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A1SSG8 (PANC_PSYIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:Ping_0579
OrganismPsychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP]
Taxonomic identifier357804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPsychromonadaceaePsychromonas

Protein attributes

Sequence length289 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 – 289289Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305521

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding149 – 1524ATP By similarity
Nucleotide binding186 – 1894ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1551Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1SSG8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 33C9FD3623583E9C

FASTA28931,603
        10         20         30         40         50         60 
MLIIDNPQQL REKIKQLKQQ GSEIAFVPTM GNLHEGHLTL VQAGQKKAAV VIVSIFINPM 

        70         80         90        100        110        120 
QFNNAQDLLN YPKTMAQDCE KLAAAGVNII FTPAASSIYP NGLNAQTYVE VPLLSNCLEG 

       130        140        150        160        170        180 
ELRPGHFRGM STIVNKLFNL VQPDYACFGE KDFQQLAIVK QMVSDLGMPI EIIPVATMRE 

       190        200        210        220        230        240 
KNGLAMSSRN GKLSSLEKQK APLLAKVMNQ LAVDVQAQKT ELSILIDDAS IILNNAGFNT 

       250        260        270        280 
DAIHIVDAQT LQAVNCHSKE AVILMAAFLG ETRLIDNKVV ILNHSATKI 

« Hide

References

[1]"Complete sequence of Psychromonas ingrahamii 37."
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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000510 Genomic DNA. Translation: ABM02433.1.
RefSeqYP_942032.1. NC_008709.1.

3D structure databases

ProteinModelPortalA1SSG8.
SMRA1SSG8. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357804.Ping_0579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM02433; ABM02433; Ping_0579.
GeneID4624134.
KEGGpin:Ping_0579.
PATRIC23065981. VBIPsyIng103130_0638.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAQKDAQQF.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycPING357804:GJBJ-614-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_PSYIN
AccessionPrimary (citable) accession number: A1SSG8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 47 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