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A1WDW5 (PANC_VEREI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Veis_0029
OrganismVerminephrobacter eiseniae (strain EF01-2) [Complete proteome] [HAMAP]
Taxonomic identifier391735 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVerminephrobacter

Protein attributes

Sequence length280 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 – 280280Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305573

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1531Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WDW5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 2330BB083A05A6E6

FASTA28030,761
        10         20         30         40         50         60 
MLIARSIADL RQALAPYRHP AFVPTMGNLH DGHIALMRLA KPLGDVTVAS IFVNRLQFLP 

        70         80         90        100        110        120 
HEDFDSYPRT WEADCAQLQA VGCDLLFAPR EADLYPQPQT FKLHPDPALA DRLEGQFRPG 

       130        140        150        160        170        180 
FFVGVGTVVL KLFACVLGKT GGTAVFGKKD YQQLMVIRQM VQQLALPIEI VAGETCRAAD 

       190        200        210        220        230        240 
GLALSSRNGF LSLAERQEAV ALPLALQQLA RRWREARNPG PALEQQALDA LRARGWQPDY 

       250        260        270        280 
LTVCRRADLQ PATAQDAPGT LVALGAARLA TTRLIDNLEF 

« Hide

References

[1]"Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EF01-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000542 Genomic DNA. Translation: ABM55822.1.
RefSeqYP_994840.1. NC_008786.1.

3D structure databases

ProteinModelPortalA1WDW5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391735.Veis_0029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM55822; ABM55822; Veis_0029.
GeneID4693590.
KEGGvei:Veis_0029.
PATRIC24013326. VBIVerEis120356_0066.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMADYFEARH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycVEIS391735:GHY5-29-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_VEREI
AccessionPrimary (citable) accession number: A1WDW5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 49 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