ID A0A1N6QMX4_9ACTN Unreviewed; 715 AA.
AC A0A1N6QMX4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05421833_10147 {ECO:0000313|EMBL:SIQ17706.1};
OS Microbispora rosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=58117 {ECO:0000313|EMBL:SIQ17706.1, ECO:0000313|Proteomes:UP000186096};
RN [1] {ECO:0000313|EMBL:SIQ17706.1, ECO:0000313|Proteomes:UP000186096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIQ17706.1,
RC ECO:0000313|Proteomes:UP000186096};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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}.
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DR EMBL; FTNI01000001; SIQ17706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6QMX4; -.
DR STRING; 58117.SAMN05421833_10147; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000186096; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 229..343
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 388..705
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 715 AA; 75338 MW; 8C88EF112C5DD1A0 CRC64;
MTFDWYLRRA LRIALPGRAV GPRLDRGDCA MAIGVYVAAG DARSNKGTIA LGMIELLTRQ
VGTVGVFRPV VRSGREDSLV NTVRSRFGIG LPYAMCTGVT YEEVHADEER AAGEILARYR
ALAGRCDAVV VIGTDYTDVG APTEFVFNAE LAANLGTPVM NVVTGLDRTP DDIAAAVEMS
RKELAERHAT ELATVVTGVV PGLVDEVAAR VPAYVLPEVR RLSAPTVSDL MAACDGDLFI
GDADQLGRET GGLMIGAMSL PNILERLTEG LAVVVPADRA AALVPGLLAA HKAPTFPALS
AIILNGGLEL PDAVVRLLKG MDIRLPIITT GGGTFETATK LSKAEGRFSP DAKGKIDTAL
GVFAEHVDGG ALLRSLQVTK AAAITPLMFE YDLLDRARAD RRHIVLPEGA EPRILRAADS
LLRRGVAELT LLGDEREIRL AAATMGLAVD GARVVSPFDP ELRELFAEEY ARLRAHKGVT
AGQARDIVTD VSYFGTMMVH LGLADGMVSG AAHTTAHTIR PSFEIIKTSP GVGVVSSVFF
MCLADRVLVY GDCAVVPDPT AAQLADIAIS SAATAARFGV EPRVAMLSYS TGESGAGPEV
DKVREATARV RELRPDLPVE GPIQYDAAAE PSVARTKMPG SPVAGRATVF VVPDLNTGNN
LYKAVQRSAG AVAIGPVLQG LRKPVNDLSR GATVGDIVNT VAITAIQAQA HREAQ
//
