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Protein

Phosphate acetyltransferase

Gene

pta

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Acetyl-CoA + phosphate = CoA + acetyl phosphate.

Enzyme regulationi

Allosterically inhibited by NADH.1 Publication

Kineticsi

  1. KM=162.1 µM for acetyl-CoA1 Publication
  2. KM=329.3 µM for acetyl phosphate1 Publication
  1. Vmax=142.2 µM/h/mg enzyme for acetyl-CoA-forming reaction1 Publication
  2. Vmax=20.6 µM/h/mg enzyme for acetyl phosphate-forming reaction1 Publication

Pathway: acetyl-CoA biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes acetyl-CoA from acetate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Acetate kinase (ackA)
  2. Phosphate acetyltransferase (pta)
This subpathway is part of the pathway acetyl-CoA biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from acetate, the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2353-MONOMER.
BRENDAi2.3.1.8. 2169.
UniPathwayiUPA00340; UER00459.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphate acetyltransferase (EC:2.3.1.8)
Alternative name(s):
Phosphotransacetylase
Gene namesi
Name:pta
Ordered Locus Names:STM2338
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi252 – 2521R → H: Increases speed of forward and back reactions by 2-3 fold. Not inhibited by NADH. 1 Publication
Mutagenesisi273 – 2731G → D: Increases speed of forward and back reactions by 2-3 fold. 1 Publication
Mutagenesisi294 – 2941M → I: Slightly decreases speed of forward and back reactions. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 714713Phosphate acetyltransferasePRO_0000405551Add
BLAST

Proteomic databases

PaxDbiQ8ZND6.
PRIDEiQ8ZND6.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM2338.

Structurei

3D structure databases

ProteinModelPortaliQ8ZND6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 714325Phosphate acetyltransferaseAdd
BLAST

Domaini

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

Sequence similaritiesi

In the N-terminal section; belongs to the CobB/CobQ family.Curated
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.Curated

Phylogenomic databases

eggNOGiCOG0280.
HOGENOMiHOG000053797.
KOiK13788.
OMAiKPIAQPH.
OrthoDBiEOG6BKJ5W.
PhylomeDBiQ8ZND6.

Family and domain databases

Gene3Di3.40.1390.20. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR010766. DRTGG.
IPR016475. P-Actrans_bac.
IPR027417. P-loop_NTPase.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
IPR028979. Ser_kin/Pase_Hpr_N_like.
[Graphical view]
PfamiPF07085. DRTGG. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFiPIRSF006107. PhpActrans_proteobac. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF75138. SSF75138. 1 hit.
TIGRFAMsiTIGR00651. pta. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8ZND6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRAGGDAP
60 70 80 90 100
DQTTTIVRAN STLPAAEPLK MSHVESLLSS NQKDVLMEEI IANYHANTKD
110 120 130 140 150
AEVVLVEGLV PTRKHQFAQS LNYEIAKTLN AEIVFVMSQG TDTPEQLNER
160 170 180 190 200
IELTRSSFGG AKNTNITGVI INKLNAPVDE QGRTRPDLSE IFDDSSKAQV
210 220 230 240 250
IKIDPAKLQE SSPLPVLGAV PWSFDLIATR AIDMARHLNA TIINEGDIKT
260 270 280 290 300
RRVKSVTFCA RSIPHMLEHF RAGSLLVTSA DRPDVLVAAC LAAMNGVEIG
310 320 330 340 350
ALLLTGGYEM DARISKLCER AFATGLPVFM VNTNTWQTSL SLQSFNLEVP
360 370 380 390 400
VDDHERIEKV QEYVANYVNA EWIESLTATS ERSRRLSPPA FRYQLTELAR
410 420 430 440 450
KAGKRVVLPE GDEPRTVKAA AICAERGIAT CVLLGNPDEI NRVAASQGVE
460 470 480 490 500
LGAGIEIVDP EVVRESYVAR LVELRKSKGM TEPVAREQLE DNVVLGTLML
510 520 530 540 550
EQDEVDGLVS GAVHTTANTI RPPLQLIKTA PGSSLVSSVF FMLLPEQVYV
560 570 580 590 600
YGDCAINPDP TAEQLAEIAI QSADSAIAFG IEPRVAMLSY STGTSGAGSD
610 620 630 640 650
VEKVREATRL AQEKRPDLMI DGPLQYDAAV MADVAKSKAP NSPVAGRATV
660 670 680 690 700
FIFPDLNTGN TTYKAVQRSA DLISIGPMLQ GMRKPVNDLS RGALVDDIVY
710
TIALTAIQAS QQQQ
Length:714
Mass (Da):77,278
Last modified:March 1, 2002 - v1
Checksum:iD9DFE86F4AB21060
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL21239.1.
RefSeqiNP_461280.1. NC_003197.1.
WP_000086692.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21239; AAL21239; STM2338.
GeneIDi1253860.
KEGGistm:STM2338.
PATRICi32383291. VBISalEnt20916_2475.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL21239.1.
RefSeqiNP_461280.1. NC_003197.1.
WP_000086692.1. NC_003197.1.

3D structure databases

ProteinModelPortaliQ8ZND6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2338.

Proteomic databases

PaxDbiQ8ZND6.
PRIDEiQ8ZND6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21239; AAL21239; STM2338.
GeneIDi1253860.
KEGGistm:STM2338.
PATRICi32383291. VBISalEnt20916_2475.

Phylogenomic databases

eggNOGiCOG0280.
HOGENOMiHOG000053797.
KOiK13788.
OMAiKPIAQPH.
OrthoDBiEOG6BKJ5W.
PhylomeDBiQ8ZND6.

Enzyme and pathway databases

UniPathwayiUPA00340; UER00459.
BioCyciSENT99287:GCTI-2353-MONOMER.
BRENDAi2.3.1.8. 2169.

Family and domain databases

Gene3Di3.40.1390.20. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR010766. DRTGG.
IPR016475. P-Actrans_bac.
IPR027417. P-loop_NTPase.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
IPR028979. Ser_kin/Pase_Hpr_N_like.
[Graphical view]
PfamiPF07085. DRTGG. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFiPIRSF006107. PhpActrans_proteobac. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF75138. SSF75138. 1 hit.
TIGRFAMsiTIGR00651. pta. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiPTA_SALTY
AccessioniPrimary (citable) accession number: Q8ZND6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 1, 2002
Last modified: May 27, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.