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Database: UniProt
Entry: A0A495IAV3_9MICO
LinkDB: A0A495IAV3_9MICO
Original site: A0A495IAV3_9MICO 
ID   A0A495IAV3_9MICO        Unreviewed;       719 AA.
AC   A0A495IAV3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
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=C8E83_0220 {ECO:0000313|EMBL:RKR73133.1};
OS   Frondihabitans australicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=386892 {ECO:0000313|EMBL:RKR73133.1, ECO:0000313|Proteomes:UP000280008};
RN   [1] {ECO:0000313|EMBL:RKR73133.1, ECO:0000313|Proteomes:UP000280008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17894 {ECO:0000313|EMBL:RKR73133.1,
RC   ECO:0000313|Proteomes:UP000280008};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-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:RKR73133.1}.
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DR   EMBL; RBKS01000001; RKR73133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495IAV3; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000280008; 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:UP000280008};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          221..333
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          378..695
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
FT   REGION          699..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  75736 MW;  734996A997DBFDAE CRC64;
     MSTRIFITSA EGHTGKSTIA LGVLDTLSHE LGRVGVFRPV ARSVSEPDYV LELLLAHDSV
     DLPYEQCVGV TYDEVHADPD AALATIVARF AAIERQCDAV VIVGSDYTDV GSPTELSFNA
     RIAANLGAPV LLVLGGRTSD GSHARTGADM RQVADVTTAE LRSEHASLLA VIANRADPEH
     LDEIVAGVRE SVAASAEGAE PVPVWALPED RVLVAPTLRS VMDATGARLV RGDEALLERE
     AVGVVVAAMS MENVLPRLIE GSVVVVPGDR TDVLVATVLA HASETFPSLA GIILNGGFDL
     APQVVRLLGG LDSSLPILWN ELGTYDTALR ITETRGRLAA DSTRKYDLAL SLFETHVDGA
     ALLALLEVAP SQVVTPLMFE YQLLDRARSI RKHIVLPEGD DDRILRAASS LLQRGVAKLT
     LLGNESAVRA RGAELGLDLA DADVLDPNDP ALQRQFAAEY ATLRAHKGTT VDMAMDTVTD
     VSYFGTMMVK MGLADGMVSG AKHTTAHTIR PAFEVIKTLP DVSVVSSVFL MALADRVLVY
     GDCAVIPDPT AEQLADIAIS SAQTAQQFGI EPRIAMLSYS TGDSGSGADV DKVRQATALV
     RERRPDLLVE GPIQYDAAAD PTVAATKMPD SQVAGRATVF IFPDLNTGNN TYKAVQRSAG
     AVAIGPILQG LRKPINDLSR GALVSDIVNT VAITAIQAGT QEPGSPAEAP APTPEGASS
//
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