ID   PTA_NITEU               Reviewed;         695 AA.
AC   Q820S1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=NE0298;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84209.1; -; Genomic_DNA.
DR   RefSeq; WP_011110933.1; NC_004757.1.
DR   AlphaFoldDB; Q820S1; -.
DR   SMR; Q820S1; -.
DR   STRING; 228410.NE0298; -.
DR   EnsemblBacteria; CAD84209; CAD84209; NE0298.
DR   KEGG; neu:NE0298; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_4; -.
DR   OMA; FFMCLAD; -.
DR   OrthoDB; 1301815at2; -.
DR   PhylomeDB; Q820S1; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001416; 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..695
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405548"
FT   REGION          372..695
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   695 AA;  74998 MW;  711FE70A7908EC5D CRC64;
     MHTFFVTSTG FGVGLTSTSL GLVRALEYGG LKAGFYKPVA QQHPGNSKLE YSTELISRTL
     GLAPPAPLPL ATVEHLLGEG QIDDLMEDIV RRFKQASEGY DVMVVEGMVP TRHVSYASRV
     NTRLASSLDA DIILVSSAED DALQAITDRI EIQAQFFGGA QNPRLLGVIL NKIRTDHSDD
     LFEQLKNHST LFHQSSFQIL GCIPWEDSLN APRMADVVTQ LQAQIVNAGD SEKRRVQDIV
     LFASAAPNSV TLLRPGVLVV TPGDRDDIVM AASLAVLNGV PLAGLLLCSD FPPDPRVLEL
     CKGALTKGLP VCTVTTNSYD TAANLHRMNR EIPLDDHERA ERITNFVANH IRQELLVKRC
     GEPQEQRLSP PAFRYRLVKR AQEADCRIVL PEGYEPRTIQ AATICQERGI ARCVLLAKPD
     AVKAVASARG ITLPEGLEMI DPEKVRRNYV AAMVELRKHK GLNEPMALAQ LEDNVVLGTM
     MLATGEVDGL VSGAINTTAN TIRPALQLIK TAPGFKLVSS VFFMLLPEQV VVYGDCAVNP
     NPTAEELADI ALQSAASAQA LGIEPRVAML SYSTGDSGSG QEVEKVREAT RLARLARPDL
     LIDGPLQYDA AAIASVGRQK APGSPVAGRA TVFIFPDLNT GNTTYKAVQR SANVVSVGPM
     LQGLRKPVND LSRGASVEDI VYTIALTAVQ AASQR