ID A0A2V1HUW3_9MICO Unreviewed; 706 AA.
AC A0A2V1HUW3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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=DDQ50_05980 {ECO:0000313|EMBL:PVZ96395.1};
OS Amnibacterium flavum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Amnibacterium.
OX NCBI_TaxID=2173173 {ECO:0000313|EMBL:PVZ96395.1, ECO:0000313|Proteomes:UP000244893};
RN [1] {ECO:0000313|EMBL:PVZ96395.1, ECO:0000313|Proteomes:UP000244893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8JJ-5 {ECO:0000313|EMBL:PVZ96395.1,
RC ECO:0000313|Proteomes:UP000244893};
RA Tuo L.;
RT "Amnibacterium sp. M8JJ-5, whole genome shotgun sequence.";
RL Submitted (MAY-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:PVZ96395.1}.
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DR EMBL; QEOP01000001; PVZ96395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1HUW3; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000244893; 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:UP000244893};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 222..335
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 380..697
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 706 AA; 74526 MW; 259A9D1765654A3A CRC64;
METRNVYITS VEGDTGKSTV ALGVLDTLTH ELDRVGVFRP VARSTSERDY VLELLLEHDG
VDLAYEDCIG VSYDDVHANP EAALSRIVDR YKAVEAQCSA VVILGSDYTD VGTPTELSFN
ARVAANLGAP VVLVLGGRAA QHGGELTAPR ARTADELAQI AEVAVGELHN EHATLLAVVA
NRVDPAILQA VRFSVGLSVH DQGVPVWAIP EDVMLVAPTM QNLLDATGGT LVTGDAAMLQ
RSVYGVVVAG MSMVNVLPRL TEGAVVVVPS DRVEVLVAAL LAQSSGTFPS LAGILLNGGF
PLPEQIERLI EGVEVNLPIV TTPLGTYETT LRVTRARGRL AAESPAKFEQ ALALFERSVD
RKALVDLLEV KRTTITTPLM FEHRLLEQAR AAGSHIVLPE GGDDRILLAA DRLLRRDVVK
LTILGDEAEI RARASSLGAD LSAASIVSPL DPELRQRFAE EYTRLRAHKG MTIDIALNVV
TDVSYFGTMM VHLGLADGMV SGAAHTTAHT IRPSFEIIKT KPGVSVVSSV FLMALADRVL
VYGDCAVIPD PTSDQLADIA VSSATTASAF GIDPRIAMLS YSTGESGEGA DVEKVRAATA
LVRERRPDLL VEGPIQYDAA ADVAVAAAKL PGSAVAGRAT VFIFPDLNTG NNTYKAVQRS
AGAVAIGPVL QGLNKPVNDL SRGALVHDIV NTVAITAIQA GNEAAS
//
