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A1VKS2 (PANC_POLNA) 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:Pnap_0933
OrganismPolaromonas naphthalenivorans (strain CJ2) [Complete proteome] [HAMAP]
Taxonomic identifier365044 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length283 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 – 283283Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305509

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding148 – 1514ATP By similarity
Nucleotide binding185 – 1884ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1541Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1VKS2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 39B78A134AB6AC04

FASTA28331,011
        10         20         30         40         50         60 
MHIVHTIAEL RQQLSGFKRP AFVPTMGNLH EGHIALVRQA RPLGDVTVSS IFVNRLQFAP 

        70         80         90        100        110        120 
HEDFDSYPRT LDADAERLEA AGCDVVFAPR EKDLYPEPQT FKVHPATDLS DILEGHFRPG 

       130        140        150        160        170        180 
FFIGVSTVVM KLFSCVFAGM PTGVAAFGKK DYQQVMVVRR LVQQFALPIE ILAGETQRAE 

       190        200        210        220        230        240 
DGLALSSRNS YLSPAERQEA VHLSRALRAL GEAARAATGQ PDLAALESQA LQALARRGWK 

       250        260        270        280 
PDYLTVRRRA DLAPPQGALA DVPLVVLGAA KLGNTRLIDN LEI 

« Hide

References

[1]"Complete sequence of chromosome 1 of Polaromonas naphthalenivorans CJ2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Madsen E.L., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CJ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000529 Genomic DNA. Translation: ABM36250.1.
RefSeqYP_981171.1. NC_008781.1.

3D structure databases

ProteinModelPortalA1VKS2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING365044.Pnap_0933.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM36250; ABM36250; Pnap_0933.
GeneID4689781.
KEGGpna:Pnap_0933.
PATRIC22946409. VBIPolNap76733_1762.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAEIDYVEV.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycPNAP365044:GJ8X-945-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_POLNA
AccessionPrimary (citable) accession number: A1VKS2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 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