ID   PTA_DESVH               Reviewed;         704 AA.
AC   Q726S7;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=DVU_3029;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(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}.
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; AE017285; AAS97500.1; -; Genomic_DNA.
DR   RefSeq; WP_010940288.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_012240.1; NC_002937.3.
DR   AlphaFoldDB; Q726S7; -.
DR   SMR; Q726S7; -.
DR   IntAct; Q726S7; 3.
DR   STRING; 882.DVU_3029; -.
DR   PaxDb; Q726S7; -.
DR   EnsemblBacteria; AAS97500; AAS97500; DVU_3029.
DR   KEGG; dvu:DVU_3029; -.
DR   PATRIC; fig|882.5.peg.2747; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_3_0_7; -.
DR   OMA; FFMCLAD; -.
DR   PhylomeDB; Q726S7; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000002194; 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..704
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405547"
FT   REGION          380..704
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   704 AA;  76830 MW;  C0459B13A61D8DAA CRC64;
     MSNNLYITAT ESKSGKSAVV LGMMQLLLRD VRKVAFFRPI INQASTDVRD HDINLILRHF
     GLDIAYEDTY AYSLQDAREL INNGQHATLL DNILKKYKKL EDAYDFVLCE GTDFLGKDAA
     FEFELNADIA ANLGCPVMVV ANGQQKAARE LIASTQLTID LLDEKGLDVV TAVINRATVT
     EAEREEIIKS LECKVNCSNP LAVYVLPEES TLGKPTMNDV KKWLGAQVLY GHGRLDTLVD
     DYIIAAMQIG NFLDYVSQGC LVITPGDRSD IILSSLASRL STAYPDISGL LLTGGLEPAA
     NVHRLIEGWT GVPIPILSVK DHTYKTIQTL NELYGKIEPD NDRKINTALA LFERHIDSSE
     LGSRLINRKS SRITPKMFEF NLIEKAKRNR MRIVLPEGAE ERILRAADIL VRREVADIIL
     LGDANTVGSR IGDLGLDMDG VQIVQPNLSP KFDEYVAAYH ECRKKKGISM EQARDMMNDP
     TYFGTMMVHK GDADGMVSGA INTTAHTIRP AFEFIKTKPG VSIVSSVFLM CLKDRVLVFG
     DCAVNPNPTA EQLAEIAISA SHTARIFGVD PRVAMLSYST GSSGKGADVE KVIEATRIAK
     ERAPELLLEG PLQYDAAIDM DVARTKLPGS TVAGQATVFI FPDLNTGNNT YKAVQRAAGA
     VAIGPVLQGL NKPVNDLSRG CTVADIVNTV AITAIQAQAE KGLI