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Q6ALV3 (PANC_DESPS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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 [Complete proteome] [HAMAP]
Taxonomic identifier84980 [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 MF_00158

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158

Subunit structure

Homodimer By similarity. HAMAP MF_00158

Subcellular location

Cytoplasm Potential HAMAP MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158

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-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Pantothenate synthetase HAMAP 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 

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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: 15305914] [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

HSSPHSSP built from PDB template 1IHO based on UniProtKB P31663.
ProteinModelPortalQ6ALV3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2947572.
GenomeReviewsGene locus DP1943 in contig CR522870_GR.
KEGGdps:DP1943.
NMPDRfig|177439.1.peg.1943.
PATRIC21713840. VBIDesPsy67261_2113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG428839.
OMAEMDGLAM.

Enzyme and pathway databases

BioCycDPSY177439:DP1943-MONOMER.

Family and domain databases

HAMAPMF_00158. PanC.
[Tree]
InterProIPR004821. Cyt_trans-rel.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01918.
PANTHERPTHR21299:SF1. Pantoate_ligase. 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: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families