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A9KEG8 (PANC_COXBN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:CBUD_1650
OrganismCoxiella burnetii (strain Dugway 5J108-111) [Complete proteome] [HAMAP]
Taxonomic identifier434922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length257 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 – 257257Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000097055

Regions

Nucleotide binding29 – 368ATP By similarity
Nucleotide binding145 – 1484ATP By similarity
Nucleotide binding182 – 1854ATP By similarity

Sites

Active site361Proton donor By similarity
Binding site601Beta-alanine By similarity
Binding site601Pantoate By similarity
Binding site1511Pantoate By similarity
Binding site1741ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KEG8 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: A885741FB0CD01D9

FASTA25729,478
        10         20         30         40         50         60 
MTKVIEALSD WQSIRKTIND LSVGFVPTMG NLHAGHLSLL ERSKCENTIT VLSLFINPTQ 

        70         80         90        100        110        120 
FNNKNDFKNY PRTLAQDIAM AEENGIDYVL APTDDALYPD QYAYKITNST INNQEAEFRP 

       130        140        150        160        170        180 
RHFDGVLTVV MKLLLLVKPT RAYFGEKDYQ QLQLVKGLAE AFFLDTEIIG CKIVRNEFGL 

       190        200        210        220        230        240 
PLSSRNRRLT EDQYQLAQRF SEIFHSDLSC DEIKNALIQE GIIVDYIEDY NERRFAAVHV 

       250 
GDIRLIDNIP FAKDKKC 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Dugway 5J108-111.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000733 Genomic DNA. Translation: ABS77519.1.
RefSeqYP_001424988.1. NC_009727.1.

3D structure databases

ProteinModelPortalA9KEG8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434922.CBUD_1650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS77519; ABS77519; CBUD_1650.
GeneID5457695.
KEGGcbd:CBUD_1650.
PATRIC17923114. VBICoxBur32972_1647.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAIADFRQW.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycCBUR434922:GJTP-1747-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]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_COXBN
AccessionPrimary (citable) accession number: A9KEG8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 47 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