ID   PTA_ACIAD               Reviewed;         720 AA.
AC   Q6FEP2;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=ACIAD0540;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Involved in acetate metabolism. {ECO:0000250}.
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   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 2/2.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC       acetyltransferase and butyryltransferase family. {ECO:0000305}.
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DR   EMBL; CR543861; CAG67466.1; -; Genomic_DNA.
DR   RefSeq; WP_004920051.1; NC_005966.1.
DR   AlphaFoldDB; Q6FEP2; -.
DR   SMR; Q6FEP2; -.
DR   STRING; 62977.ACIAD0540; -.
DR   EnsemblBacteria; CAG67466; CAG67466; ACIAD0540.
DR   GeneID; 45233019; -.
DR   KEGG; aci:ACIAD0540; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_3_0_6; -.
DR   OMA; FFMCLAD; -.
DR   OrthoDB; 1301815at2; -.
DR   BioCyc; ASP62977:ACIAD_RS02455-MON; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000430; 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   Gene3D; 3.40.1390.20; -; 1.
DR   Gene3D; 3.40.50.10750; -; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF07085; DRTGG; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..720
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405544"
FT   REGION          389..720
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   720 AA;  77882 MW;  2657B1A8C48606CB CRC64;
     MNTILMIPTG EGVGLTSACL GLIYALDCNG IKAGFLKPFS QELPNQVDRT TSLFSHLFQG
     KTVTSISHEK VLQRLALGER DELLEEAVSI HRNVAANYDV IIVEGLLPNA QDHFATELNA
     ALAQALDAKV VLVSTADVQN PRRTAEKIEA HLHHFGGVSS NRTAGVLFMR TRGLPEETAQ
     IPLTIDPSLR LNTEIAAFSQ ELQRYNRNLG TTTLPIIGLV PFSNTLSVPR TLDIASIIEG
     DWIHQGEARH RRILHSSLIA SSIEYELNKF VAGELIISAS ERTDVLLASS LATSNGIPLA
     GLVLTERKAP NPQILDFCQH AIKQGLPILH TQLNTLETAQ RLADFGNEIP VDDTERAEQV
     TRFVSSHIDT AWLNSQINTG VQPRLSPSAF RHELVQKSIA AKKRIVLPEG DEPRTVQAAA
     ICQSRGIAHC ILLAKPEAVV EVAKARGIEL PDDLEIIDPD LIRNQYITPM VELRNGKLNE
     LQAKEQLQDT VVLGTMMLAL DQVDGLVSGA IHTTANTVRP AFQLIKTAPD YSLVSSVFFM
     LLPDEVYVYG DCAINPDPDA DQLAEIAIQS ADSAKAFGIN PRIAMISYST GTSGAGADVE
     KVAKATEIAK QRRPDLLIDG PLQYDAASVE SVGRQKAPDS QVAGRANVFI FPDLNTGNTT
     YKAVQRSANV VSVGPMLQGL NKPVNDLSRG ALVDDIVFTI ALTAIQAEQQ LEAKAAALAS