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Q135F0 (PANC_RHOPS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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:RPD_3063
OrganismRhodopseudomonas palustris (strain BisB5) [Complete proteome] [HAMAP]
Taxonomic identifier316057 [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.

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_0000305535

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
Q135F0 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 6CB7EE7A64882E21

FASTA28330,747
        10         20         30         40         50         60 
MARPPVVART LPALRRALGD LRRRNASVAL VPTMGALHDG HLSLVRLAKR RATKVVVSVF 

        70         80         90        100        110        120 
VNPTQFAPHE DFGSYPRTWK ADASKLAAEG VDLIWNPDVK TMYPEGFATR IEVDGPAVAG 

       130        140        150        160        170        180 
LEDRFRPHFF GGVATVVGKL FLQVRPDVAI FGSKDFQQLR VVTRMAGDLD TGVKVIGAPT 

       190        200        210        220        230        240 
IRERDGLAMS SRNVYLTPEE RQVAPTLYRA MKETAKQLRA GKSADASLSV GAKMITAAGF 

       250        260        270        280 
SLDYFEARHA DTLAPIHSLK AGPIRLLVAA KLGKTRLIDN VAV 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisB5."
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., Lykidis A., 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: BisB5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000283 Genomic DNA. Translation: ABE40289.1.
RefSeqYP_570190.1. NC_007958.1.

3D structure databases

ProteinModelPortalQ135F0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316057.RPD_3063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE40289; ABE40289; RPD_3063.
GeneID4023566.
KEGGrpd:RPD_3063.
PATRIC23281197. VBIRhoPal120395_3161.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMADYFEARH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycRPAL316057:GHDC-3112-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_RHOPS
AccessionPrimary (citable) accession number: Q135F0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 31, 2006
Last modified: June 11, 2014
This is version 50 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