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A9L2H4 (PANC_SHEB9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Sbal195_0879
OrganismShewanella baltica (strain OS195) [Complete proteome] [HAMAP]
Taxonomic identifier399599 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length281 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 – 281281Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000097110

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
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A9L2H4 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: E90FBFDE901C0B42

FASTA28130,448
        10         20         30         40         50         60 
MITSAHIDDI RTQVRAWRAK GETVAFVPTM GNLHQGHITL VKEAASKCDH VVASIFVNPM 

        70         80         90        100        110        120 
QFGQNEDLDA YPRTLAADSE ALTAAGAELL FTPTPAVMYP KGLEQQTYVE VPGISNVLCG 

       130        140        150        160        170        180 
ASRPGHFRGV ATIVCKLFNI VQPDVALFGN KDYQQLLVIK TMVEDLSLPI EIIGVDTIRE 

       190        200        210        220        230        240 
DSGLAMSSRN GYLTAAEKAA APALKQAIDA MAAGIKQGES FEQMTEQAKA CLVAAGFTPD 

       250        260        270        280 
YLEIRHAHTL EQAQNQDHAL VILAAAYIGK ARLIDNLRFD R 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS195."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS195.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000891 Genomic DNA. Translation: ABX48056.1.
RefSeqYP_001553316.1. NC_009997.1.

3D structure databases

ProteinModelPortalA9L2H4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399599.Sbal195_0879.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX48056; ABX48056; Sbal195_0879.
GeneID5752600.
KEGGsbn:Sbal195_0879.
PATRIC23467769. VBISheBal33754_0909.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAHLGHITL.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycSBAL399599:GH6B-908-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_SHEB9
AccessionPrimary (citable) accession number: A9L2H4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: February 19, 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