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Database: UniProt
Entry: W6M856_9GAMM
LinkDB: W6M856_9GAMM
Original site: W6M856_9GAMM 
ID   W6M856_9GAMM            Unreviewed;       719 AA.
AC   W6M856;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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:CDI01925.1};
GN   ORFNames=BN873_210146 {ECO:0000313|EMBL:CDI01925.1};
OS   Candidatus Competibacter denitrificans Run_A_D11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria;
OC   Candidatus Competibacteraceae; Candidatus Competibacter.
OX   NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI01925.1, ECO:0000313|Proteomes:UP000035760};
RN   [1] {ECO:0000313|EMBL:CDI01925.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI01925.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI01925.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI01925.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA   Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT   "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT   functional metabolic diversity.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDI01925.1}.
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DR   EMBL; CBTJ020000027; CDI01925.1; -; Genomic_DNA.
DR   RefSeq; WP_048671504.1; NZ_CBTJ020000027.1.
DR   AlphaFoldDB; W6M856; -.
DR   STRING; 1400863.BN873_210146; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000035760; 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:UP000035760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          234..339
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          390..705
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   719 AA;  78209 MW;  EDC5C5B6E0F36A75 CRC64;
     MTTAILVVPS EQRVGLTTVA LGLVHALDRE GIPVGFCKPI SQPHASDTGP ERSTRLARMV
     TSLNPPEPIP VSETENLLGH DRENVLLEEV IGRFEQAAHH TSAVIVEGLM DTEEQPYGTR
     LNAKMAQSLD AKIIVVTAPG RDTPRQVADT VEIIARAYGG IHHERMLGAI INLLDAPVDQ
     TGHIRFDFSR AENGYHPGHE AEFRAECTRH WPQTFALLGC IPWQRELSAP RVCDIMQLIG
     AQILNEGQLN RRVTHVVLGA ASLISSCQEL RPGAMVIIPG DRDDLLLAIC MATMSGTHVA
     GVLLAGGLKP DLRVWKLCSP ALDAGLPVLT IPHSALQSVL YLPHLNLEVP LDDRDRMQQA
     VETVASHITL DWKEPLLSRI QERRLSPPAF QHTLVQRARK ANKRIILPEG NEPRTIEAAI
     ICHQRGIARC VLMGDAGRMH RLSARRGMSI PPDIEIIDST QIDRRYIDAL VALRQHKGLN
     SGLAEEALHD AVVLGTLMLQ LGEVDGLVSG AVHTTANTIR PALQLVKTAP DVRLVSSIFF
     MCLPEQVLIY GDCAININPN AEDLADIAIQ SAESAKAFGI IPRVAMLSYS TGTSGSGSDV
     EKVKAATRLA RERRPDLLID GPLQYDAATI KAVAQSKAPD SQVAGRATVF IFPDLNTGNT
     TYKAVQRSAD VISIGPMLQG LNKPVNDLSR GALVEDIVFT IALTAIQAEQ ALERERNQR
//
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