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A0R580 (PANC_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 54. 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:MSMEG_6097, MSMEI_5938
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
Reference 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 – 314314Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305487

Regions

Nucleotide binding43 – 508ATP By similarity
Nucleotide binding161 – 1644ATP By similarity
Nucleotide binding198 – 2014ATP By similarity

Sites

Active site501Proton donor By similarity
Binding site751Beta-alanine By similarity
Binding site751Pantoate By similarity
Binding site1671Pantoate By similarity
Binding site1901ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0R580 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: AABE76E46E7E96AF

FASTA31433,525
        10         20         30         40         50         60 
MTISRTPKFS AGELNVYSAP ADVAAVTRAL RTAGRRIVLV PTMGALHEGH LTLVRAAKRT 

        70         80         90        100        110        120 
PGAVVVVSIF VNPLQFGPNE DLNAYPRTLE DDLTALRAEG VEIVFTPTGS DMYPDGTRTS 

       130        140        150        160        170        180 
VHPGPLGDDL EGSSRPGHFA GVLTVVLKLF SIVRPDRAYF GEKDYQQLTL LRQMVADLNV 

       190        200        210        220        230        240 
DVQIVGVPTV RESDGLALSS RNRYLDKDQR EQAGALSAAL LAGKYAAAGG AEAALDAARA 

       250        260        270        280        290        300 
VLDEVPALEV DYLQVRDPML GPAPAEGQAR LLVAARLGRT RLIDNIAIDV GASAGIDGHP 

       310 
RVGNDQNHEL PWRN 

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK70073.1.
CP001663 Genomic DNA. Translation: AFP42371.1.
RefSeqYP_006570666.1. NC_018289.1.
YP_890318.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0R580.
SMRA0R580. Positions 7-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_6097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK70073; ABK70073; MSMEG_6097.
AFP42371; AFP42371; MSMEI_5938.
GeneID4531246.
KEGGmsg:MSMEI_5938.
msm:MSMEG_6097.
PATRIC18084433. VBIMycSme59918_5936.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-6096-MONOMER.
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]
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_MYCS2
AccessionPrimary (citable) accession number: A0R580
Secondary accession number(s): I7GFF1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 54 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