        260        270        280 
KIDYLEARHA ETLAPVASRK DGPIRLLVAA TIGTTRLIDN VAV 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisB18."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisB18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000301 Genomic DNA. Translation: ABD88874.1. Different initiation.
RefSeqYP_533193.1. NC_007925.1.

3D structure databases

ProteinModelPortalQ211R2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316056.RPC_3332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD88874; ABD88874; RPC_3332.
GeneID3973442.
KEGGrpc:RPC_3332.
PATRIC23271470. VBIRhoPal29154_3419.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycRPAL316056:GH3E-3374-MONOMER.
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]
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_RHOPB
AccessionPrimary (citable) accession number: Q211R2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: June 11, 2014
This is version 48 of the entry and version 2 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