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P0A5R1 (PANC_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Mb3632c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length309 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 – 309309Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128242

Regions

Nucleotide binding40 – 478ATP By similarity
Nucleotide binding158 – 1614ATP By similarity
Nucleotide binding195 – 1984ATP By similarity

Sites

Active site471Proton donor By similarity
Binding site721Beta-alanine By similarity
Binding site721Pantoate By similarity
Binding site1641Pantoate By similarity
Binding site1871ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A5R1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: EB51DBE3485F970A

FASTA30932,678
        10         20         30         40         50         60 
MTIPAFHPGE LNVYSAPGDV ADVSRALRLT GRRVMLVPTM GALHEGHLAL VRAAKRVPGS 

        70         80         90        100        110        120 
VVVVSIFVNP MQFGAGEDLD AYPRTPDDDL AQLRAEGVEI AFTPTTAAMY PDGLRTTVQP 

       130        140        150        160        170        180 
GPLAAELEGG PRPTHFAGVL TVVLKLLQIV RPDRVFFGEK DYQQLVLIRQ LVADFNLDVA 

       190        200        210        220        230        240 
VVGVPTVREA DGLAMSSRNR YLDPAQRAAA VALSAALTAA AHAATAGAQA ALDAARAVLD 

       250        260        270        280        290        300 
AAPGVAVDYL ELRDIGLGPM PLNGSGRLLV AARLGTTRLL DNIAIEIGTF AGTDRPDGYR 


AILESHWRN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248346 Genomic DNA. Translation: CAD95818.1.
RefSeqNP_857271.1. NC_002945.3.

3D structure databases

ProteinModelPortalP0A5R1.
SMRP0A5R1. Positions 3-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb3632c.

Chemistry

BindingDBP0A5R1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD95818; CAD95818; Mb3632c.
GeneID1093343.
KEGGmbo:Mb3632c.
PATRIC18009701. VBIMycBov88188_3978.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAALHKGHQ.
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_MYCBO
AccessionPrimary (citable) accession number: P0A5R1
Secondary accession number(s): O06280
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 53 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