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Database: UniProt
Entry: K6V0C7_9ACTN
LinkDB: K6V0C7_9ACTN
Original site: K6V0C7_9ACTN 
ID   K6V0C7_9ACTN            Unreviewed;       702 AA.
AC   K6V0C7;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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:GAB89278.1};
GN   ORFNames=GORHZ_055_00620 {ECO:0000313|EMBL:GAB89278.1};
OS   Gordonia rhizosphera NBRC 16068.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1108045 {ECO:0000313|EMBL:GAB89278.1, ECO:0000313|Proteomes:UP000008363};
RN   [1] {ECO:0000313|EMBL:GAB89278.1, ECO:0000313|Proteomes:UP000008363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 16068 {ECO:0000313|EMBL:GAB89278.1,
RC   ECO:0000313|Proteomes:UP000008363};
RA   Takarada H., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA   Ohji S., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia rhizosphera NBRC 16068.";
RL   Submitted (AUG-2012) 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:GAB89278.1}.
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DR   EMBL; BAHC01000055; GAB89278.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6V0C7; -.
DR   STRING; 1108045.GORHZ_055_00620; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000008363; 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; 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:UP000008363};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          212..322
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          370..687
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   702 AA;  74645 MW;  EADDEFDDA7116663 CRC64;
     MGERNVTSST IYIASVEGDT GKSTVALGML ALLSATGGRV GVFRPISRAA AGERDYILDL
     LIDHVSVDIP YEDCIGVTYE QVHADPEAAI AEIVARFHAV QARCDTVLVI GSDYTDVASP
     SELSYNARIA ANLSAPIILA VKAAGRTPAE VHDLAVLALS EVSGAHATTA ALIANRCDPE
     QLVVVGKELQ KTGIPIWCLP EDPVLFAPTM AELMEALGAE LYSGDEALLD REALLVMVGG
     MTVEHILERL TDGTVVIAPA DRSDVLLSLV NANTAQGFPR LTGIILNGGL QPHPMIEALV
     NGLKPSLPII MCEQGTYETA RTAALTRGRV GVESVRKIDA ALALMEEYVD SEAILRVLDV
     RGPAVMTPQM FEYALLARAR SQQRHIVLPE GEEDRILRAA GRLLRRGVAR LTLLGNTDAV
     HTRAAELGIA LDGVDVIDPR TSDYLDEFAT IYTDLRKHKG MDFERAQETM HDVSYFGTMM
     VHTGKADGMV SGSVHTTAHT IRPAFEIIKT KPGVSTVSSV FFMCLSDRVL TYGDCAVVPD
     PTDEQLADIA ISSAETAAQF GIDPRVAMLS YSTGKSGSGA DVDKVRVATE LVRERAPEIL
     VEGPIQYDAA VEPSVAATKM PDSPVAGQAT VLIFPDLNTG NNTYKAVQRS AGAIAIGPVL
     QGLNKPINDL SRGALVSDIV NTVAITAIQA QQAPTDVEGG TR
//
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