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Database: UniProt
Entry: I3QGD9_9FLAO
LinkDB: I3QGD9_9FLAO
Original site: I3QGD9_9FLAO 
ID   I3QGD9_9FLAO            Unreviewed;       757 AA.
AC   I3QGD9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Bifunctional malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP+)/phosphate acetyltransferase {ECO:0000313|EMBL:AFJ90674.1};
GN   Name=maeB {ECO:0000313|EMBL:AFJ90674.1};
GN   ORFNames=BGIGA_224 {ECO:0000313|EMBL:AFJ90674.1};
OS   Blattabacterium sp. (Blaberus giganteus).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=1186051 {ECO:0000313|EMBL:AFJ90674.1, ECO:0000313|Proteomes:UP000006466};
RN   [1] {ECO:0000313|EMBL:AFJ90674.1, ECO:0000313|Proteomes:UP000006466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGIGA {ECO:0000313|EMBL:AFJ90674.1,
RC   ECO:0000313|Proteomes:UP000006466};
RX   PubMed=22843586; DOI=10.1128/JB.00789-12;
RA   Huang C.Y., Sabree Z.L., Moran N.A.;
RT   "Genome Sequence of Blattabacterium sp. Strain BGIGA, Endosymbiont of the
RT   Blaberus giganteus Cockroach.";
RL   J. Bacteriol. 194:4450-4451(2012).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC       family. {ECO:0000256|ARBA:ARBA00007686}.
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DR   EMBL; CP003535; AFJ90674.1; -; Genomic_DNA.
DR   RefSeq; WP_014726545.1; NC_017924.1.
DR   AlphaFoldDB; I3QGD9; -.
DR   STRING; 1186051.BGIGA_224; -.
DR   KEGG; bbg:BGIGA_224; -.
DR   PATRIC; fig|1186051.3.peg.223; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_012366_0_0_10; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000006466; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; 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; IPR012188; ME_PTA.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
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   PIRSF; PIRSF036684; ME_PTA; 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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036684-2};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW   Transferase {ECO:0000313|EMBL:AFJ90674.1}.
FT   DOMAIN          21..154
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          166..403
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        97
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         79..86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         139
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         140
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         165
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         290
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   757 AA;  84578 MW;  A67EEF0B812745DC CRC64;
     MRKNISNFRE ESLNYHSQFP SGKIQITPTK KYSSQRDLSL AYSPGVAEPC KEIARSSIEV
     YKYTSKGNLV AVITNGSAVL GLGDIGALAS KPVMEGKALL FKIFSGIDVF DIEIDASDPE
     KFIETVKAIA PTFGGINLED IKAPEAFEIE RRLKKELNIP VMHDDQHGTA IISGAALLNA
     ITYVNKKIHE IKMVVNGAGA AAISCARTYK QLGVKPENIL MFDSKGLLHV SRKDLNKEKR
     EFSVNIDPIK KLDQAINNTD VFIGLSIGGI LTPNMLKSMA KNPIVFAMAN PDPEIDYNLA
     IKVRPDVIMA TGRSDYPNQV NNVLGFPYIF RGALDVHANV INDEMKLAAV YAIASLAKEP
     VPEQVNIVYN KKNISFGKEY IIPKPFDNRL ITRVAPAVAK AAMDSGVAKN PILDWKIYQE
     KLLDRMGYES KMLRMIQNRA RTNPKKIVFC NGEEYDILKS VQILHEEGII SIPIVLGNED
     RIKRLIHENN LNIELEIVDP EKNIKEVEEF SKILWKRRNR KGLTLYDSKI RMRTNDHFGA
     MMVDQGKADA VITGYSRSFS LSLRPMLEVI GKDDFVHKTA GMMILLTKRG PLFLADTAVI
     PDPTTEELAR IALMASHVVK SFDIEPRIAM LSFQNFSSNS KTSSKVSKTV AFLHKKYPNL
     IVDGEVQPDF ALNEFLLSRK FPFSKLVKKR ANIFIFPNLE SGNLTYKFIR GLGDVQTIGP
     VMLGMRKPAH VMQMQSSIEE IVHLATLAVI DAQIRKN
//
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