ID   PTA_DEIRA               Reviewed;         702 AA.
AC   Q9RY77;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=DR_0073;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF09663.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AE000513; AAF09663.1; ALT_INIT; Genomic_DNA.
DR   PIR; G75563; G75563.
DR   RefSeq; NP_293799.1; NC_001263.1.
DR   RefSeq; WP_027480235.1; NC_001263.1.
DR   AlphaFoldDB; Q9RY77; -.
DR   SMR; Q9RY77; -.
DR   STRING; 243230.DR_0073; -.
DR   EnsemblBacteria; AAF09663; AAF09663; DR_0073.
DR   KEGG; dra:DR_0073; -.
DR   PATRIC; fig|243230.17.peg.236; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_0; -.
DR   InParanoid; Q9RY77; -.
DR   OrthoDB; 1301815at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000002524; Chromosome I.
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..702
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405546"
FT   REGION          375..702
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   702 AA;  74665 MW;  192F97376746F7D7 CRC64;
     MKTLFLAPTR NGVGLSSTAL GLARALERQS LKVAFLKPIA QTYEPRTDDS VHFARAVAHL
     TTPDPIPLTR AEELLSQGGE EDLMEQVIAL AREAAGEGSD VLIAEGLALN ERNVYAGTLN
     ARLARNLEAD TVLVSSLAGV TPAELADELE IAAQGYRRSD GSGLAGFVLN FAPRELDFGS
     LMAELRSRSR VLASGELPLL GVVSLDPALR QLRTLDVARA LDAEIINAGE AESRRVSSTV
     VTARSVPQMT NLFTSGALIV TPADREDVIM AAALSHLSGT PLAGLMYTSG SAPEATIQQL
     CEVALTSSLP VLRVPTNSFE TASRLVHLDF RVPHDDPRRM DRMLDYIADR LDTVPLGARL
     RAPGVAGERR LPPSAFRYEL IQRARAANKR IVLPEGDEPR TVKAAIRCTE KGIARCVLLA
     PPEKVRQVAQ GQGLELPEGL EIIDPETVRG KYVAPMVELR KSKGLTEPQA EAQLEDSVVL
     GTMMLALGEV DGLVSGAVHT TASTVRPALQ LIKTAPGSSL VSSVFFMLMP EQVLVYGDAA
     INPDPNAQEL ADIAIQSADS AHAFGIPVRV AMLSYSTGES GSGEDVEKVK EATKLVRERR
     PELLVDGPLQ YDAASVPSVG RSKAPDSPVA GRATVFIFPD LNTGNTTYKA VQRSAGVVAV
     GPMLQGLRKP VNDLSRGALV DDIVYTIALT AIQATQSAAD CG