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Reviewed, UniProtKB/Swiss-Prot A1R163 (PANC_ARTAT)

Last modified October 13, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: AAur_0147
OrganismArthrobacter aurescens (strain TC1) [Complete proteome] [HAMAP]
Taxonomic identifier290340 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

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Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity.

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

Sequence similarities

Belongs to the pantothenate synthetase family.

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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: 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: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Pantothenate synthetase HAMAP MF_00158
PRO_0000305392

Regions

Nucleotide binding29 – 368ATP By similarity
Nucleotide binding158 – 1614ATP By similarity
Nucleotide binding195 – 1984ATP By similarity

Sites

Active site361Proton donor By similarity
Binding site601Beta-alanine By similarity
Binding site601Pantoate By similarity
Binding site1641Pantoate By similarity
Binding site1871ATP; via amide nitrogen and carbonyl oxygen By similarity

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Sequences

Sequence LengthMass (Da)Tools
A1R163-1 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 1281B74506B59932

FASTA29531,211
        10         20         30         40         50         60 
MTTAAELRAE SARLLAAKGG NSQGLVPTMG ALHSGHAALA RTAVAENDVV VATIFVNPLQ 

        70         80         90        100        110        120 
FGDAVDLDRY PRTLDADMAL LDAEGVDLVF APSVDEVYPG GQPLVRVTSG PLGEKWEGAS 

       130        140        150        160        170        180 
RPGHFDGALT VVAKLLHYGL PGGAAADGTT AAYRAYFGQK DAQQLALVKR MVSDLNFPVE 

       190        200        210        220        230        240 
IIPVPIVRSE DGLALSSRNR FLSDAERDAA LVLSRALRLI ESRANAHEPL HLDSAVALVE 

       250        260        270        280        290 
SQPLVELDYF DVVDPATLEP LAENCKETPF RGEGLAIIAA KVGAVRLIDN APLFS

« Hide

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References

[1]"Secrets of soil survival revealed by the genome sequence of Arthrobacter aurescens TC1."
Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.
PLoS Genet. 2:2094-2106(2006) [PubMed: 17194220] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000474 Genomic DNA. Translation: ABM07369.1. Different initiation.
RefSeqYP_945975.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1R163.

Genome annotation databases

GeneID4638578.
GenomeReviewsGene locus AAur_0147 in contig CP000474_GR.
KEGGaau:AAur_0147.
TIGRAAur_0147.

Family and domain databases

HAMAPMF_00158.
[Tree]
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

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Entry information

Entry namePANC_ARTAT
AccessionPrimary (citable) accession number: A1R163
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: October 13, 2009
This is version 19 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents