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A1WUU4 (PANC_HALHL) 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:Hhal_0674
OrganismHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]
Taxonomic identifier349124 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira

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_0000305462

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
A1WUU4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 087F1BBE1BC89E2F

FASTA28531,430
        10         20         30         40         50         60 
MRQVTERNAM RELSRAWRAR GERIGLVPTM GNLHRGHLEL VERLARRVDR LVVSIFVNPL 

        70         80         90        100        110        120 
QFGPGEDYDA YPRTLEADLN ALEGRGVDAV FAPNAREMYP GVEPPWTGVD VPALTQTLCG 

       130        140        150        160        170        180 
AARPGHFAGV AVVVIKLLNI VEPDVAAFGR KDYQQLQVIR RVVGDLDLSV EIVEVPIVRE 

       190        200        210        220        230        240 
ADGLALSSRN GYMDGEQRRR APALYATLCE VAAALEAGRR DWSQLEAQAC RRLEAAGFDA 

       250        260        270        280 
AEYVAVRRCD DLAEPQGDEP RLVCLGAARL GAARLIDNVE ARLKR 

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000544 Genomic DNA. Translation: ABM61456.1.
RefSeqYP_001002258.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WUU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349124.Hhal_0674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM61456; ABM61456; Hhal_0674.
GeneID4710190.
KEGGhha:Hhal_0674.
PATRIC22095655. VBIHalHal112047_0684.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAIVRDSDH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycHHAL349124:GI3I-693-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_HALHL
AccessionPrimary (citable) accession number: A1WUU4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 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