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
//