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Q11F81 (PANC_CHESB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:Meso_2560
OrganismChelativorans sp. (strain BNC1) [Complete proteome] [HAMAP]
Taxonomic identifier266779 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeChelativorans

Protein attributes

Sequence length284 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 – 284284Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305481

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
Q11F81 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 61A75EFB8756BCF6

FASTA28430,423
        10         20         30         40         50         60 
MSVPIFRTVK ELRAAVADWR RDGLRVGVVP TMGALHEGHL SLVRAALANT DRVIVTLFVN 

        70         80         90        100        110        120 
PKQFNNAGDL AAYPRTEKED AAKLAPLGAH MLYAPDGAEM YPNGFSTTVS VSGVSEGLCG 

       130        140        150        160        170        180 
AFRPGHFDGV ATVVTKLLLQ TGADLAFFGE KDFQQLHVVR RLTRDLDIPT QIIACPTVRE 

       190        200        210        220        230        240 
ADGLALSSRN VRLSADDRRN APKLAEALFA AAGRLAEGTP VAEVLPNARD AILAAGYQEV 

       250        260        270        280 
EYLELRGEDD LAPLSGLDRP ARLLVAAWIG GVRLIDNLPV AQPA 

« Hide

References

[1]"Complete sequence of chromosome of Mesorhizobium sp. BNC1."
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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BNC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000390 Genomic DNA. Translation: ABG63944.1.
RefSeqYP_675109.1. NC_008254.1.

3D structure databases

ProteinModelPortalQ11F81.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266779.Meso_2560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG63944; ABG63944; Meso_2560.
GeneID4182975.
KEGGmes:Meso_2560.
PATRIC21345334. VBICheSp72577_3281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAIVRDSDH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycCSP266779:GI09-2604-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. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_CHESB
AccessionPrimary (citable) accession number: Q11F81
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: August 22, 2006
Last modified: June 11, 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