ID   A0A1G0PGH9_9BACT        Unreviewed;       653 AA.
AC   A0A1G0PGH9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00012707};
DE            EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707};
DE   Flags: Fragment;
GN   ORFNames=A2068_00495 {ECO:0000313|EMBL:OGU34844.1};
OS   Ignavibacteria bacterium GWB2_35_6b.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798424 {ECO:0000313|EMBL:OGU34844.1, ECO:0000313|Proteomes:UP000178800};
RN   [1] {ECO:0000313|EMBL:OGU34844.1, ECO:0000313|Proteomes:UP000178800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OGU34844.1}.
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DR   EMBL; MGZW01000156; OGU34844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0PGH9; -.
DR   Proteomes; UP000178800; Unassembled WGS sequence.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR004614; P_AcTrfase.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
DR   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR   PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:OGU34844.1}.
FT   DOMAIN          1..52
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          64..300
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OGU34844.1"
SQ   SEQUENCE   653 AA;  72423 MW;  EFA30D4A1AD4CF12 CRC64;
     RFADIDVFDI ELNTKDPKEV IRTVQLLEPT FGGINLEDIK APECFEIEEE LKRTMNIPVF
     HDDQHGTAII SCAALINAAE VIGKKLSNMR MVVSGAGAAA ISCCNLYMMA GLKRENIFMF
     DSKGLIHKDR PDLNKYKIPF AHENKYASLE DAMKGADVFV GLSKADVVTG EMVKSMAKDP
     IVFAMANPNP EIKYDVAKAA REDVVMATGR SDYPNQVNNV LGFPFIFRGA LDVRAKAINE
     EMKMAAVKAL SNLAKEKVPE VVKNAYGGTD FSFGREYIIP KPFDPRVLWN VAPAVARAAI
     ETGVARVQIT DWKAYEEELK ERLGYSEQVI RVMVRKAQDN PKKIVYPEGE EEKIIRAANS
     VVREKIANPI LLGNKEAIIA KINELGYNEK DFIIIDPLTS DKFDEYVKEF YSVRQRKGVT
     LRESKELMKQ RNYFGSMMVR KGDADSLIGG LNSHYPQTIR PALQVLGIKK GANVVSGLYI
     VIIKRKVYFF ADTTVNINPT AEELAEIAIS AADTVKEFDI EPKVAMLSFS NFGSSKHPES
     DKVAKATAIV KEKRPDIICD GEMQADTAVV PSIIEKEFPF SNLKGGANIL VFPNLSAGNI
     AYKLFERLTS ATVIGPILMG LEKPIHVMQR GASVEDIIKM TAIAVVEARH NNK
//