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A4F6T0 (PANC_SACEN) 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:SACE_0406
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

Protein attributes

Sequence length302 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 – 302302Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305542

Regions

Nucleotide binding47 – 548ATP By similarity
Nucleotide binding165 – 1684ATP By similarity
Nucleotide binding202 – 2054ATP By similarity

Sites

Active site541Proton donor By similarity
Binding site791Beta-alanine By similarity
Binding site791Pantoate By similarity
Binding site1711Pantoate By similarity
Binding site1941ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A4F6T0 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: DAB95294C26C3930

FASTA30232,264
        10         20         30         40         50         60 
MTAPERVGAG PGFAPGALTV HHHPDELAKV TRALRATGRR ITLVPTMGAL HEGHLELIRR 

        70         80         90        100        110        120 
ARRDSNSVVV VSIFVNPLQF GPGEDFTSYP RTFETDVEAC RAEGVELVFA PDRDDVYGPD 

       130        140        150        160        170        180 
PQITVHPGPL GDELEGASRP GHFAGVLTIV AKLLGIVRPD LALFGEKDYQ QLVLIRRMAR 

       190        200        210        220        230        240 
ELNIDTAIQG IPIVRAPDGL ALSSRNVYLS EEERGAALAL SAALAAGAHA GREGAEAVLR 

       250        260        270        280        290        300 
AAREVLATEP LVRLDYLELR DTELGAAPAE GEARLLVAAK VGETRLIDNA LVLLGDQGDS 


RP 

« Hide

References

[1]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NRRL 23338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM420293 Genomic DNA. Translation: CAL99754.1.
RefSeqYP_001102680.1. NC_009142.1.

3D structure databases

ProteinModelPortalA4F6T0.
SMRA4F6T0. Positions 11-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405948.SACE_0406.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL99754; CAL99754; SACE_0406.
GeneID4940273.
KEGGsen:SACE_0406.
PATRIC23408182. VBISacEry28377_0412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

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_SACEN
AccessionPrimary (citable) accession number: A4F6T0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: April 17, 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