Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q1LTN0 (PANC_BAUCH)

Last modified June 16, 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

Hide | Top

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: BCI_0231
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Hide | Top

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: 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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Pantothenate synthetase HAMAP MF_00158
PRO_0000305403

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding149 – 1524ATP By similarity
Nucleotide binding186 – 1894ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1551Pantoate By similarity
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q1LTN0-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: E3D1F484A338E507

FASTA28532,539
        10         20         30         40         50         60 
MLIIDNITIL RQTIKQWRKS IQSIALIPTM GNLHDGHMTI VNQGRSHTNI VIVSIFVNPM 

        70         80         90        100        110        120 
QFDREEDLFL YPRTLQSDYE KLHKIGVDAV FVPSVETMYR DNINCHTFLD VPNLSSILEG 

       130        140        150        160        170        180 
IYRPNHFRGV ATIISKLFNL VQPNVVYFGE KDFQQLVLIR QMVRDMNYDI EIIAVPTVRA 

       190        200        210        220        230        240 
NDGLALSSRN SYLTPEQRKI APKLYQVMQT LVTNLCSGEK NIDVLLNKAA KQLSKFGFTP 

       250        260        270        280 
EILEIRDAIT LQPITINSKK VVVLFSAWLG KARLIDNTQV SIPKE

« Hide

Hide | Top

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

CP000238 Genomic DNA. Translation: ABF14074.1.
RefSeqYP_588684.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4056175.
GenomeReviewsGene locus BCI_0231 in contig CP000238_GR.
KEGGbci:BCI_0231.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LTN0.
OMAQ1LTN0. VADFNIP.

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...

Hide | Top

Entry information

Entry namePANC_BAUCH
AccessionPrimary (citable) accession number: Q1LTN0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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