ID A0A3Q9FJZ9_9BACT Unreviewed; 697 AA.
AC A0A3Q9FJZ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=EI427_06340 {ECO:0000313|EMBL:AZQ61870.1};
OS Flammeovirga pectinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ61870.1, ECO:0000313|Proteomes:UP000267268};
RN [1] {ECO:0000313|EMBL:AZQ61870.1, ECO:0000313|Proteomes:UP000267268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12M1 {ECO:0000313|EMBL:AZQ61870.1,
RC ECO:0000313|Proteomes:UP000267268};
RA Bae J.-W., Jeong Y.-S., Kang W.;
RT "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT scallop, Patinopecten yessoensis.";
RL Submitted (DEC-2018) 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; CP034562; AZQ61870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9FJZ9; -.
DR KEGG; fll:EI427_06340; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000267268; Chromosome 1.
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:UP000267268};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 215..327
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; 76005 MW; 03D01462C19B3E68 CRC64;
MTNSIYISTA EPNSGKALVA LGILENSLRK SSKVGFFKPV IGDYQSGKGD EHISLVIEHF
GLNLTHEEAY GLTLKKANEL ISQGKKDEML EIVISKYKKL EERFDFILIE SSDYKNSITL
EHSLNIEFAK NLASPVLVLT NANNKSVHEC TDALRVSIDD FSSNDCKVIG AVVNRVEADI
INELNVVLAD NFAQEEMLLA TIPGDERISS PTIRDIAEHL KAKVLYGEDN LDVLVDNITI
AAMQMQNFLP KVKPNSLVIT PGDRGDIVLG TISAHRSQSY PNIAGILLTT GLAPDESIKR
VIEGMQDMIP VLSVDHNTYV TANDANEVTA SMRANDLTRI SYAKELFAKH VDNKLLDNLL
STVKVEGMTP KMFQYMLTQR AKQKRSRIVL PEGNDPRILE ASAILATQNI VDIILLGKEE
EIIDVARNNH VNIDFSQVEI IDPVKYSKFN EYVNTLYELR KHKGMNLDMA TDAMSDVSYF
GTMMVQMGDA NGMVSGAVHT TAATIRPALQ IIKTKPGTSV VSSVFFMSLP DRVLVYGDCA
VNPNPNSEQL SEIAISSAET AMSFGIEPKI AMLSYSSGAS GSGEEVEKVR KATAIAKEKR
PDLKIEGPIQ YDAAVDAKVG AQKMPGSDVA GQANVLIFPD LNTGNNTYKA VQRETGALAI
GPVLQGLNKP VNDLSRGCLV EDVLNTVIIT AIQGNQS
//
