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B6J9H9 (PANC_COXB1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:CbuK_1645
OrganismCoxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)) [Complete proteome] [HAMAP]
Taxonomic identifier434924 [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_1000097053

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
B6J9H9 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 2A8DD0535687A595

FASTA25729,479
        10         20         30         40         50         60 
MTKVIEALSD WQSIRKTIND LSVGFVPTMG NLHAGHLSLL ERSKCENTIT VLSLFINPTQ 

        70         80         90        100        110        120 
FNDKNDFKNY 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: CbuK_Q154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001020 Genomic DNA. Translation: ACJ20793.1.
RefSeqYP_002305938.1. NC_011528.1.

3D structure databases

ProteinModelPortalB6J9H9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434924.CbuK_1645.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ20793; ACJ20793; CbuK_1645.
GeneID7016158.
KEGGcbc:CbuK_1645.
PATRIC17918756. VBICoxBur77120_1662.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OrthoDBEOG6Z6FZ4.
ProtClustDBCLSK914057.

Enzyme and pathway databases

BioCycCBUR434924:GHWU-1641-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_COXB1
AccessionPrimary (citable) accession number: B6J9H9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 33 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