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A5D5T5 (PANC_PELTS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:PTH_0221
OrganismPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) [Complete proteome] [HAMAP]
Taxonomic identifier370438 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum

Protein attributes

Sequence length282 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 – 282282Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000076860

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1761ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5D5T5 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: DE055CC15AE04AE9

FASTA28231,547
        10         20         30         40         50         60 
MLVCNTISEI RAFVREARSK GRSIGFVPTM GYLHEGHLEL MRRAKERCDT VVISIFVNPT 

        70         80         90        100        110        120 
QFGPNEDYDR YPRDLERDAR LAGQVGVDAI FNPSVEEMYP AGYCTYVDVE RLTGKLCGLS 

       130        140        150        160        170        180 
RPGHFRGVCT VVTKLFNIVK PDYAFFGQKD AQQALVIKRM AADLNMDLEV ITVPTVREAD 

       190        200        210        220        230        240 
GLAMSSRNVY LDPEQRRAAL VLSRSLEKAG EAFRAGERDA SKLRQMVLDM IKAEPLANID 

       250        260        270        280 
YVEIYSYPEL EPLDQINGPA LLALAVKIGQ TRLIDNAILG QL 

« Hide

References

[1]"The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13744 / JCM 10971 / SI.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009389 Genomic DNA. Translation: BAF58402.1.
RefSeqYP_001210771.1. NC_009454.1.

3D structure databases

ProteinModelPortalA5D5T5.
SMRA5D5T5. Positions 1-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370438.PTH_0221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF58402; BAF58402; PTH_0221.
GeneID5138277.
KEGGpth:PTH_0221.
PATRIC22907240. VBIPelThe8413_0253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAEIDYVEV.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycPTHE370438:GCGQ-227-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_PELTS
AccessionPrimary (citable) accession number: A5D5T5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 48 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