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Database: UniProt
Entry: H0QXV1_9ACTN
LinkDB: H0QXV1_9ACTN
Original site: H0QXV1_9ACTN 
ID   H0QXV1_9ACTN            Unreviewed;       703 AA.
AC   H0QXV1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
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:GAB17652.1};
GN   ORFNames=GOEFS_036_00910 {ECO:0000313|EMBL:GAB17652.1};
OS   Gordonia effusa NBRC 100432.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB17652.1, ECO:0000313|Proteomes:UP000035034};
RN   [1] {ECO:0000313|EMBL:GAB17652.1, ECO:0000313|Proteomes:UP000035034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB17652.1,
RC   ECO:0000313|Proteomes:UP000035034};
RA   Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL   Submitted (DEC-2011) 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:GAB17652.1}.
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DR   EMBL; BAEH01000036; GAB17652.1; -; Genomic_DNA.
DR   RefSeq; WP_007316990.1; NZ_BAEH01000036.1.
DR   AlphaFoldDB; H0QXV1; -.
DR   STRING; 1077974.GOEFS_036_00910; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000035034; 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   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; 2.
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:UP000035034};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          213..325
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          371..688
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   703 AA;  74212 MW;  D93C41D0F4A5326C CRC64;
     MALDTVASNS IYVASSAAET GKSTIALGLL AILSATGGRI GVFRPISRAV SEGERDYILE
     LLLAHDSVDL SYDECIGVTY DQVNEDAEGA ISEIVARFHA VQAQCDTVLV VGSDYTDVGN
     PSELGFNARI AANLSSPIVL ALNASGRSAD EVVGSAEHAL HEVSAAHATA VAVVANRCEP
     DLLNGITKAL KAIPVASWAL PEVPILSAPT MGELSEALGG YLYSGDADLL DREALNVMVG
     GMTVEHILER LVDGTAVITP ADRSDVLLAL VNANAAQGFP RLAGIILNGG LKPHPMIQAL
     VNGLNPTLPI ISCEQGTYDT ARIAAHTRGR VAYQSARKIE AALALMEEHI DVDQILKEVD
     LDIPAVVTPQ MFEYQLVARA KADRRHIVLP EGEEDRILRA TGHLLRRGVA RLTLLGDIDI
     VAKKAGALDI DLTDVDVIDP LTSELTEQFA QTYAELRKHK NVALDRARDL MRDVSYFGTM
     MVHLGMADGM VSGAVHTTAH TIRPSFEIIK TKPGVSTVSS VFFMCLADEV LTYGDCAVVP
     DPTDTQLADI AISSAETASV FGIDPRIAML SYSTGESGTG ADVDKVRAAT EMVRERSPEL
     LVEGPIQYDA AIEPSVAATK MPDSPVAGKA TVLIFPDLNT GNNTYKAVQR SAGAIAIGPV
     LQGLNKPIND LSRGALVADI VNTVAITAIQ AQNLANSAGG QDK
//
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