ID V7DD90_9PSED Unreviewed; 695 AA.
AC V7DD90;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=O164_07130 {ECO:0000313|EMBL:ESW40284.1};
OS Pseudomonas taiwanensis SJ9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1388762 {ECO:0000313|EMBL:ESW40284.1, ECO:0000313|Proteomes:UP000018511};
RN [1] {ECO:0000313|EMBL:ESW40284.1, ECO:0000313|Proteomes:UP000018511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ9 {ECO:0000313|EMBL:ESW40284.1,
RC ECO:0000313|Proteomes:UP000018511};
RA Hong S.-J., Shin J.-H.;
RT "Whole Genome Shotgun Sequence of Pseudomonas taiwanensis SJ9.";
RL Submitted (OCT-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:ESW40284.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AXUP01000072; ESW40284.1; -; Genomic_DNA.
DR RefSeq; WP_013970947.1; NZ_AXUP01000072.1.
DR AlphaFoldDB; V7DD90; -.
DR PATRIC; fig|1388762.3.peg.1433; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000018511; 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 217..328
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 374..688
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 695 AA; 74585 MW; FA74AEB0B69A7B59 CRC64;
MHTFFIAPTD FGVGLTSISL GLVRTLERAG LKVGFFKPIA QPHPGDTGPE RSTELVARTH
GIKPPVPLSL AHVERMLGDG QLDELLEEII RLYQQACIGN DVVVVEGMVP TRHASYAARV
NLHLAKSLDA EVILVSAPEN EVLSELSGRV ELQAQLFGGP RDPKVLGVIL NKVRTDESMA
DFSTRLREHS PLLRGNDFRL LGCIPYQPEL NAPRTRDVAD LLGAQVLNAG DYEQRRMSKI
IICARTVANT VPLLTSGTLV VTPGDRDDII LAVSLAAING VPLAGLLLTS DSKPDARILG
LCRGALQAGL PILSVSTGSY DTANQLNSLN REIPVDDRER AEFITDFVAS HLDAAWLHQR
CGTPRELRLS PAVFRYQLIQ RAQQANKRIV LPEGAEPLLV QAAAICQARG IARCVLLAKP
EDVDAVARAQ GITLPPGLEI LDPEVIRGRY VEPMVELRKS KNLNAPMAEQ QLEDPVVIGT
MMLALDEVDG LVSGLVHSTA NTIRPALQLI KTAPGSSLVS SVFFMLFPEQ VLVYGDCVMN
PHPSAVELAE IARQSAESAQ AFGIAPRVAM ISYSSDSASD EEVEKVREAT RLAQGAAQEL
LIDGPLQYDA AANPAIARDL APGSPVAGRA TVFVFPDLNT GNTTHKAVQR STDGVSLGPM
LQGLRKPVND LPRGAQVDDI VHTIALTAIQ ASVAG
//
