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A0QA93 (PANC_MYCA1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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:MAV_0551
OrganismMycobacterium avium (strain 104) [Complete proteome] [HAMAP]
Taxonomic identifier243243 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length308 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 – 308308Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305485

Regions

Nucleotide binding39 – 468ATP By similarity
Nucleotide binding157 – 1604ATP By similarity
Nucleotide binding194 – 1974ATP By similarity

Sites

Active site461Proton donor By similarity
Binding site711Beta-alanine By similarity
Binding site711Pantoate By similarity
Binding site1631Pantoate By similarity
Binding site1861ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QA93 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 951D38A77E023859

FASTA30832,767
        10         20         30         40         50         60 
MKPAFTAGEL NTYTSPGDVT AVSRALRHTG RRVMLVPTMG ALHDGHLALV RAAKRVPGSV 

        70         80         90        100        110        120 
VVVSIFVNPL QFSAGEDLDA YPRTLDDDLA LLRSEGVEIA FTPTAAAMYP NGLRTTVQPG 

       130        140        150        160        170        180 
PLAAELEGGP RPTHFAGVLT VVCKLLQIVR PDRIFFGEKD YQQLVMIRQM VADLNIDVQV 

       190        200        210        220        230        240 
VGVPTVREAD GLAMSSRNRY LDATQRELAV TLSAALTAGA HAAHLGGAAA LRAARAVLDA 

       250        260        270        280        290        300 
VPELTVDYLE LRDAGLGPAP AHGSARLLVA ARLGNTRLLD NIEMQIETPA GTAGPDGDRQ 


YAQSPWRN 

« 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: 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000479 Genomic DNA. Translation: ABK64754.1.
RefSeqYP_879831.1. NC_008595.1.

3D structure databases

ProteinModelPortalA0QA93.
SMRA0QA93. Positions 3-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243243.MAV_0551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK64754; ABK64754; MAV_0551.
GeneID4528629.
KEGGmav:MAV_0551.
PATRIC17982838. VBIMycAvi38287_0532.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycMAVI243243:GH3Y-551-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_MYCA1
AccessionPrimary (citable) accession number: A0QA93
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 9, 2007
Last modified: June 11, 2014
This is version 50 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