ID A0A5B8V0B8_9SPHI Unreviewed; 705 AA.
AC A0A5B8V0B8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 16.
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=FRZ54_19755 {ECO:0000313|EMBL:QEC64702.1};
OS Mucilaginibacter ginsenosidivorans.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=398053 {ECO:0000313|EMBL:QEC64702.1, ECO:0000313|Proteomes:UP000321479};
RN [1] {ECO:0000313|EMBL:QEC64702.1, ECO:0000313|Proteomes:UP000321479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 3017 {ECO:0000313|EMBL:QEC64702.1,
RC ECO:0000313|Proteomes:UP000321479};
RX PubMed=28821948; DOI=.1007/s00284-017-1329-4;
RA Kim M.M., Siddiqi M.Z., Im W.T.;
RT "Mucilaginibacter ginsenosidivorans sp. nov., Isolated from Soil of Ginseng
RT Field.";
RL Curr. Microbiol. 74:1382-1388(2017).
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}.
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DR EMBL; CP042436; QEC64702.1; -; Genomic_DNA.
DR RefSeq; WP_147033536.1; NZ_CP042436.1.
DR AlphaFoldDB; A0A5B8V0B8; -.
DR KEGG; mgin:FRZ54_19755; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000321479; 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 CDD; cd03109; DTBS; 1.
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:UP000321479};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 215..325
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 372..691
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 705 AA; 77909 MW; 228958747E0734E6 CRC64;
MIKTVFIAST EAHSGKSIVS IGLVNMLLGK AQKIGYYKPV ISQNLLVKKD DHIDTILTHF
DLPMTYDDTF ALTWQEAMGQ METESQGEML DIIIRKYKSL EEKYDFIVVE GTDYPGEGAA
FEFETNAQIA KNLQAPVIVV VSGEDKTIAQ VVSAALTAIH NFDAREVQVL AIVANRIRQE
HAKDVEELLR HQLSPEILLA IIPLDTRLQS PTMKEIYEQL NGKLLFGEDH LSNQADNFVT
GAMQVPNFLN YLTENVLIVT PGDRGDIIIC ALQANLSTSY PKVAGIVLTA GYQPEEPILR
LIEGLQTVVP IISVETGTFQ TSNVIGDIRS QITSDNTKKI RLAIDTFNKY VNTSELDKRL
VTFKPSGLTP RMFQYQLTEW ARSSKKHIVL PEGNDERILR AAARLISQEI VDLTLLGDTA
DIKAVLNRLD INLDLDKVRI VNPAYDQYYD DYVNTLYELR KSKNVTLEMA RDLMTDVSYF
GTMMVYKGHA DGMVSGAVHT TLHTIRPALQ FIKTKPGISV VSSIFFMCLP DRVSIFGDCA
VNPNPTAEQL AEIAISSADS SQRFGIEPRI AMLSYSSGTS GEGEEVEKVR RATEIVKQKR
PDLKVEGPIQ YDAAVDPVVG SSKLPGSEVA GRASVLIFPD LNTGNNTYKA VQRETGALAI
GPMLQGLNKP VNDLSRGCTV DDIFNTVIIT AIQCQDTSQT LEKHS
//
