ID A0A1I1VQ68_9FLAO Unreviewed; 697 AA.
AC A0A1I1VQ68;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN05216297_112184 {ECO:0000313|EMBL:SFD82670.1};
OS Flavobacterium phragmitis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=739143 {ECO:0000313|EMBL:SFD82670.1, ECO:0000313|Proteomes:UP000199672};
RN [1] {ECO:0000313|EMBL:SFD82670.1, ECO:0000313|Proteomes:UP000199672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10370 {ECO:0000313|EMBL:SFD82670.1,
RC ECO:0000313|Proteomes:UP000199672};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- 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; FOMH01000012; SFD82670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1VQ68; -.
DR STRING; 739143.SAMN05216297_112184; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000199672; 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 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 697 AA; 76400 MW; 4CEB47267A8702B5 CRC64;
MSKAIYIATS DHNSGKSIIT LGLMSILIGK TAKVGYFRPI IEDFVDGEVD NHIETVLSYF
NLDIHFEDAY AITKSRLIKK KNKGKIGEVL DLIIEKYKKL EERFDFVLVE GTSFTGEGTS
IELDLNVLIA KNLGIPTIIV GSGVGKTLEE LLDSLYLVYD SFKLKEVEVL SVFANKVQPE
NIELVTNSLQ KTLPSNVLIN TIPLISSLNN PTMQEIVNEL NAKVLFGENY LNNEIGHYSV
GAMQLHNYLV HLHDNALVIT PGDRSDIILG ALQANESANY PTISGIILTG NIVPEESILK
LIEGLSAIVP IIAVDGGTYH ITNKIGSIKS EIYANNTHKI ETSITTFEKY VDNDALSERL
ITFQAEGMTP KMFQYNMVKR AKQHRKHIVL PEGNDDRIIT AAARLLDMDV VDISIIGDKK
QIENKVVELG ITLDFSKVNI INPIESEFYE DYANTYYELR KAKNVSITMA RDLMEDVSYF
GTMMVYKGHA DGMVSGAAHT TQHTILPALQ FIKTKPNSSV VSSVFFMCLE DRVSVFGDCA
INPNPTAEQL AEIAISSAES SLAFGIEPKI AMLSYSSGSS GKGDEVDKVR TATAIVKEKR
PDLKIEGPIQ YDAAVDLSVG KSKMPDSEVA GQASVLIFPD LNTGNNTYKA VQRETGALAI
GPMLQGLNKP VNDLSRGCTV DDIINTVVIT AIQAQGM
//
