ID A0A2X0IFX0_9ACTN Unreviewed; 719 AA.
AC A0A2X0IFX0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DN069_28210 {ECO:0000313|EMBL:RAG82321.1};
OS Streptacidiphilus pinicola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptacidiphilus.
OX NCBI_TaxID=2219663 {ECO:0000313|EMBL:RAG82321.1, ECO:0000313|Proteomes:UP000248889};
RN [1] {ECO:0000313|EMBL:RAG82321.1, ECO:0000313|Proteomes:UP000248889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS16-CNU450 {ECO:0000313|EMBL:RAG82321.1,
RC ECO:0000313|Proteomes:UP000248889};
RA Roh S.G., Park S., Kim M.-K., Yun B.-R., Park J., Kim M.J., Kim Y.S.,
RA Kim S.B.;
RT "Streptacidiphilus pinicola sp. nov., isolated from pine grove soil.";
RL Submitted (JUN-2018) 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:RAG82321.1}.
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DR EMBL; QKYN01000117; RAG82321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0IFX0; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000248889; 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 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:UP000248889};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 210..320
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 367..699
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 719 AA; 76478 MW; 1302203BDF85272F CRC64;
MARSVYVTGI GRGDGRQAVE LGVMELLTRH VDRVGLFRPL VHPPTDHVVE LLRGRYRVDL
PREALYGLSY DEAAAIQAER GQEELVGLLV DRFRAVERDC EAVLVLGTDF ASTNIPDELA
LNARLANEFG AGVLPVIGGH RESAETVVNE VRNAHRSYTD LGCSILAMVA NRVAPGDKQA
VARRLAKGPD VPCYVIPDDP ALSAPTVTQV AEATHAEVLL GDPAGLARDV RRFVFGGAML
PKFLDALSDG CLVITPGDRA DLLIGSLAAH AAGAPPIAGV LLTLGETPGP TVMKLAERLA
PGTPVLAVQE GSYPTAMDLS TLEGKLTAAS PRKAETALGL FELHVDTAEL TDRIELTRTE
RVTPMMFEHE LLERARGATL REIVLPEGAE ERVLRAAEVL LRRNVCHLTL LGAEDAVRRK
VAELGLNLTF EVEDVADEAN GARARARIID PVTSPLRDRF AEVYAELRKH KGMTVELALD
VVSEVSYFGT LMVQEGLADG MVSGAVHSTA ATIRPAFEII KTSPEAKIVS SVFFMCLADR
VLVYGDCAVN PDPDAEQLAD IAIQSAATAG RFGVSPRVAM LSYSTGTSGS GADVDKVRKA
TELVRGQRPD IQVEGPIQYD AAVDPSVART KLPGSAVAGQ ASVLIFPDLN TGNNTYKAVQ
RSAGAIAVGP VLQGLRKPVN DLSRGALVQD IVNTVAITAV QAQQAAAHQA AARQKENGQ
//
