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Q8ZND6

- PTA_SALTY

UniProt

Q8ZND6 - PTA_SALTY

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Protein
Phosphate acetyltransferase
Gene
pta, STM2338
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - 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 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

Pathwayi

GO - Molecular functioni

  1. phosphate acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. acetyl-CoA biosynthetic process Source: UniProtKB-UniPathway
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: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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 – 11Removed By similarity
Chaini2 – 714713Phosphate acetyltransferase
PRO_0000405551Add
BLAST

Proteomic databases

PaxDbiQ8ZND6.
PRIDEiQ8ZND6.

Interactioni

Subunit structurei

Homohexamer Inferred.1 Publication

Protein-protein interaction databases

STRINGi99287.STM2338.

Structurei

3D structure databases

ProteinModelPortaliQ8ZND6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 714325Phosphate acetyltransferase
Add
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.

Sequence similaritiesi

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

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

MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRAGGDAP    50
DQTTTIVRAN STLPAAEPLK MSHVESLLSS NQKDVLMEEI IANYHANTKD 100
AEVVLVEGLV PTRKHQFAQS LNYEIAKTLN AEIVFVMSQG TDTPEQLNER 150
IELTRSSFGG AKNTNITGVI INKLNAPVDE QGRTRPDLSE IFDDSSKAQV 200
IKIDPAKLQE SSPLPVLGAV PWSFDLIATR AIDMARHLNA TIINEGDIKT 250
RRVKSVTFCA RSIPHMLEHF RAGSLLVTSA DRPDVLVAAC LAAMNGVEIG 300
ALLLTGGYEM DARISKLCER AFATGLPVFM VNTNTWQTSL SLQSFNLEVP 350
VDDHERIEKV QEYVANYVNA EWIESLTATS ERSRRLSPPA FRYQLTELAR 400
KAGKRVVLPE GDEPRTVKAA AICAERGIAT CVLLGNPDEI NRVAASQGVE 450
LGAGIEIVDP EVVRESYVAR LVELRKSKGM TEPVAREQLE DNVVLGTLML 500
EQDEVDGLVS GAVHTTANTI RPPLQLIKTA PGSSLVSSVF FMLLPEQVYV 550
YGDCAINPDP TAEQLAEIAI QSADSAIAFG IEPRVAMLSY STGTSGAGSD 600
VEKVREATRL AQEKRPDLMI DGPLQYDAAV MADVAKSKAP NSPVAGRATV 650
FIFPDLNTGN TTYKAVQRSA DLISIGPMLQ GMRKPVNDLS RGALVDDIVY 700
TIALTAIQAS QQQQ 714
Length:714
Mass (Da):77,278
Last modified:March 1, 2002 - v1
Checksum:iD9DFE86F4AB21060
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL21239.1.
RefSeqiNP_461280.1. NC_003197.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL21239.1 .
RefSeqi NP_461280.1. NC_003197.1.

3D structure databases

ProteinModelPortali Q8ZND6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM2338.

Proteomic databases

PaxDbi Q8ZND6.
PRIDEi Q8ZND6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL21239 ; AAL21239 ; STM2338 .
GeneIDi 1253860.
KEGGi stm:STM2338.
PATRICi 32383291. VBISalEnt20916_2475.

Phylogenomic databases

eggNOGi COG0280.
HOGENOMi HOG000053797.
KOi K13788.
OMAi KPIAQPH.
OrthoDBi EOG6BKJ5W.
PhylomeDBi Q8ZND6.

Enzyme and pathway databases

UniPathwayi UPA00340 ; UER00459 .
BioCyci SENT99287:GCTI-2353-MONOMER.
BRENDAi 2.3.1.8. 2169.

Family and domain databases

Gene3Di 3.40.1390.20. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR010766. DRTGG.
IPR016475. P-Actrans_bac.
IPR027417. P-loop_NTPase.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
IPR028979. Ser_kin/Pase_Hpr_N_like.
[Graphical view ]
Pfami PF07085. DRTGG. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view ]
PIRSFi PIRSF006107. PhpActrans_proteobac. 1 hit.
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF75138. SSF75138. 1 hit.
TIGRFAMsi TIGR00651. pta. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 67 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

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