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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//