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Q0B0P5 (PANC_SYNWW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:Swol_0102
OrganismSyntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen) [Complete proteome] [HAMAP]
Taxonomic identifier335541 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesSyntrophomonadaceaeSyntrophomonas

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_0000305565

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding148 – 1514ATP By similarity
Nucleotide binding185 – 1884ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1541Pantoate By similarity
Binding site1771ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0B0P5 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: F6FEDEC568C04354

FASTA28232,021
        10         20         30         40         50         60 
MQVFENITKM QEWAREQKKQ GQSIALVPTM GYLHEGHLAL VKEARRQCDK VVVSIFVNPI 

        70         80         90        100        110        120 
QFGAGEDFEQ YPRDLEQDSA LLEKERVDAL FSPGIRDMYP GSFQTFVEVY GEITEKMCGA 

       130        140        150        160        170        180 
SRPGHFKGVT TVVSKLFNIC QPDRAYFGQK DAQQLMIVEK MVRELNFPLE IIRVPIVREK 

       190        200        210        220        230        240 
DGLAMSSRNV YLSPEERAEA LVLYRALKMA EEEIKNGERE IGIIRQKMEE MIKACPRAAI 

       250        260        270        280 
DYIAINNAND LSELQTCAGK VLIALAVKFG KTRLIDNLIV EV 

« Hide

References

[1]"The genome of Syntrophomonas wolfei: new insights into syntrophic metabolism and biohydrogen production."
Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.
Environ. Microbiol. 12:2289-2301(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2245B / Goettingen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000448 Genomic DNA. Translation: ABI67459.1.
RefSeqYP_752830.1. NC_008346.1.

3D structure databases

ProteinModelPortalQ0B0P5.
SMRQ0B0P5. Positions 1-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335541.Swol_0102.

Proteomic databases

PRIDEQ0B0P5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI67459; ABI67459; Swol_0102.
GeneID4282378.
KEGGswo:Swol_0102.
PATRIC23854876. VBISynWol51738_0109.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHLGHITL.
OrthoDBEOG6Z6FZ4.
ProtClustDBCLSK2780165.

Enzyme and pathway databases

BioCycSWOL335541:GHL1-116-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_SYNWW
AccessionPrimary (citable) accession number: Q0B0P5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 51 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