ID A0A371NU66_9MICO Unreviewed; 704 AA.
AC A0A371NU66;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DY023_08110 {ECO:0000313|EMBL:REJ05898.1};
OS Microbacterium bovistercoris.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2293570 {ECO:0000313|EMBL:REJ05898.1, ECO:0000313|Proteomes:UP000262172};
RN [1] {ECO:0000313|EMBL:REJ05898.1, ECO:0000313|Proteomes:UP000262172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-LLE {ECO:0000313|EMBL:REJ05898.1,
RC ECO:0000313|Proteomes:UP000262172};
RA Ling L.;
RT "Isolation, diversity and antifungal activity of Actinobacteria from cow
RT dung.";
RL Submitted (AUG-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:REJ05898.1}.
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DR EMBL; QUAB01000039; REJ05898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371NU66; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000262172; 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:UP000262172};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 222..333
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 380..696
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 704 AA; 74439 MW; 70210B266FE51A65 CRC64;
MAQSIYITSA EGHTGKSTIA LGVLDALMRV SPRVGVFRPI ARSTTERDDI LELLIAHDGV
QLDYDECIGV TYDDVRADPD TALATIVARF KAVEAQCDAV VVLGSDYTDV ASPAELGYNA
RVAANLGAPV LLVLSGRDQQ TQAERLGTTT ARTPAQVGQM ASLALAELAA ERAELFAVIV
NRADPDALQQ TVEIVEAAPP KRTPVWAIPE DRSLVAPSMR GVLRAVDGRL LKGDPALLDR
EALDVVISGM SMVNVLPRIT EGAVVVIAAD RTEVLLAALL ASASGTFPQI AGIVLNGPFE
LPEPIEQLLE GFEIGVPIVA TDLGTFDTAT HIMNTRGRLS VQSGQRYDKA LGLFQRNVDL
TELTIELGLA ESSVVTPLMF EYGLIERARA DRKRIVLPEG GDDRILRAAA ILLARDVADL
TILGDETDIR ARASALGLDL GAAQILSPTD PELVERFAAE YARLRAHKGV TMQQAADTVT
DVSYFGTMMV HLGLADGMVS GAAHTTAHTI RPAFEIIKTR PGVEVVSSVF LMALADRVLV
YGDCAVIPEP TSVQLADIAI SSAATARQFG IDPRVAMLSY STGESGSGAE VDKVRAATAL
VRERAPELPV EGPIQYDAAA DAAVARAKLP DSAVAGRATV FVFPDLNTGN NTYKAVQRSA
GAVAMGPVLQ GLNKPINDLS RGALVDDIVN TVAITAIQAQ GENR
//
