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A1B2L1 (PANC_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:Pden_1658
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length282 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 – 282282Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305504

Regions

Nucleotide binding32 – 398ATP By similarity
Nucleotide binding149 – 1524ATP By similarity
Nucleotide binding186 – 1894ATP By similarity

Sites

Active site391Proton donor By similarity
Binding site631Beta-alanine By similarity
Binding site631Pantoate By similarity
Binding site1551Pantoate By similarity
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A1B2L1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 968B48FF0879AFA6

FASTA28230,473
        10         20         30         40         50         60 
MNAPIVRPLA ELRSMVRGWK SRGETIGVVP TMGALHEGHL SLVRAARASC DRVIVTLFVN 

        70         80         90        100        110        120 
PRQFNNTEDY AKYPRTEHTD AALLAPLGVD ALFVPDGDEV YPPDHATVIS VSGVTAPLEG 

       130        140        150        160        170        180 
AHRPGHFDGV ATVVTLLFNM TGADRAFFGE KDWQQLQLVR RLVQDLKLPV EIVPCPCVRA 

       190        200        210        220        230        240 
EDGLALSSRN QRLTAEGRTR AAALPRTLFE AARRIEAGAP TAEALAAAQE GLEAAGIGPV 

       250        260        270        280 
EYLELRDGET LGEPQLGRPA RLLVAAWLDG VRLIDNVAVT LR 

« Hide

References

[1]"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000489 Genomic DNA. Translation: ABL69755.1.
RefSeqYP_915451.1. NC_008686.1.

3D structure databases

ProteinModelPortalA1B2L1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_1658.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL69755; ABL69755; Pden_1658.
GeneID4579812.
KEGGpde:Pden_1658.
PATRIC22854391. VBIParDen97112_1584.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHAGHMEL.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-1676-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_PARDP
AccessionPrimary (citable) accession number: A1B2L1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 48 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