ID   MAOX_GEOSE              Reviewed;         478 AA.
AC   P16468;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=NAD-dependent malic enzyme;
DE            Short=NAD-ME;
DE            EC=1.1.1.38;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=2644282; DOI=10.1016/s0021-9258(18)94051-2;
RA   Kobayashi K., Doi S., Negoro S., Urabe I., Okada H.;
RT   "Structure and properties of malic enzyme from Bacillus
RT   stearothermophilus.";
RL   J. Biol. Chem. 264:3200-3205(1989).
CC   -!- FUNCTION: In addition to the NAD-dependent oxidative decarboxylation of
CC       L-malate, the enzyme catalyzes the decarboxylation of oxaloacetate.
CC       {ECO:0000269|PubMed:2644282}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC         Evidence={ECO:0000269|PubMed:2644282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=1.1.1.38;
CC         Evidence={ECO:0000269|PubMed:2644282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:2644282};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:2644282};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000269|PubMed:2644282};
CC   -!- ACTIVITY REGULATION: The activity is enhanced 5-7 times by ammonium and
CC       potassium. {ECO:0000269|PubMed:2644282}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2644282}.
CC   -!- MISCELLANEOUS: This enzyme has a higher affinity for NAD than for NADP.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; M19485; AAA22585.1; -; Genomic_DNA.
DR   PIR; A33307; DEBSXS.
DR   AlphaFoldDB; P16468; -.
DR   SMR; P16468; -.
DR   PRIDE; P16468; -.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR015884; Malic_enzyme_CS.
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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..478
FT                   /note="NAD-dependent malic enzyme"
FT                   /id="PRO_0000160207"
FT   DOMAIN          12..86
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         211
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         212
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         237
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         270..273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         363
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         393
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
SQ   SEQUENCE   478 AA;  51537 MW;  8CE6629A2E6AFE74 CRC64;
     MALPGGAAMN ITIRLQFEKD IVSFSDIAAA IGKAGGDIVG IDVISSSKVH TVRDITVSAL
     DTKQCDLIIE ALKKIRGVKI VNVSDRTFLM HIGGKIETNS KIPVKTRDDL SRVYTPGVAR
     VCTAIAEDPR KAYSLTIKRN TVAVVSDGTA VLGLGDIGPY AAMPVMEGKA MLFKEFAGVD
     AFPICLDTKD TEEIIQIVKA IAPAFGGINL EDISAPRCFE IEKRLKEELD IPVFHDDQHG
     TAVVLLAGLL NALKIVDKKL EDIKVVLTGI GAAGIACTKI LLAAGVRNII GVDRHGAIHR
     DETYENPYWQ EYAQLTNPDN LKGSLSDVIA GADVFIGVSA PGILKVEDVK KMARDPIVFA
     MANPIPEIDP ELAEPYVRVM ATGRSDYPNQ INNVLCFPGI FRGALDCRAR EINEEMKLAA
     AKAIASVVTE DELNETYIIP SVFNSKVVER VRQAVVEAAY RTGVARKDNI PVGGYTGQ