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A0JR91 (PANC_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Arth_0160
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length304 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 – 304304Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305393

Regions

Nucleotide binding29 – 368ATP By similarity
Nucleotide binding167 – 1704ATP By similarity
Nucleotide binding204 – 2074ATP By similarity

Sites

Active site361Proton donor By similarity
Binding site601Beta-alanine By similarity
Binding site601Pantoate By similarity
Binding site1731Pantoate By similarity
Binding site1961ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JR91 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 15D698482BC97990

FASTA30432,382
        10         20         30         40         50         60 
MTTAAQLRAE SARLLTEKQG SSQGLVPTMG ALHEGHARLA RTAVEQNDVV VASIFVNPLQ 

        70         80         90        100        110        120 
FGEAVDLDRY PRTLEADMEL LDAEGVDLVF APAVEEVYPG GEPLVRVTAG RLAGKWEGAS 

       130        140        150        160        170        180 
RPGHFDGALT VVAKLLHYGI PGTGLPGGGA FVTGAGAGLP AYRAYFGQKD AQQLTLVRRM 

       190        200        210        220        230        240 
VTDLNFPVEI VAVPTVRSAD GLALSSRNRF LSGEEREAAL VLSRALRLLE ERANAHEPLD 

       250        260        270        280        290        300 
LESAQALVES QPLVGLDYFD VVDPETLEPL AENCKETPFR GEGLAIIAAK VGPVRLIDNL 


PLSS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000454 Genomic DNA. Translation: ABK01561.1.
RefSeqYP_829661.1. NC_008541.1.

3D structure databases

ProteinModelPortalA0JR91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290399.Arth_0160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK01561; ABK01561; Arth_0160.
GeneID4447388.
KEGGart:Arth_0160.
PATRIC20995549. VBIArtSp72239_0507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAQMVESTI.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycASP290399:GHIF-165-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]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePANC_ARTS2
AccessionPrimary (citable) accession number: A0JR91
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 52 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