ID A0A5C6A5W4_9BACT Unreviewed; 699 AA.
AC A0A5C6A5W4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 15.
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:TWT94826.1};
GN ORFNames=Pla108_36770 {ECO:0000313|EMBL:TWT94826.1};
OS Botrimarina colliarenosi.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Pirellulales;
OC Lacipirellulaceae; Botrimarina.
OX NCBI_TaxID=2528001 {ECO:0000313|EMBL:TWT94826.1, ECO:0000313|Proteomes:UP000317421};
RN [1] {ECO:0000313|EMBL:TWT94826.1, ECO:0000313|Proteomes:UP000317421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pla108 {ECO:0000313|EMBL:TWT94826.1,
RC ECO:0000313|Proteomes:UP000317421};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op Den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) 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:TWT94826.1}.
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; SJPR01000006; TWT94826.1; -; Genomic_DNA.
DR RefSeq; WP_146446374.1; NZ_SJPR01000006.1.
DR AlphaFoldDB; A0A5C6A5W4; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000317421; 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 FunFam; 3.40.50.10750:FF:000001; Phosphate acetyltransferase; 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; IPR050500; Phos_Acetyltrans/Butyryltrans.
DR InterPro; IPR002505; PTA_PTB.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR NCBIfam; NF004167; PRK05632.1; 1.
DR NCBIfam; NF007233; PRK09653.1; 1.
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:UP000317421};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 214..327
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 372..689
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 699 AA; 74709 MW; 98A8DC68076299BD CRC64;
MSNAAYVVAW EPHSGKSLVV LGLMELLSRR VERLAYFRPL VDGDPEADPH LRLVRERYRL
ATPIGQMVGV NLNRAEQLVA EGQEATLIKE VLARFRACAA EVDFVLCEGT DYVGGQAALE
FDFNSRLAVH LGAPVVTVGA GVGRSAEETI RGARSAHATF VEQGNVIAAS FVNRVAPDQA
EAMREEFRRR PFGDGPVYVL DEEPSLARPT LAQVATAIGA RWLHDPGDVA ERDIATCRVA
AMTLPNFLNH TADGALVITP GDRSDILLGS VASLISDGVP KAAGVLLTGG LTPETSVQRL
LDGMRRWLPP LMAIDCDTYS AATAVEAVRP VIAPENATKI AAALGAFERV VDLAALAERI
AVTRTERVTP LMFEYDLIER AKKAPRTIVL PEGQDDRILR AAAVLLRRQV ASLVILGDPE
TITARAATLG LDLTGAKLMD PHTSPDRQRL ADELARLRAH KGVTQAMAYD QLGDPNYFGT
MMVEVGDADG MVSGAMHTTA QTIRPALQVI RTRPECSIVS SVFLMCLADR VLVYGDCAVN
PDPTPEQLAD IAISSADTAR RFGVTPRVAM LSYSTGASGT GAAVDKVREA TRLVRERAPD
LSVEGPIQYD AAVDASVAKS KLPGSQVAGQ ATVFVFPDLD SGNNTYKAVQ RSARAVAIGP
ILQGLRKPVN DLSRGCLVDD IVNTVAITAI QAQPEEAAE
//
