Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8ZND6 (PTA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. 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:
Phosphate acetyltransferase

EC=2.3.1.8
Alternative name(s):
Phosphotransacetylase
Gene names
Name:pta
Ordered Locus Names:STM2338
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine. Ref.2

Catalytic activity

Acetyl-CoA + phosphate = CoA + acetyl phosphate.

Enzyme regulation

Allosterically inhibited by NADH. Ref.3

Pathway

Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.

Subunit structure

Homohexamer Probable. Ref.3

Subcellular location

Cytoplasm Potential.

Domain

The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site By similarity.

Sequence similarities

In the N-terminal section; belongs to the CobB/CobQ family.

In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=162.1 µM for acetyl-CoA Ref.3

KM=329.3 µM for acetyl phosphate

Vmax=142.2 µM/h/mg enzyme for acetyl-CoA-forming reaction

Vmax=20.6 µM/h/mg enzyme for acetyl phosphate-forming reaction

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphate acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 714713Phosphate acetyltransferase
PRO_0000405551

Regions

Region390 – 714325Phosphate acetyltransferase

Experimental info

Mutagenesis2521R → H: Increases speed of forward and back reactions by 2-3 fold. Not inhibited by NADH. Ref.3
Mutagenesis2731G → D: Increases speed of forward and back reactions by 2-3 fold. Ref.3
Mutagenesis2941M → I: Slightly decreases speed of forward and back reactions. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8ZND6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D9DFE86F4AB21060

FASTA71477,278
        10         20         30         40         50         60 
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRAGGDAP DQTTTIVRAN 

        70         80         90        100        110        120 
STLPAAEPLK MSHVESLLSS NQKDVLMEEI IANYHANTKD AEVVLVEGLV PTRKHQFAQS 

       130        140        150        160        170        180 
LNYEIAKTLN AEIVFVMSQG TDTPEQLNER IELTRSSFGG AKNTNITGVI INKLNAPVDE 

       190        200        210        220        230        240 
QGRTRPDLSE IFDDSSKAQV IKIDPAKLQE SSPLPVLGAV PWSFDLIATR AIDMARHLNA 

       250        260        270        280        290        300 
TIINEGDIKT RRVKSVTFCA RSIPHMLEHF RAGSLLVTSA DRPDVLVAAC LAAMNGVEIG 

       310        320        330        340        350        360 
ALLLTGGYEM DARISKLCER AFATGLPVFM VNTNTWQTSL SLQSFNLEVP VDDHERIEKV 

       370        380        390        400        410        420 
QEYVANYVNA EWIESLTATS ERSRRLSPPA FRYQLTELAR KAGKRVVLPE GDEPRTVKAA 

       430        440        450        460        470        480 
AICAERGIAT CVLLGNPDEI NRVAASQGVE LGAGIEIVDP EVVRESYVAR LVELRKSKGM 

       490        500        510        520        530        540 
TEPVAREQLE DNVVLGTLML EQDEVDGLVS GAVHTTANTI RPPLQLIKTA PGSSLVSSVF 

       550        560        570        580        590        600 
FMLLPEQVYV YGDCAINPDP TAEQLAEIAI QSADSAIAFG IEPRVAMLSY STGTSGAGSD 

       610        620        630        640        650        660 
VEKVREATRL AQEKRPDLMI DGPLQYDAAV MADVAKSKAP NSPVAGRATV FIFPDLNTGN 

       670        680        690        700        710 
TTYKAVQRSA DLISIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAS QQQQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities."
Starai V.J., Garrity J., Escalante-Semerena J.C.
Microbiology 151:3793-3801(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: LT2.
[3]"In vivo and in vitro analyses of single-amino acid variants of the Salmonella enterica phosphotransacetylase enzyme provide insights into the function of its N-terminal domain."
Brinsmade S.R., Escalante-Semerena J.C.
J. Biol. Chem. 282:12629-12640(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-252; GLY-273 AND MET-294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL21239.1.
RefSeqNP_461280.1. NC_003197.1.

3D structure databases

ProteinModelPortalQ8ZND6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2338.

Proteomic databases

PaxDbQ8ZND6.
PRIDEQ8ZND6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL21239; AAL21239; STM2338.
GeneID1253860.
KEGGstm:STM2338.
PATRIC32383291. VBISalEnt20916_2475.

Phylogenomic databases

eggNOGCOG0280.
HOGENOMHOG000053797.
KOK13788.
OMAKPIAQPH.
OrthoDBEOG6BKJ5W.
PhylomeDBQ8ZND6.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2353-MONOMER.
BRENDA2.3.1.8. 2169.
UniPathwayUPA00340; UER00459.

Family and domain databases

Gene3D3.40.1390.20. 1 hit.
3.40.50.300. 1 hit.
InterProIPR010766. DRTGG.
IPR016475. P-Actrans_bac.
IPR027417. P-loop_NTPase.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
IPR028979. Ser_kin/Pase_Hpr_N_like.
[Graphical view]
PfamPF07085. DRTGG. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFPIRSF006107. PhpActrans_proteobac. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF75138. SSF75138. 1 hit.
TIGRFAMsTIGR00651. pta. 1 hit.
ProtoNetSearch...

Entry information

Entry namePTA_SALTY
AccessionPrimary (citable) accession number: Q8ZND6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 67 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