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

Q3ZXF9 (PANC_DEHMC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:cbdbA782
OrganismDehalococcoides mccartyi (strain CBDB1) [Complete proteome] [HAMAP]
Taxonomic identifier255470 [NCBI]
Taxonomic lineageBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

Protein attributes

Sequence length268 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 – 268268Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305436

Regions

Nucleotide binding18 – 258ATP By similarity
Nucleotide binding135 – 1384ATP By similarity
Nucleotide binding172 – 1754ATP By similarity

Sites

Active site251Proton donor By similarity
Binding site491Beta-alanine By similarity
Binding site491Pantoate By similarity
Binding site1411Pantoate By similarity
Binding site1641ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ZXF9 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: A33EE7CB26AE51E5

FASTA26830,386
        10         20         30         40         50         60 
MKKLHREICG PVGLVPTMGY LHEGHLSLVR ASKKQDINTV ASIFVNPTQF GPHEDFKKYP 

        70         80         90        100        110        120 
RDEKRDMAML ENTGVDYVFV PSVEDMYPAG FDSWVEPGIL QQCLEGAVRP GHFRGVCTVV 

       130        140        150        160        170        180 
AKLFTIIRPD RAYFGQKDYQ QYLIIKRMAS DLNLDVSVEM LPIIRENDGL ALSSRNTYLS 

       190        200        210        220        230        240 
PAERQAALVL YRSLLTARSL FDEKEHRAEV IRKKMTDVIQ HESMAEIDYV SLSHQDTLCE 

       250        260 
SDEVSAKTIA LVAARFGKTR LIDNMFLA 

« Hide

References

[1]"Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1."
Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.
Nat. Biotechnol. 23:1269-1273(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CBDB1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ965256 Genomic DNA. Translation: CAI82936.1.
RefSeqYP_307852.1. NC_007356.1.

3D structure databases

ProteinModelPortalQ3ZXF9.
SMRQ3ZXF9. Positions 8-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING255470.cbdb_A782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI82936; CAI82936; cbdbA782.
GeneID3623296.
KEGGdeh:cbdb_A782.
PATRIC21611655. VBIDehSp125902_0663.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
KOK01918.
OMAGDGHETW.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycDSP255470:GJXW-675-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_DEHMC
AccessionPrimary (citable) accession number: Q3ZXF9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 27, 2005
Last modified: May 14, 2014
This is version 56 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