ID A0A3N6MS18_9BURK Unreviewed; 730 AA.
AC A0A3N6MS18;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528};
DE EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707};
DE AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108};
GN ORFNames=D1Y85_24710 {ECO:0000313|EMBL:RQH00591.1};
OS Paraburkholderia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2305225 {ECO:0000313|EMBL:RQH00591.1, ECO:0000313|Proteomes:UP000272778};
RN [1] {ECO:0000313|EMBL:RQH00591.1, ECO:0000313|Proteomes:UP000272778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOA04 {ECO:0000313|EMBL:RQH00591.1,
RC ECO:0000313|Proteomes:UP000272778};
RA Gao Z.-H., Qiu L.-H., Fu J.-C.;
RT "Paraburkholderia sp. DHOA04, isolated from soil.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family.
CC {ECO:0000256|ARBA:ARBA00008756}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC {ECO:0000256|ARBA:ARBA00009786}.
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:RQH00591.1}.
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DR EMBL; RQIS01000026; RQH00591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6MS18; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000272778; 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:0000313|EMBL:RQH00591.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000272778};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RQH00591.1}.
FT DOMAIN 216..327
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 373..688
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
FT REGION 702..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 76862 MW; CA2D933FDC53E75C CRC64;
MSNTARIFYL VPVSRDAGLT SMALGLVRAL QLAGVRVGFA KPVAQAEADA AEPDLSGYFA
RTLCSTQTLE PIAYTRAIER VRAGDLAGLM EDVVSNVDAA GEGNQIVVVE GLIPDVDFQI
ATRLNIEIVR ALGAELIPVV SARARGIDDL DAIAAGAAEQ YGDGGRRPLA GVLVNHADVQ
PETSAENKLS ETLADGTPVL ATVPTAEHLL SPRLIDVVSN LGLRVLRTGA TAPARVQNVL
VAASSPEKLL PHLRPGTLVV LPSDRADAML AVALAALRGM PIAGMLLTGG GALPAELAGL
FRGRPLDHLP ILGTDEDTFH VASRLANLSS HIGRGDAERM EQVIDFIGER IMTAPLVARL
DVPVMPLMSP PIFRTRLVES ARAANRRIVL PEGDEPRTIQ AAALCAARGI ARCVLLGSPE
TIRAVAAGHG IELPANVEIV DPEVVREHYV APMVELRRAK GLTELQAHQQ LEDTVVLGTM
MLATGEVDGL VSGAVHTTAN TVRPALQLIR TLPDSPLVSS VFFMLMPDQV FVYGDCAINP
DPNAEELAQI AIQSADSARA FGIDPRVAMI SYSTGTSGAG ADVEKVKEAT AIARRLRPDL
VIDGPIQYDA AAVEDVARQK APGSPLGGHA NVFVFPDLNT GNTTYKAVQR SANVVSVGPM
LQGLRKPVND LSRGALVDDI VYTIALTAIQ AATRKTVQKE RAAAAPAARS VHSARSVPRA
EFGEAPREAA
//
