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Q5HWH4 (PANC_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:CJE0342
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length282 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 – 282282Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128217

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding146 – 1494ATP By similarity
Nucleotide binding183 – 1864ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site601Beta-alanine By similarity
Binding site601Pantoate By similarity
Binding site1521Pantoate By similarity
Binding site1751ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HWH4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: B72B528DECE36CBD

FASTA28231,951
        10         20         30         40         50         60 
MEVITSIKEA KQTVKNWKSH NLSIGYVPTM GFLHDGHLSL VKNAKTQDKV IVSIFVNPMQ 

        70         80         90        100        110        120 
FGPNEDFSSY PRDLERDIKM CQDNGVDMVF IPDAAQMYLK NFSTYVDMNT ITDKLCGAKR 

       130        140        150        160        170        180 
LGHFRGVCTV LAKFFNILNP DIVYMGQKDA QQCVVVRHMV DDLNFDLKIQ ICPIIREEDG 

       190        200        210        220        230        240 
LAKSSRNVYL SEEERKASLA ISQSIFLAEK LVQEGEKDTS KIIQAMKDIL EKEKLIKIDY 

       250        260        270        280 
IELVDFNTME NIKNIADNVL GAVAAFVGKT RLIDNFLVQG LK 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW34931.1.
RefSeqYP_178361.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HWH4.
SMRQ5HWH4. Positions 1-278.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE0342.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW34931; AAW34931; CJE0342.
GeneID3231104.
KEGGcjr:CJE0342.
PATRIC20042388. VBICamJej134361_0343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAHAGHMEL.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-347-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_CAMJR
AccessionPrimary (citable) accession number: Q5HWH4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 59 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