ID M7RV14_SALDU Unreviewed; 709 AA.
AC M7RV14;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528, ECO:0000256|PIRNR:PIRNR006107};
DE EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707, ECO:0000256|PIRNR:PIRNR006107};
DE AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108, ECO:0000256|PIRNR:PIRNR006107};
GN ORFNames=A670_05218 {ECO:0000313|EMBL:EMR49596.1};
OS Salmonella enterica subsp. enterica serovar Dublin str. UC16.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1192688 {ECO:0000313|EMBL:EMR49596.1, ECO:0000313|Proteomes:UP000013259};
RN [1] {ECO:0000313|EMBL:EMR49596.1, ECO:0000313|Proteomes:UP000013259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC16 {ECO:0000313|EMBL:EMR49596.1,
RC ECO:0000313|Proteomes:UP000013259};
RA McClelland M., Porwollik S., Desai P., Cheng P., Wollam A., Pepin K.,
RA Bhonagiri V., Fulton L., Fulton R., Delehaunty K., Fronick C., Godfrey J.,
RA Waligorski J., Appelbaum E., Tomlinson C., Warren W., Sodergren E.,
RA Weinstock G., Wilson R.K.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in acetate metabolism.
CC {ECO:0000256|PIRNR:PIRNR006107}.
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:0000256|PIRNR:PIRNR006107};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989,
CC ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006107}.
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. {ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family.
CC {ECO:0000256|ARBA:ARBA00008756, ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC {ECO:0000256|ARBA:ARBA00009786, ECO:0000256|PIRNR:PIRNR006107}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMR49596.1}.
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DR EMBL; APMR01000173; EMR49596.1; -; Genomic_DNA.
DR AlphaFoldDB; M7RV14; -.
DR PATRIC; fig|1192688.3.peg.4887; -.
DR HOGENOM; CLU_019723_2_1_6; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000013259; Unassembled WGS sequence.
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 CDD; cd03109; DTBS; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00651; pta; 1.
DR PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR Pfam; PF13500; AAA_26; 1.
DR Pfam; PF07085; DRTGG; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR006107};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR006107};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 228..338
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 386..701
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 709 AA; 76678 MW; D178C5440CB0D9E4 CRC64;
MLIPTGTSVG LTSVSLGVIR AMERKGVRLS VFKPIAQPRA GGDAPDQTTT IVRANSTLPA
AEPLKMSHVE SLLSSNQKDV LMEEIIANYH ANTKDAEVVL VEGLVPTRKH QFAQSLNYEI
AKTLNAEIVF VMSQGTDTPE QLNERIELTR SSFGGAKNTN ITGVIINKLN APVDEQGRTR
PDLSEIFDDS SKAQVIKIDP AKLQESSPLP VLGAVPWSFD LIATRAIDMA RHLNATIINE
GDIKTRRVKS VTFCARSIPH MLEHFRAGSL LVTSADRPDV LVAACLAAMN GVEIGALLLT
GGYEMDARIS KLCERAFATG LPVFMVNTNT WQTSLSLQSF NLEVPVDDHE RIEKVQEYVA
NYVNAEWIES LTATSERSRR LSPPAFRYQL TELARKAGKR VVLPEGDEPR TVKAAAICAE
RGIATCVLLG NPDEINRVAA SQGVELGAGI EIVDPEVVRE SYVARLVELR KSKGMTEPVA
REQLEDNVVL GTLMLEQDEV DGLVSGAVHT TANTIRPPLQ LIKTAPGSSL VSSVFFMLLP
EQVYVYGDCA INPDPTAEQL AEIAIQSADS AIAFGIEPRV AMLSYSTGTS GAGSDVEKVR
EATRLAQEKR PDLMIDGPLQ YDAAVMADVA KSKAPNSPVA GRATVFIFPD LNTGNTTYKA
VQRSADLISI GPMLQGMRKP VNDLSRGALV DDIVYTIALT AIQASQQQQ
//
