ID A0A126Z5F8_9MICO Unreviewed; 708 AA.
AC A0A126Z5F8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AX769_18625 {ECO:0000313|EMBL:AMM21794.1};
OS Frondihabitans sp. PAMC 28766.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM21794.1, ECO:0000313|Proteomes:UP000070552};
RN [1] {ECO:0000313|EMBL:AMM21794.1, ECO:0000313|Proteomes:UP000070552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA Park H.;
RT "Complete genome of Frondihabitans sp.";
RL Submitted (FEB-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; CP014513; AMM21794.1; -; Genomic_DNA.
DR RefSeq; WP_066282197.1; NZ_CP014513.1.
DR AlphaFoldDB; A0A126Z5F8; -.
DR STRING; 1795630.AX769_18625; -.
DR KEGG; frp:AX769_18625; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000070552; Chromosome.
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:UP000070552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 219..331
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 376..693
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 708 AA; 74849 MW; BE170DCA0EB08922 CRC64;
MSTRIYITSA EGHTGKSTVA LGVLDTLSHE LGRVGVFRPV ARSTSEPDYV LELLLAHDSV
DLPYEDCIGV TYDDVHADPD AALATIIGRF AAVERQCDAV VIVGSDYTDV GSPTELSFNA
RIAANLGAPV LLVLGGRAAD GSRARSGVDV RQVAELTTAE LRSEHASLLA VIVNRAEPDR
LAEVVEGIGE ALEASPEGRV PVWALPEDRV LVSPTLRAVM EATQARLVRG DDALLEREAI
GVVVAAMSME NVLPRLTEGA VVVVPGDRSD VLVATVLAHS SDTFPSIAGI ILNGGFDLAP
QVVRLLGGLD SSLPILWNEL GTYDTATRIT QTSGRLAAES PRKYDLALSL FETNVDGDAL
LRLLEISPSK VVTPLMFEYQ LLDRARSVKK HIVLPEGDDD RILRAASSLL QRGVASLTLL
GNEPSVRARG AELGLDLGDA SVLDPTDPEL QLKFATEYAA LRAHKGTTVE MAMDTVTDVS
YFGTMMVKMG LADGMVSGAK HTTAHTIRPA FEVIKTRPEV NVVSSVFLMA LADRVLVYGD
CAVIPDPTSE QLADIAISSA ETAVQFGIEP RIAMLSYSTG DSGSGADVEK VRAATALVRE
RRPELLVEGP IQYDAAADPT VAAAKMPDSD VAGRATVFIF PDLNTGNNTY KAVQRSAGAV
AIGPILQGLR KPINDLSRGA LVSDIINTVA ITAIQAGTAQ PGTEGAFL
//
