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Database: UniProt
Entry: A0A1V4A9J3_9ACTN
LinkDB: A0A1V4A9J3_9ACTN
Original site: A0A1V4A9J3_9ACTN 
ID   A0A1V4A9J3_9ACTN        Unreviewed;       691 AA.
AC   A0A1V4A9J3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-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=B1H18_13500 {ECO:0000313|EMBL:OON79597.1};
OS   Streptomyces tsukubensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=83656 {ECO:0000313|EMBL:OON79597.1, ECO:0000313|Proteomes:UP000190539};
RN   [1] {ECO:0000313|EMBL:OON79597.1, ECO:0000313|Proteomes:UP000190539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F601 {ECO:0000313|EMBL:OON79597.1,
RC   ECO:0000313|Proteomes:UP000190539};
RA   Zong G., Zhong C., Fu J., Qin R., Cao G.;
RT   "Draft Genome Sequence of Streptomyces tsukubaensis F601, a Producer of the
RT   immunosuppressant tacrolimus FK506.";
RL   Submitted (FEB-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}.
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:OON79597.1}.
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DR   EMBL; MVFC01000009; OON79597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4A9J3; -.
DR   STRING; 83656.B1H18_13500; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000190539; 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   CDD; cd03109; DTBS; 1.
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:UP000190539};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          210..317
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          366..683
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   691 AA;  73691 MW;  3BFA4813A7DAA88A CRC64;
     MTRSVYVTGI DRGDGRQVVE LGVMELLTRQ VDRVGVFRPL VHDGPDRLYE LLRARYRLSQ
     DPRSVYGMDY HEASTLQAEQ GTDELVSRLV DRFREVADAY EVVLVLGSDF AATQLPDELS
     LNARLANEFG ASVLAVVGGR DQPAESVRSE TRNAHRAYTQ LGCDVLAVVV NRVAPDDRDE
     IEDRLTAGMP VPCYVLPDDA ALSAPTVAQI THSLGGTVLL GDDSGLARDA LDFVFGGATL
     PNFLNALTPG CLVVTPGDRA DLVVGALAAH NASTPPIAGV LLTLGERPNT PVLALAQRLA
     PGTPVVSVPG NSFPTAGELF GLEGKLSAAN PRKAETALGL FERWVDTSGL LGLIQVSRSG
     RVTPMMFEHE LLEQARTDRR RVVLPEGSEE RVLRAAEVLL RRGVCDLTLL GREETIRKMA
     ADLGVDLADA QLIDPATSEL RQRFAEEYAE LRAHRGVSVE LAYDVVADVN YFGTLMVRAG
     LADGMVSGSV HSTAATIRPA FEIIKTKPDA ELVSSAFFMC LADKVLVYAD CAVNPDPDAA
     QLADIAVQSA ATAARFGVEP RIAMLSYSTG TSGSGADVDK VREATELVRA ARSELRIEGP
     IQYDAAVEPS VAATKMPESE VAGRASVLIF PDLNTGNNTY KAVQRSAGAV AVGPVLQGLR
     KPVNDLSRGA LVQDIVNTVA ITAIQAQVPA E
//
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