PTA_SALTY
ID PTA_SALTY Reviewed; 714 AA.
AC Q8ZND6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.222 {ECO:0000305|PubMed:12700259};
DE EC=2.3.1.8 {ECO:0000269|PubMed:17339319};
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=STM2338;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=12700259; DOI=10.1128/jb.185.9.2802-2810.2003;
RA Palacios S., Starai V.J., Escalante-Semerena J.C.;
RT "Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and
RT propionate catabolic pathways needed for expression of the prpBCDE operon
RT during growth of Salmonella enterica on 1,2-propanediol.";
RL J. Bacteriol. 185:2802-2810(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16272400; DOI=10.1099/mic.0.28156-0;
RA Starai V.J., Garrity J., Escalante-Semerena J.C.;
RT "Acetate excretion during growth of Salmonella enterica on ethanolamine
RT requires phosphotransacetylase (EutD) activity, and acetate recapture
RT requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta)
RT activities.";
RL Microbiology 151:3793-3801(2005).
RN [4]
RP CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ARG-252; GLY-273 AND MET-294.
RX PubMed=17339319; DOI=10.1074/jbc.m611439200;
RA Brinsmade S.R., Escalante-Semerena J.C.;
RT "In vivo and in vitro analyses of single-amino acid variants of the
RT Salmonella enterica phosphotransacetylase enzyme provide insights into the
RT function of its N-terminal domain.";
RL J. Biol. Chem. 282:12629-12640(2007).
CC -!- FUNCTION: Involved in acetate metabolism. Catalyzes the reversible
CC interconversion of acetyl-CoA and acetyl phosphate. The direction of
CC the overall reaction changes depending on growth conditions. Required
CC for acetate recapture but not for acetate excretion when this organism
CC is grown on ethanolamine (EA); is unable to complement an eutD deletion
CC during growth on EA (PubMed:16272400). Works with proprionate kinase
CC PduW to capture exogenous propionate and regenerate propionyl-CoA
CC during degradation of propionate and 1,2-propanediol (1,2-PD)
CC (PubMed:12700259). {ECO:0000269|PubMed:12700259,
CC ECO:0000269|PubMed:16272400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC Evidence={ECO:0000269|PubMed:17339319, ECO:0000305|PubMed:16272400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19522;
CC Evidence={ECO:0000269|PubMed:17339319};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19523;
CC Evidence={ECO:0000269|PubMed:17339319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + propanoyl-CoA = CoA + propanoyl phosphate;
CC Xref=Rhea:RHEA:28046, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58933; EC=2.3.1.222;
CC Evidence={ECO:0000305|PubMed:12700259};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by NADH.
CC {ECO:0000269|PubMed:17339319}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=162.1 uM for acetyl-CoA {ECO:0000269|PubMed:17339319};
CC KM=329.3 uM for acetyl phosphate {ECO:0000269|PubMed:17339319};
CC Vmax=142.2 uM/h/mg enzyme for acetyl-CoA-forming reaction
CC {ECO:0000269|PubMed:17339319};
CC Vmax=20.6 uM/h/mg enzyme for acetyl phosphate-forming reaction
CC {ECO:0000269|PubMed:17339319};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2.
CC -!- SUBUNIT: Homohexamer. {ECO:0000305|PubMed:17339319}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12700259,
CC ECO:0000305|PubMed:16272400}.
CC -!- DOMAIN: The N-terminal region seems to be important for proper
CC quaternary structure. The C-terminal region contains the substrate-
CC binding site (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Decreased propionate kinase activity, cells grow
CC to lower density on 1,2-PD and excrete more propionate into the medium
CC (PubMed:12700259). A double acs-pta deletion excretes but no longer
CC recpautres acetate (PubMed:16272400). {ECO:0000269|PubMed:12700259,
CC ECO:0000269|PubMed:16272400}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family. {ECO:0000305}.
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DR EMBL; AE006468; AAL21239.1; -; Genomic_DNA.
DR RefSeq; NP_461280.1; NC_003197.2.
DR RefSeq; WP_000086692.1; NC_003197.2.
DR AlphaFoldDB; Q8ZND6; -.
DR SMR; Q8ZND6; -.
DR STRING; 99287.STM2338; -.
DR PaxDb; Q8ZND6; -.
DR EnsemblBacteria; AAL21239; AAL21239; STM2338.
DR GeneID; 1253860; -.
DR KEGG; stm:STM2338; -.
DR PATRIC; fig|99287.12.peg.2475; -.
DR HOGENOM; CLU_019723_2_1_6; -.
DR OMA; FFMCLAD; -.
DR PhylomeDB; Q8ZND6; -.
DR BioCyc; SENT99287:STM2338-MON; -.
DR BRENDA; 2.3.1.8; 2169.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1390.20; -; 1.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010766; DRTGG.
DR InterPro; IPR016475; P-Actrans_bac.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004614; P_AcTrfase.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR Pfam; PF07085; DRTGG; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75138; SSF75138; 1.
DR TIGRFAMs; TIGR00651; pta; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..714
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000405551"
FT REGION 390..714
FT /note="Phosphate acetyltransferase"
FT MUTAGEN 252
FT /note="R->H: Increases speed of forward and back reactions
FT by 2-3 fold. Not inhibited by NADH."
FT /evidence="ECO:0000269|PubMed:17339319"
FT MUTAGEN 273
FT /note="G->D: Increases speed of forward and back reactions
FT by 2-3 fold."
FT /evidence="ECO:0000269|PubMed:17339319"
FT MUTAGEN 294
FT /note="M->I: Slightly decreases speed of forward and back
FT reactions."
FT /evidence="ECO:0000269|PubMed:17339319"
SQ SEQUENCE 714 AA; 77278 MW; D9DFE86F4AB21060 CRC64;
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRAGGDAP DQTTTIVRAN
STLPAAEPLK MSHVESLLSS NQKDVLMEEI IANYHANTKD AEVVLVEGLV PTRKHQFAQS
LNYEIAKTLN AEIVFVMSQG TDTPEQLNER IELTRSSFGG AKNTNITGVI INKLNAPVDE
QGRTRPDLSE IFDDSSKAQV IKIDPAKLQE SSPLPVLGAV PWSFDLIATR AIDMARHLNA
TIINEGDIKT RRVKSVTFCA RSIPHMLEHF RAGSLLVTSA DRPDVLVAAC LAAMNGVEIG
ALLLTGGYEM DARISKLCER AFATGLPVFM VNTNTWQTSL SLQSFNLEVP VDDHERIEKV
QEYVANYVNA EWIESLTATS ERSRRLSPPA FRYQLTELAR KAGKRVVLPE GDEPRTVKAA
AICAERGIAT CVLLGNPDEI NRVAASQGVE LGAGIEIVDP EVVRESYVAR LVELRKSKGM
TEPVAREQLE DNVVLGTLML EQDEVDGLVS GAVHTTANTI RPPLQLIKTA PGSSLVSSVF
FMLLPEQVYV YGDCAINPDP TAEQLAEIAI QSADSAIAFG IEPRVAMLSY STGTSGAGSD
VEKVREATRL AQEKRPDLMI DGPLQYDAAV MADVAKSKAP NSPVAGRATV FIFPDLNTGN
TTYKAVQRSA DLISIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAS QQQQ
