Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A0PV50 (PANC_MYCUA) 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:MUL_4184
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length315 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 – 315315Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305492

Regions

Nucleotide binding45 – 528ATP By similarity
Nucleotide binding163 – 1664ATP By similarity
Nucleotide binding200 – 2034ATP By similarity

Sites

Active site521Proton donor By similarity
Binding site771Beta-alanine By similarity
Binding site771Pantoate By similarity
Binding site1691Pantoate By similarity
Binding site1921ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PV50 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 9FF2B9FF0670E89C

FASTA31533,322
        10         20         30         40         50         60 
MRANAGRAPV FKPGELNVYS APRDVGEVSR ALRHTGRRVM LVPTMGALHE GHLALVRAAK 

        70         80         90        100        110        120 
RTPGAVVVVS IFVNPLQFGA GEDLDAYPRT LDQDLAKLRA EGVEIAFTPT AASMYPNGLR 

       130        140        150        160        170        180 
TTVQPGPMAA ELEGGSRPTH FAGVLTVVLK LLQIVAPDRA FFGEKDYQQL VLIRQMVADL 

       190        200        210        220        230        240 
NVNVQVIGVP IVREHDGLAM SSRNRYLDPA QREAAIALSA ALTAGAHAAT AGVQAALDAA 

       250        260        270        280        290        300 
RGVLEAVPGI VVDYVELRDG ELGPVSPSGS GRLLVAVRFG TTRLLDNVAI EIESIAGTDG 

       310 
QPVGPDGRVQ SPWRN 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL06219.1.
RefSeqYP_907690.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PV50.
SMRA0PV50. Positions 9-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_4184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL06219; ABL06219; MUL_4184.
GeneID4549749.
KEGGmul:MUL_4184.
PATRIC18176100. VBIMycUlc37413_4860.

Organism-specific databases

GenoListMUL_4184.
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_MYCUA
AccessionPrimary (citable) accession number: A0PV50
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 9, 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