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Database: UniProt
Entry: A0A1Y6KY45_9GAMM
LinkDB: A0A1Y6KY45_9GAMM
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ID   A0A1Y6KY45_9GAMM        Unreviewed;       715 AA.
AC   A0A1Y6KY45;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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   Name=pta {ECO:0000313|EMBL:SMY17061.1};
GN   ORFNames=PAQU9191_02308 {ECO:0000313|EMBL:SMY17061.1};
OS   Photobacterium aquimaris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=512643 {ECO:0000313|EMBL:SMY17061.1, ECO:0000313|Proteomes:UP000196485};
RN   [1] {ECO:0000313|Proteomes:UP000196485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=type strain: CECT 9192 {ECO:0000313|Proteomes:UP000196485};
RA   Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL   Submitted (JUN-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; FYAH01000003; SMY17061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6KY45; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000196485; 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   Reference proteome {ECO:0000313|Proteomes:UP000196485};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          233..344
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          391..706
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   715 AA;  76942 MW;  969B207D7F06F49D CRC64;
     MSRTIMLIPV GAGVGLTSVS LGVLRAMERK GVRVSFFKPI AQPRHGGDQP DLTTTIIRAN
     STMELADPFS MASAEELIRN DKTDVLLEDI VARFKAATAN AEVALIEGLV PTRKHPFANQ
     INYEIAKTLD AEIVFVVSPG TDNPAQLKER IEVACSNFGG IKNKQISGVI VNKLNAPVDS
     EGRTRPDLSE IFDDVEGTVP SNVEIMQVFN SSPIRVLGCA PWSAELIATR ATDIAQHLNA
     EIINTGDLET RRIKSITFCA RSIPNMVEHF RPGSLLVTSA DRPDVIVAAC LAAMNGVELG
     ALLLTGGYDL PKPVMDLCER AFATGLPVMT AQGNTWQTSL NLQSFTLEVP ADDKERVELV
     NEYMASHIDG NWIESLSEGS TRERRLSPPA FRYQLTELAR KAAKRIVLPE GDEPRTVKAA
     AICAERGIAE CVLLGNPEEI RRVAEQQGVV LGAGVTIINS DEVRENYVAR LVELRGAKGM
     TDVVAREKLQ DSVFLGTMML ENDEVDGLVS GAVHTTANTI VPPFQIIKTA PDASIVSSVF
     FMLLPDQVLV YGDCAINPDP TAEQLAEIAI QSADSAKAFG IEPRVAMISY STGTSGKGAD
     VDKVREATKL AQEKRPDLII DGPLQYDAAI MENVAASKAP NSPVAGKATV FVFPDLNTGN
     TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TVALTAIQAE QANAK
//
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