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Q1H3S1 (PANC_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Mfla_0596
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus

Protein attributes

Sequence length278 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 – 278278Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305483

Regions

Nucleotide binding28 – 358ATP By similarity
Nucleotide binding145 – 1484ATP By similarity
Nucleotide binding182 – 1854ATP By similarity

Sites

Active site351Proton donor By similarity
Binding site591Beta-alanine By similarity
Binding site591Pantoate By similarity
Binding site1511Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1H3S1 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 64DCA02B2CB13355

FASTA27830,727
        10         20         30         40         50         60 
MTLQIIPEIS SLRARLAGEN SIALVPTMGN LHAGHIHLVE LARQRAGCVV TSIFVNPLQF 

        70         80         90        100        110        120 
GANEDLDNYP RTLAEDCAKL QAAGADIVFT PSVQEMYPTT QTMRITPPPI ANELCGAARP 

       130        140        150        160        170        180 
GHFDGVATVV MKLFNIVQPH IAVFGKKDFQ QLFIIRELVR QFNLPIDIIA GETQREHTGL 

       190        200        210        220        230        240 
ALSSRNGYLN EGQKLEAQRL YRTLKLIVDN VQQGNRDYPA IEAQSSQYLT QLGWIVDYIS 

       250        260        270 
IRSSTTLLPA SLDDHNLVVL AAARQGNTRL IDNIEFSV 

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
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., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000284 Genomic DNA. Translation: ABE48866.1.
RefSeqYP_544707.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1H3S1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265072.Mfla_0596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE48866; ABE48866; Mfla_0596.
GeneID3999066.
KEGGmfa:Mfla_0596.
PATRIC32266743. VBIMetFla97085_0611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAASSKENH.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycMFLA265072:GHWJ-618-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_METFK
AccessionPrimary (citable) accession number: Q1H3S1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 53 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