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Q1GLQ5 (PANC_RUEST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:TM1040_3439
Encoded onPlasmid megaplasmid TM1040
OrganismRuegeria sp. (strain TM1040) (Silicibacter sp.) [Complete proteome] [HAMAP]
Taxonomic identifier292414 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length280 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
Plasmid
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 – 280280Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305556

Regions

Nucleotide binding32 – 398ATP By similarity
Nucleotide binding149 – 1524ATP By similarity
Nucleotide binding186 – 1894ATP By similarity

Sites

Active site391Proton donor By similarity
Binding site631Beta-alanine By similarity
Binding site631Pantoate By similarity
Binding site1551Pantoate By similarity
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GLQ5 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: F3243C1E435EE050

FASTA28030,783
        10         20         30         40         50         60 
MTPPILRRLD DLRALRRDWM KKGDTLGLVP TMGALHAGHL SLVEAAKAAC DHVVVTIFVN 

        70         80         90        100        110        120 
PKQFNSPEDL ANYPRTEHED AQKLAPYGVD AIYVPDPDQI YPEGYATTVS LTGVTDVMEG 

       130        140        150        160        170        180 
PNRPGHFEGV ATVVAKLFLQ SGADRAFFGE KDYQQLMVVR RMARDLDIPI EVIGCPTVRE 

       190        200        210        220        230        240 
ASGLAMSSRN MRLSAAATKT AGQLNPLMEA AATRLRAGED YAPLEAEMRA QLSDLGFAEI 

       250        260        270        280 
EYIDLRCAQD LTSLDRLDRP ARMFVAAWLD GVRLIDNIAV 

« Hide

References

[1]"Complete sequence of megaplasmid of Silicibacter sp. TM1040."
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., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM1040.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000376 Genomic DNA. Translation: ABF62411.1.
RefSeqYP_611673.1. NC_008043.1.

3D structure databases

ProteinModelPortalQ1GLQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292414.TM1040_3439.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF62411; ABF62411; TM1040_3439.
GeneID4075613.
KEGGsit:TM1040_3439.
PATRIC23383324. VBIRueSp69653_0522.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycRSP292414:GHCT-3500-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_RUEST
AccessionPrimary (citable) accession number: Q1GLQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 59 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