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Q6N528 (PANC_RHOPA) 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:RPA3155
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [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_0000305532

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
Q6N528 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4D51B9A80DA2D665

FASTA28330,809
        10         20         30         40         50         60 
MSRPPVVART LPALRRALAE LRKRNASVAL VPTMGALHDG HLSLVRLAKR RADKVVVSVF 

        70         80         90        100        110        120 
VNPTQFAPHE DFGSYPRTFK ADASKLAEEN VDLIWNPDVK VMYPEGFASK ILTEAPAVAG 

       130        140        150        160        170        180 
LEDSFRPHFF GGVTTVVGKL FIQCRPDVAI FGSKDFQQLR VVTRMAADLD LGVKVIGAPT 

       190        200        210        220        230        240 
VRERDGLAMS SRNVYLSAEE RAIAPTLYRA MKEVAKRIKA GKTIASSLTA GAELITEAGF 

       250        260        270        280 
VLDYLEARHA ETLAPIKSPK EGPIRLLVAA KLGKTRLIDN IAV 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572603 Genomic DNA. Translation: CAE28596.1.
RefSeqNP_948494.1. NC_005296.1.

3D structure databases

ProteinModelPortalQ6N528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING258594.RPA3155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE28596; CAE28596; RPA3155.
GeneID2689631.
KEGGrpa:RPA3155.
PATRIC23290785. VBIRhoPal84835_3316.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHLGHITL.
OrthoDBEOG6Z6FZ4.
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...

Entry information

Entry namePANC_RHOPA
AccessionPrimary (citable) accession number: Q6N528
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 5, 2004
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