ID A0A2D2M2R9_9PSED Unreviewed; 698 AA.
AC A0A2D2M2R9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=CS390_04190 {ECO:0000313|EMBL:ATR81801.1};
OS Pseudomonas sp. HLS-6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2049589 {ECO:0000313|EMBL:ATR81801.1, ECO:0000313|Proteomes:UP000230810};
RN [1] {ECO:0000313|EMBL:ATR81801.1, ECO:0000313|Proteomes:UP000230810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLS-6 {ECO:0000313|EMBL:ATR81801.1,
RC ECO:0000313|Proteomes:UP000230810};
RA Hu Y., Zhang T., Lei D., Yao S., Lin K., Chen X., Cui C.;
RT "Complete genome of Pseudomonas sp. HSL-6, a multiple-antibiotic-resistant
RT bacteria isolated from drinking water source in East China.";
RL Submitted (OCT-2017) 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}.
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DR EMBL; CP024478; ATR81801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D2M2R9; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000230810; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000230810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 217..329
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 374..689
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 698 AA; 75348 MW; E69A7E619D528375 CRC64;
MQTFFIAPTD FGVGLTSISL GLVRTLERAG LKVGFFKPIA QPHPGDTGPE RSTELIARTH
GLKPPKPLSL AHVERMLGDG QLDELLEEIV TLYQQACEDK DVVVVEGMVP TRHASYAARV
NLHLAKSLDA EVILVSAPEN DVLAELSGRV ELQAQLFGGP KDPKVLGVIL NKVRSDESMH
AFATRLKEHS PVLRSGDFRL LGCIPYQADL NAPRTRDVAE LLGAQVLNAG DCEQRRMNKI
ILCARTVANT VPLLTPGTLV VTPGDRDDII LAVSLASING VPLAGLLLTS DSKPDPRILE
LCRGALAAGL PVLSVSTGSY DTANQLNQLN KEIPVDDRER AEIITDFVAS HLDASWLHQR
CGTPREMRLS PAVFRYQLIQ RAQQANKRIV LPEGAEPMTV QAAAICQTRG IARCVLLAKP
QEVQAVARAQ GIELPEGLEI LDPDLIRERY VEPMVNLRKS KSLNAPMAEQ QLEDPVVIGT
MMLALDEVDG LVSGLVHSTA NTIRPALQLI KTAPGCTLVS SVFFMLFPEQ VLVYGDCVMN
PHPSASELAE IALQSADSAE AFGITPRVAM ISYSSGDSAS GEEVEKVREA TLLAQESQRD
LQIDGPLQYD TAANENTARE LAPNSPVAGR ATVFVFPDLN TGNTTHKAVQ RSADCVSLGP
MLQGLRKPVN DLPRGAQVDD IVYTIALTAI QANRSLDS
//
