ID   MAOX_MYCTO              Reviewed;         548 AA.
AC   P9WK24; L0T9I1; P71880;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Putative malate oxidoreductase [NAD];
DE            EC=1.1.1.38;
DE   AltName: Full=Malic enzyme;
GN   Name=mez; OrderedLocusNames=MT2394;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46686.1; -; Genomic_DNA.
DR   PIR; E70705; E70705.
DR   RefSeq; WP_003899273.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK24; -.
DR   SMR; P9WK24; -.
DR   EnsemblBacteria; AAK46686; AAK46686; MT2394.
DR   KEGG; mtc:MT2394; -.
DR   PATRIC; fig|83331.31.peg.2582; -.
DR   HOGENOM; CLU_011405_5_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
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   Gene3D; 3.40.50.10380; -; 1.
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; 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   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..548
FT                   /note="Putative malate oxidoreductase [NAD]"
FT                   /id="PRO_0000427728"
FT   ACT_SITE        96
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         240
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         241
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         264
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         297..300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         410
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
FT   BINDING         455
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40927"
SQ   SEQUENCE   548 AA;  59423 MW;  407248FE6BDFC875 CRC64;
     MSDARVPRIP AALSAPSLNR GVGFTHAQRR RLGLTGRLPS AVLTLDQQAE RVWHQLQSLA
     TELGRNLLLE QLHYRHEVLY FKVLADHLPE LMPVVYTPTV GEAIQRFSDE YRGQRGLFLS
     IDEPDEIEEA FNTLGLGPED VDLIVCTDAE AILGIGDWGV GGIQIAVGKL ALYTAGGGVD
     PRRCLAVSLD VGTDNEQLLA DPFYLGNRHA RRRGREYDEF VSRYIETAQR LFPRAILHFE
     DFGPANARKI LDTYGTDYCV FNDDMQGTGA VVLAAVYSGL KVTGIPLRDQ TIVVFGAGTA
     GMGIADQIRD AMVADGATLE QAVSQIWPID RPGLLFDDMD DLRDFQVPYA KNRHQLGVAV
     GDRVGLSDAI KIASPTILLG CSTVYGAFTK EVVEAMTASC KHPMIFPLSN PTSRMEAIPA
     DVLAWSNGRA LLATGSPVAP VEFDETTYVI GQANNVLAFP GIGLGVIVAG ARLITRRMLH
     AAAKAIAHQA NPTNPGDSLL PDVQNLRAIS TTVAEAVYRA AVQDGVASRT HDDVRQAIVD
     TMWLPAYD