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Q04S98 (PANC_LEPBJ) 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:LBJ_1667
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length285 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 – 285285Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305472

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding148 – 1514ATP By similarity
Nucleotide binding185 – 1884ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1541Pantoate By similarity
Binding site1771ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04S98 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 83414C3FD0AD15EB

FASTA28532,038
        10         20         30         40         50         60 
MIICRTPEEI SVQVRRWKAE DKKVGFVPTM GYLHEGHASL FRECLSKADK TVVSIFVNPA 

        70         80         90        100        110        120 
QFNDPEDYAK YPINTDGDLK ICESGKVDLV FLPEKETIYP EGIPNVVLQV PHLMRNLCAV 

       130        140        150        160        170        180 
SRPGHFEGVL LVISRLFHFV KPDFAFFGKK DYQQYLLVKE FCKILAFPVE VIGCETIRSD 

       190        200        210        220        230        240 
KGLALSSRNS RLSEDEKEES LLISRALKLG EAQILSGIKD PVVVRDIMKD VLDSSPKIRL 

       250        260        270        280 
DYLEVLNADT LESLEILEGN ILLAAAVFIG SVRLIDNRTL RVASV 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000350 Genomic DNA. Translation: ABJ76222.1.
RefSeqYP_800980.1. NC_008510.1.

3D structure databases

ProteinModelPortalQ04S98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355277.LBJ_1667.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ76222; ABJ76222; LBJ_1667.
GeneID4410795.
KEGGlbj:LBJ_1667.
PATRIC22358853. VBILepBor13265_2138.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAEIDYVEV.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycLBOR355277:GHYM-1647-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_LEPBJ
AccessionPrimary (citable) accession number: Q04S98
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: November 14, 2006
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