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A8ERB8 (PANC_ARCB4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Abu_0215
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

Protein attributes

Sequence length272 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 – 272272Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000076837

Regions

Nucleotide binding27 – 348ATP By similarity
Nucleotide binding143 – 1464ATP By similarity
Nucleotide binding180 – 1834ATP By similarity

Sites

Active site341Proton donor By similarity
Binding site581Beta-alanine By similarity
Binding site581Pantoate By similarity
Binding site1491Pantoate By similarity
Binding site1721ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A8ERB8 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 27DF86B08536B23E

FASTA27230,807
        10         20         30         40         50         60 
MQVLKTIEEL QNIRKNSLGK VGLVPTMGAL HNGHISLIKQ ARNENDIVIV SIFVNPTQFL 

        70         80         90        100        110        120 
PGEDLDAYPR RDEADKKICQ MCKVNYVFMP EISTMYTKEE VLVKAPNKSY ILEGKTRPGH 

       130        140        150        160        170        180 
FDGVLQVVLK LFNLTQPTNA YFGKKDAQQL TLIQQMVKNF FLPINIVPCD IVREEDGLAL 

       190        200        210        220        230        240 
SSRNIYLNPT QRKDALLISK SLYMAGSLIS SGERSVKAVK DKIYEVMSIL DVEYVAIVDK 

       250        260        270 
EFNELETIEP TNTIILVVAR FGNTRLLDNI WL 

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM4018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000361 Genomic DNA. Translation: ABV66492.1.
RefSeqYP_001489161.1. NC_009850.1.

3D structure databases

ProteinModelPortalA8ERB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING367737.Abu_0215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV66492; ABV66492; Abu_0215.
GeneID5623748.
KEGGabu:Abu_0215.
PATRIC20961788. VBIArcBut20197_0207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAIHTIREL.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycABUT367737:GHWO-215-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_ARCB4
AccessionPrimary (citable) accession number: A8ERB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 46 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