Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q83ID9 (PANC_TROW8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:TW073
OrganismTropheryma whipplei (strain TW08/27) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier218496 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length288 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 – 288288Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305571

Regions

Nucleotide binding27 – 348ATP By similarity
Nucleotide binding181 – 1844ATP By similarity

Sites

Active site341Proton donor By similarity
Binding site581Beta-alanine By similarity
Binding site581Pantoate By similarity
Binding site1501Pantoate By similarity
Binding site1731ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83ID9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 041D1BA554EEFF76

FASTA28831,992
        10         20         30         40         50         60 
MNLKLASSPH ELRTCLAGRA FVLVPTMGAL HEGHIWLVDM ARRCNLPVVV SIFVNPLQFD 

        70         80         90        100        110        120 
DSLDLDTYPR TLEQDLEKLE GKAFAVYSPS VETMYPNGLD SIRIDPGPIG RILEGAIRPG 

       130        140        150        160        170        180 
FFDGILTIVA KLLLQTAPER VFFSKKDAQQ AFLVRRMVRE LAFPVRVEVT GFLRDKFSLP 

       190        200        210        220        230        240 
YSSRNRKLGV DAREKAQRLS QGLLSVVNNG PLTVRDCIDK ITDLANSIGV DLGYAQILDE 

       250        260        270        280 
NFCEIASDRM VTRAFHSEAC IGLNTPLFLL AARVHGVRVV DNVDLVVV 

« Hide

References

[1]"Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei."
Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G., Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A., Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J., Relman D.A.
Lancet 361:637-644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW08/27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX251410 Genomic DNA. Translation: CAD66760.1.
RefSeqNP_789023.1. NC_004551.1.

3D structure databases

ProteinModelPortalQ83ID9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218496.TW073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD66760; CAD66760; TW073.
GeneID1065020.
KEGGtws:TW073.
PATRIC23998460. VBITroWhi42739_0077.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAASSKENH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

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]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePANC_TROW8
AccessionPrimary (citable) accession number: Q83ID9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 62 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