ID A0A2A9CVT6_9ACTN Unreviewed; 716 AA.
AC A0A2A9CVT6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=ATK74_2840 {ECO:0000313|EMBL:PFG18256.1};
OS Propionicimonas paludicola.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Propionicimonas.
OX NCBI_TaxID=185243 {ECO:0000313|EMBL:PFG18256.1, ECO:0000313|Proteomes:UP000226079};
RN [1] {ECO:0000313|EMBL:PFG18256.1, ECO:0000313|Proteomes:UP000226079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15597 {ECO:0000313|EMBL:PFG18256.1,
RC ECO:0000313|Proteomes:UP000226079};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG18256.1}.
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DR EMBL; PDJC01000001; PFG18256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9CVT6; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000226079; 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:UP000226079};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 240..347
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 392..709
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 75808 MW; FA639DEAE85A25D2 CRC64;
MVGTAHPSIG EPDERTSVHG LPSVSDNLTS VSTSIYAASP EGLTGKSMVA VGLIEALTRT
LGSVGVFRPL VRDGVKDPIL QTLIEQPGVS QGYDEGIGVT YDDVRADADA AQATLVERFA
ALKDKHENVV ILGSDYTDVA SPTELNFNAK VAANLNTPVV LVVSGRARDA EGIREAAEGG
LREFRANHVK VLAVIANRVE PELVDAVKAE LAKLTDVLVA VLPCEKLLAA PTVADQFASV
DAKLVLGNPA LLNRESASVL VAAMTLPNVL SRLEPESTVI MPSDRSDMLP GLLLAHTSGS
FPPLAAILLL GGYEIPETIK TLITSIHNEL PIGTTELGTF TSAERMFRLE GAMTSSPRKV
EVARRIFSEN VDVPALLSAL QVHRSEVITP LMFEHQLQEI ARSDRRTIVL PESTDDRILK
SADILLRRGV ARLILLGDAG AIKARATHLG LALAGVEVVD PTDPRLVEQF ATEYARLRAH
KGVTLEQAKD KLKDLSYFGT MMVHLGMADG MVSGAINTTA NTIRPSLEFI KTRPGVSVVS
GSFLMCLPDR VVVYADCAVN PNPTEEQLAD IAISSAATAA GFGIEPRVAM LSYSTGTSGT
GVDVDKVRAA TEIVRQRAPE LALEGPIQFD AAVDPVVAKT KLPESAVAGR ATVFIFPDLN
TGNNTYKAVQ RSSGAVAIGP VLQGLNKPVN DLSRGALVED IVNTVAITAI QAQAAK
//
