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Database: UniProt
Entry: A0A327Z6F0_9ACTN
LinkDB: A0A327Z6F0_9ACTN
Original site: A0A327Z6F0_9ACTN 
ID   A0A327Z6F0_9ACTN        Unreviewed;       688 AA.
AC   A0A327Z6F0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=B0I29_113189 {ECO:0000313|EMBL:RAK32892.1};
OS   Actinoplanes lutulentus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK32892.1, ECO:0000313|Proteomes:UP000249341};
RN   [1] {ECO:0000313|EMBL:RAK32892.1, ECO:0000313|Proteomes:UP000249341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK32892.1,
RC   ECO:0000313|Proteomes:UP000249341};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
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:RAK32892.1}.
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DR   EMBL; QLMJ01000013; RAK32892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327Z6F0; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000249341; 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   Reference proteome {ECO:0000313|Proteomes:UP000249341};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          210..319
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          366..682
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   688 AA;  72258 MW;  A6DF98D7BB3CE23C CRC64;
     MARSVYVAGL GPGVGKGTVA LGIVELLSRR VAQVAVFRPL VAGQDRDPLL SVLRDRYPGP
     VPYEESFGVT MAEASALVAD GRREELIGRI VERYRDVERR SAAVVVIGSD FSDKADEGRE
     ELPRELAFNA RLATEFGSVV VPVVSGEGRT PESLAAAARS AYHSLVDLGA TVLAVIANRV
     PFDLEKIAGL PVPVWAMPEV AAIAAPTVAE VAAALDATVF MGTPSALDRD VLDYVVGAAQ
     VPTVLKHLTE GALLITPGDR ADLLVAASAA HAAGTATLAG LVLTLGEPPD PQAVEVIERL
     NTGLAILISQ ADSYHTIAAA GRIKAELSTP RKVEAALGVF EKNVDTAELS RMLDVARSSR
     VTPLMFENDL IDKARGDRRH LVLPEGTEER ILRATETLLR RDVADLTLLG DPAEITRRAR
     EIGVEIGGAQ LVDPSSSQWR EDFASRYAEL RKHRGVTLDL AFDVVRDVNY FGTMMVAAGL
     ADGMVSGANH TTAATIRPAF EIIKTVPGLS VASSVFFMLL ADRVLVYGDC AVNPDPDAAQ
     LADIALSSAQ TAAAFGIEPR VAMLSYSTGS SGSGADVEKV AAATALVRER RPDLPVEGPI
     QYDAAIDPAV AAAKLPGSLV AGKATVFVFP DLNTGNNTYK AVQRSANAVA VGPVMQGLRA
     PVNDLSRGAT VKDIVNTVAI TAIQAGAK
//
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