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Database: UniProt
Entry: A0A161IHF6_9MICO
LinkDB: A0A161IHF6_9MICO
Original site: A0A161IHF6_9MICO 
ID   A0A161IHF6_9MICO        Unreviewed;       704 AA.
AC   A0A161IHF6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   Name=pta {ECO:0000313|EMBL:ANC31104.1};
GN   ORFNames=I598_1551 {ECO:0000313|EMBL:ANC31104.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC31104.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC31104.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC31104.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-2016) 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; CP014209; ANC31104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161IHF6; -.
DR   STRING; 1300344.I598_1551; -.
DR   KEGG; ido:I598_1551; -.
DR   PATRIC; fig|1300344.3.peg.1558; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000076794; Chromosome.
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; 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:UP000076794};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          218..330
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          375..692
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   704 AA;  74519 MW;  85462834A0C21985 CRC64;
     MSTRSIYIAS PEGDTGKSTV ALGVLELLVR QVQRVGVFRA VSRVPDRPSA AGGQVRDHVL
     ETMLAHDGVD LTYAETVGVT YDEVHADPEA ALARIVDRYH AVAAKCDAVV VLGTDYTDVS
     GATELAFNAR VAANLDSPVL LVVSGRDRDL EDVTTLARLS LAELRANHAQ PIAVVVNRAE
     GAVADADRAT RARLSGEDLP TWVIPEEPFL TAPTIAQLTE AVDGTLLLGD KDLMAREALD
     VIVGAMTFEN LLGRLADGTV VITPGDRTDV LLGMLAVQAA PRFPSLAGVI LTGGYRPTGR
     SGQLAAALQP NVPIVLTERD TYEVARAASR TRGAMTATAQ RKHDVARAMF EQRVDGDELL
     ARLAVERTPV VTPLMFEHEL MERARADRRT VVLPEGDDDR ILRAASTVLA RGIADLVILG
     DETVIRARAT ALGLDVSAAR VLSPHDAEHV ERFAAEYARL RAHKGMTVER AREIVTDVSY
     FGTMMVHLGL ADGMVSGAAH TTAHTIRPSF EIIKTRPGVS VVSSVFLMCL PDRVLAYGDC
     AVNPDPTAEQ LADIAASSAQ TAAQFGVEPR VAMLSYSTGT SGSGADVDKV RTATELVRER
     HPELNVEGPI QYDAAVDASV AASKLPESSV AGRASVFVFP DLNTGNNTYK AVQRSAGAVA
     IGPVLQGLNK PVNDLSRGAL VADIVNTVAI TAIQAQGATN GESA
//
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