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Q6G079 (PANC_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:BQ04310
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length286 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 – 286286Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128207

Regions

Nucleotide binding32 – 398ATP By similarity
Nucleotide binding149 – 1524ATP By similarity
Nucleotide binding186 – 1894ATP By similarity

Sites

Active site391Proton donor By similarity
Binding site631Beta-alanine By similarity
Binding site631Pantoate By similarity
Binding site1551Pantoate By similarity
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G079 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 738CCCEB2C532C9A

FASTA28632,469
        10         20         30         40         50         60 
MKIKVLKTIA EVRRYIAEER RLGFSIGFVP TMGALHEGHL ALVWRARAIC DRILVSIFVN 

        70         80         90        100        110        120 
PKQFGPHEDF DKYPRDLMAD CALLEKAGVE YVFAPSVEEM WPPGNETIVK VEKLSRILIG 

       130        140        150        160        170        180 
KLRPGHFCGV TSVVAKLFNI VQPDKAFFGE KDFQQILIVR RMVEDLAFPI EIVGVPILRE 

       190        200        210        220        230        240 
ADGVASSSRN QFLTLEERKA AKIIPESGKA AEKLYRQGER SVDKLCKIVR DILQQESRAI 

       250        260        270        280 
IEKIDLRDME TLSVVKGKLN KPAVLLLTVR FGKVRLIDQY ILQEKD 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF25930.1.
RefSeqYP_032111.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6G079.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ04310.

Proteomic databases

PRIDEQ6G079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF25930; CAF25930; BQ04310.
GeneID2867251.
KEGGbqu:BQ04310.
PATRIC31952115. VBIBarQui58630_0493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAFFGMKDA.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycBQUI283165:GHZA-430-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_BARQU
AccessionPrimary (citable) accession number: Q6G079
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 63 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