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Q6ALV3 (PANC_DESPS) 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:DP1943
OrganismDesulfotalea psychrophila (strain LSv54 / DSM 12343) [Complete proteome] [HAMAP]
Taxonomic identifier177439 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea

Protein attributes

Sequence length286 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 – 286286Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305439

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ALV3 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: B60772556745A8F4

FASTA28631,808
        10         20         30         40         50         60 
MKKISSRQEI REQVKKWQEQ GLTVALVPTM GCFHQGHLSL IKKGREIADR LIVSLFVNPI 

        70         80         90        100        110        120 
QFGPGEDLDA YPRPYEKDSR LAEELGTDVL FCPETTEMYG PNFQTNISVT TLTADLCGAG 

       130        140        150        160        170        180 
RPGHFDGVAT VVTKLFHLCQ PDFAIFGEKD FQQLAMIKQL VIDLDFDLQI ISCPIYREDD 

       190        200        210        220        230        240 
GLAMSSRNKY LNAEQRLKAL CLSQALEVAK DYVLARSAAG KTIESDEVIT KARGVIIDAG 

       250        260        270        280 
YEPEYISIVD QQTLEPSPTV QPGNVMALAV RIAERIRLID NSALLT 

« Hide

References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR522870 Genomic DNA. Translation: CAG36672.1.
RefSeqYP_065679.1. NC_006138.1.

3D structure databases

ProteinModelPortalQ6ALV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177439.DP1943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG36672; CAG36672; DP1943.
GeneID2947572.
KEGGdps:DP1943.
PATRIC21713840. VBIDesPsy67261_2113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAEIDYVEV.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycDPSY177439:GJW5-2007-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_DESPS
AccessionPrimary (citable) accession number: Q6ALV3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 13, 2004
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