ID A0A0S8IBA4_9DELT Unreviewed; 712 AA.
AC A0A0S8IBA4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
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 ORFNames=AMJ94_01215 {ECO:0000313|EMBL:KPK94623.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK94623.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK94623.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK94623.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- 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:KPK94623.1}.
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DR EMBL; LJUR01000006; KPK94623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IBA4; -.
DR STRING; 1703399.AMJ94_01215; -.
DR PATRIC; fig|1703399.3.peg.1402; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000051218; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 214..328
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 373..690
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 712 AA; 77639 MW; 5E836ED5FE569A07 CRC64;
MPKAKSIYVF GAEPQAGKSV VLLGIMEVLS RQVQKLGFFR PLVREGETKD DAIRLISNRY
HLPLPNRIKY GMTHEKARAL VAEEKYDEVL KRILEGYGSL ESDCDVVVCL GTGFHDIPPG
LALDFNIDVA NNLGALAAPV ATGWGRTSQE VIRRSLVLLN LLEAKRCDVL ALFVNRVAPE
RVDEILGLLA REKSQVPIFA LPELAMLAKP TVGEIAEYLG ATRWSGDPES FTREVEDIKI
GAMELPNFLN HLVEGTLVIT PGDRSDIILG SLLADAASTY PRVAGLLLTG GLRPAPQVER
IIEGLRKSPV PVLTVEVDTF TAGTQASQVR GRIRPENPRK MAVALGHMEK YMNAQALRQR
IDLSRPERVT PIMFEHSLVE QAKSNRRHIV LPEGTEERIL RAAEILLLRG VADLTLLGPI
SEIEQKASSL GLSLKGAAFL DPAEPEHREE YAHTYYELRK HKGISEQMAF DLVADVAYFG
TLMVHRAEAD GLVSGAVHTT AHTLRPAFEI IGLKPGFSLA SSVFFMCLPD RVFVFGDCAV
NPEPTMEQLA DIATSSAETA WAFGIEPRVA MLSYSTGESG KGADVDKVRE ATRRVRSLRP
DLPVEGPIQY DAAVDPSVAR VKLPGSQVAG RATVFIFPDL NNGNITYKAV QRSANAVAIG
PVIQGLKRPV NDLSRGATVT DIVNTVAITA IQAQETVSQS NAWMRGSQVP KL
//
