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Database: UniProt
Entry: A0A1B7Z040_9FLAO
LinkDB: A0A1B7Z040_9FLAO
Original site: A0A1B7Z040_9FLAO 
ID   A0A1B7Z040_9FLAO        Unreviewed;       697 AA.
AC   A0A1B7Z040;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=A9200_10195 {ECO:0000313|EMBL:OBR36058.1};
OS   Maribacter hydrothermalis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1836467 {ECO:0000313|EMBL:OBR36058.1, ECO:0000313|Proteomes:UP000092164};
RN   [1] {ECO:0000313|Proteomes:UP000092164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T28 {ECO:0000313|Proteomes:UP000092164};
RA   Zhan P.;
RL   Submitted (JUN-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}.
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:OBR36058.1}.
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DR   EMBL; LZFP01000049; OBR36058.1; -; Genomic_DNA.
DR   RefSeq; WP_068486639.1; NZ_LZFP01000049.1.
DR   AlphaFoldDB; A0A1B7Z040; -.
DR   STRING; 1836467.BTR34_02340; -.
DR   KEGG; mart:BTR34_02340; -.
DR   OrthoDB; 9805787at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000092164; 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   Reference proteome {ECO:0000313|Proteomes:UP000092164};
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;  76371 MW;  9ECFE8B2C22F977A CRC64;
     MSKAIYIVTT EPNSGKSIVS LGLMQLLLGK TAKVGYFRPI IDDVPNGKTD NHIDTVLSYF
     NVDMKPEEAY AYTRSQVVQL KNKDKDDEIV GHIIHKYKTI ENKFDFVLVE GTDFSGEGAI
     IEWDINVLIA KNLGIPAVIL ASGKNKTLDE LVGNLYMAYD SFKEKGVEVL LIVANKVQPE
     NIKIVYNGLK EKLPNDVLVG AIPLNTVLGS PTLKEIAQEL DAKVLFGENH INNQVGSFSV
     GAMQLRNYLT HLKSDSLVIT PGDRADIILG ALQANISTNY PNLSGIVLTG GLLPEDSIIK
     LIEGLSDIIP ILSVANGTFF VTNKIGTIRP RIYAENKEKI QTSIQEFEKH IPTKELAERL
     ITFKAKGITP RMFQYNLLQK AKSSKKHIVL PEGLDERILL ATKKLIDSGA VYITLLGNRE
     QIIAKITELD IDLDINEINI INPTESDQFL DYATTLFELR KHKNVNLAMA KDLMEDVSYY
     GTMMVHKGHA DGMVSGAIHT TQHTIRPALQ FIKTRPDVSI VSSIFFMCLP NRVTVFGDCA
     INPNPNSEQL SEIAISSAAT SAAFGIEPKI AMLSYSSGAS GVGEDVDRVR KATEIIKEKR
     PDLKVEGPIQ YDAAVDAKVG LSKLPDSEVA GQASVFIFPD LNTGNNTYKA VQRETGALAI
     GPMLQGLNKP VNDLSRGCTV DDIFNTVIIT AIQAQGF
//
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