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Q6ACQ8 (PANC_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Lxx21410
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length287 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 – 287287Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305471

Regions

Nucleotide binding37 – 448ATP By similarity
Nucleotide binding154 – 1574ATP By similarity
Nucleotide binding191 – 1944ATP By similarity

Sites

Active site441Proton donor By similarity
Binding site681Beta-alanine By similarity
Binding site681Pantoate By similarity
Binding site1601Pantoate By similarity
Binding site1831ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ACQ8 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 49320EEA1D496D80

FASTA28730,061
        10         20         30         40         50         60 
MTVIACLREI LSTARRTAVA EGASDAPASR VVLVPTMGAL HEGHVRLVNH ARDLGGIVVV 

        70         80         90        100        110        120 
SIFVNPLQFG PGEDLDRYPR TLDADVALLD GLADVVFAPA AAEMYPQGES STRVTAGAVG 

       130        140        150        160        170        180 
GLFEGASRPG HFDGMLTVVA KLFGIAQPDV AVFGQKDAQQ VHLVGRMVDD LNLPVTIAVV 

       190        200        210        220        230        240 
DTVREPDGLA LSSRNRYLDA DARAAAATLS RALADGVAAC AGGAAAVLTA ARVRVEAEPV 

       250        260        270        280 
VRLDYLVIVD QGTFREVAPN YHGPAFLLIA ARVGSTRLID NERITLP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016822 Genomic DNA. Translation: AAT89835.1.
RefSeqYP_062940.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6ACQ8.
SMRQ6ACQ8. Positions 29-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281090.Lxx21410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT89835; AAT89835; Lxx21410.
GeneID2940613.
KEGGlxx:Lxx21410.
PATRIC22337974. VBILeiXyl11655_2223.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAALHKGHQ.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycLXYL281090:GH0X-2018-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_LEIXX
AccessionPrimary (citable) accession number: Q6ACQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 58 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