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Q4LA34 (PANC_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:SH0182
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length283 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 – 283283Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128277

Regions

Nucleotide binding31 – 388ATP By similarity
Nucleotide binding148 – 1514ATP By similarity
Nucleotide binding185 – 1884ATP By similarity

Sites

Active site381Proton donor By similarity
Binding site621Beta-alanine By similarity
Binding site621Pantoate By similarity
Binding site1541Pantoate By similarity
Binding site1771ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4LA34 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: B4BAADAB5FD37F47

FASTA28331,756
        10         20         30         40         50         60 
MTKVIQTVSE MQQITQELKS TGKTIGFVPT MGALHEGHLS MMRRSVEEND ITVISVFVNP 

        70         80         90        100        110        120 
LQFGPNEDFD AYPRQIDQDV ALVEAINVDY VFHPAVEEMY PNELSVTLKV GRLAEVLEGA 

       130        140        150        160        170        180 
QRPGHFDGVV TVLNKLFNIV SPNKAYFGKK DAQQLAIVEK MVEDFNHPIQ IVGIDIVREE 

       190        200        210        220        230        240 
DGLARSSRNV YLTDDERQEA VHLSKSLEIA QTLYKQGERR SHIIVGEIKT YLSEHTSGHI 

       250        260        270        280 
DEVAIYSYPD LEVATEIQGQ IFISLAVKFS KARLIDNIIL GSE 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE03491.1.
RefSeqYP_252097.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4LA34.
SMRQ4LA34. Positions 3-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH0182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE03491; BAE03491; SH0182.
GeneID3482012.
KEGGsha:SH0182.
PATRIC19616399. VBIStaHae67511_0176.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAIVRDSDH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-184-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_STAHJ
AccessionPrimary (citable) accession number: Q4LA34
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: August 2, 2005
Last modified: May 14, 2014
This is version 60 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