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Q89JV7 (PANC2_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. 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 2

Short name=PS 2
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase 2
Pantoate-activating enzyme 2
Gene names
Name:panC2
Ordered Locus Names:blr5162
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length283 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
Reference 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 – 283283Pantothenate synthetase 2 HAMAP-Rule MF_00158
PRO_0000305409

Regions

Nucleotide binding34 – 418ATP By similarity
Nucleotide binding152 – 1554ATP By similarity
Nucleotide binding189 – 1924ATP By similarity

Sites

Active site411Proton donor By similarity
Binding site651Beta-alanine By similarity
Binding site651Pantoate By similarity
Binding site1581Pantoate By similarity
Binding site1811ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89JV7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3EFFFB820731629C

FASTA28330,969
        10         20         30         40         50         60 
MSRSPLIART VPALRRAADN LRKRKATIAL VPTMGALHDG HVSLVRLAKR RASRVVVSIF 

        70         80         90        100        110        120 
VNPTQFAPTE DFGAYPRTWK ADIAKLAAED VDIVWHPGVE AMYPEGFATR IVPEGPALAG 

       130        140        150        160        170        180 
LEDRFRPHFF GGVATVVGKL FTQCRPDFAI FGEKDFQQLR VVTQMARDLD LGVKVIGSRT 

       190        200        210        220        230        240 
VRERDGLAMS SRNVYLSPQE RQTATTLYRA MKDSAGRIRA GEAIASAMAR GAATIKAAGF 

       250        260        270        280 
VLDYFEARHA ETLAQVTSRK DGPLRILVAA KLGTTRLIDN IAV 

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000040 Genomic DNA. Translation: BAC50427.1.
RefSeqNP_771802.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ89JV7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr5162.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC50427; BAC50427; BAC50427.
GeneID1051570.
KEGGbja:blr5162.
PATRIC21194004. VBIBraJap65052_5246.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OrthoDBEOG6Z6FZ4.
PhylomeDBQ89JV7.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-5200-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 namePANC2_BRADU
AccessionPrimary (citable) accession number: Q89JV7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 65 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