ID   MAOM_AMAHP              Reviewed;         623 AA.
AC   P37224;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=NAD-dependent malic enzyme 65 kDa isoform, mitochondrial;
DE            Short=NAD-ME;
DE            EC=1.1.1.39;
DE   Flags: Precursor;
OS   Amaranthus hypochondriacus (Prince-of-Wales feather) (Amaranthus hybridus
OS   var. hypochondriacus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Amaranthus.
OX   NCBI_TaxID=28502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8300616; DOI=10.1016/s0021-9258(17)42017-5;
RA   Long J.J., Wang J.-L., Berry J.O.;
RT   "Cloning and analysis of the C4 photosynthetic NAD-dependent malic enzyme
RT   of amaranth mitochondria.";
RL   J. Biol. Chem. 269:2827-2833(1994).
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=1.1.1.39;
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   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- SUBUNIT: Heterodimer of two related subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; U01162; AAA19014.1; -; mRNA.
DR   PIR; A49983; A49983.
DR   AlphaFoldDB; P37224; -.
DR   SMR; P37224; -.
DR   UniPathway; UPA00322; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0006108; P:malate metabolic process; IEA:UniProt.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; Mitochondrion; NAD;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT   CHAIN           32..623
FT                   /note="NAD-dependent malic enzyme 65 kDa isoform,
FT                   mitochondrial"
FT                   /id="PRO_0000018542"
FT   ACT_SITE        143
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        214
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            309
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   623 AA;  69688 MW;  0B0917B8506FFE48 CRC64;
     MLVLCSRSRL TSSLIRRLKD QIANVSNHRS FATSEGHRLA IVNKRSLDIL QDPWFNKGTA
     FSMTERDRLD LRGLLPPNVM TTEQQIERFT ADLRVLELTT KDGPSDTYDL AKWRILNRLH
     DRNETMFFKV LIENIEEYAP IVSTPTVGLV CQKFSGLYRR PRGMYFSSDD RGEMMSMVYN
     WPAEQVDMIV VTDGSRILGL GDLGVHGIGV AIGKLDLYVA AAGINPQRVL PVMIDVGTNN
     EDLLKNPLYL GLQKKRLDGE EYLAVMDEFM EAVFTRWPNV IVQFEDIQNK WALTLLQRYR
     HKYRTFNVDV QGTSGVAIAG LLGAVRAQGR PMIDFPKQKI VVAGAGSSGV GVLNAARKTM
     ARMLGNDESA FDRARSQFWV VDDKGLITEK RANLDPEVQP FAWKENEISL QGLNEGAKLV
     EVVRQVKPDV LLGLSAYGGL FSKEVLEALK DSTSTRPAIF AMSNPTKNAE CTPEEAFSIV
     GDHVVYASGS PFKDVDLGNG KIGHVNQGNN MYLFPGIGLG VLLSGSRIIS DSMFQAAAER
     LAGYMTDEEV INGVIYPSIS RIRDITKEVA AAVIKEAVEE DLAEGYRDMD ARELQKLNEE
     QILEYIEKNM WNPEYPTLVY KKR