ID A0A1G9DAX1_9ACTN Unreviewed; 685 AA.
AC A0A1G9DAX1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05216298_0776 {ECO:0000313|EMBL:SDK61029.1};
OS Glycomyces sambucus.
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Glycomyces.
OX NCBI_TaxID=380244 {ECO:0000313|EMBL:SDK61029.1, ECO:0000313|Proteomes:UP000198662};
RN [1] {ECO:0000313|EMBL:SDK61029.1, ECO:0000313|Proteomes:UP000198662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDK61029.1,
RC ECO:0000313|Proteomes:UP000198662};
RA de Groot N.N.;
RL Submitted (OCT-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; FNGF01000001; SDK61029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9DAX1; -.
DR STRING; 380244.SAMN05216298_0776; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000198662; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 203..314
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 362..678
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 685 AA; 71844 MW; A8A29458C022A7B2 CRC64;
MAQSLYLASL DPGSGKSTVA VGVMDLLTRR AGSVAVYRPI VRDDHTDAGD PIITLLRDQY
RLPASYAASV GVTYSDVRAD ADAALTEIVE RYHELADKHE VVLVVGSDFS DVSSPVEFAY
NTRVAVNLAA PMLLIVTGHR KSPADIAAAL RFGTAQAEAD HATVLGTVVN RVDAADAGLV
QDAHPGTGVV VEDPELIAPT VGELIEAADA TLISGDPDVF TRTVGDVVVA AMTLPNLLTR
LADGKAVILP GDRSEVLLGL IAAHLAEGTP SLSAVFLTGG IRPEPQILDI VAGLDSRLPI
ALVQHDTFDM ANLVGDVTGN LAAGGQRKIT RALEDFAQGV DGDDLLDRLA LSKPAVVTPI
MFEHSMLGRA KALDKHIVLP EGAEPRILKA AEILMRRDVA RLTLLGVEAE IRSQAAQLGV
DISGAAILNP GDHEIRERFA KEYARLRAHK GVTVEAAYDQ VADVSYFGTM MVHTGMADGM
VSGAVHTTAH TIRPSFEIIK TKPEVAVVSS VFFMCLEDRV LVYGDCAVNP NPDAGQLADI
ALSSAGTAAE FGVEPRVAML SYSTGTSGHG EAVDKVRAAT EIVRSRRPDL PVEGPIQYDA
AADAGVAGTK LPDSQVAGKA TVFIVPDLNT GNNLYKAVQR SANAVAVGPV LQGLRKPVND
LSRGATVPDI VNTVALTAIQ ASQTA
//
