MDHM_BRANA
ID MDHM_BRANA Reviewed; 341 AA.
AC Q43744;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Malate dehydrogenase, mitochondrial;
DE EC=1.1.1.37;
DE Flags: Precursor;
GN Name=MDH;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Andor; TISSUE=Leaf;
RA Witt U., Gruneberg-Seiler M., Abel W.O.;
RT "A full-length cDNA coding for mitochondrial malate dehydrogenase from
RT Brassica napus L.";
RL (er) Plant Gene Register PGR95-068(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
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DR EMBL; X89451; CAA61621.1; -; mRNA.
DR PIR; S57958; S57958.
DR RefSeq; NP_001302862.1; NM_001315933.1.
DR AlphaFoldDB; Q43744; -.
DR SMR; Q43744; -.
DR PRIDE; Q43744; -.
DR GeneID; 106360426; -.
DR KEGG; bna:106360426; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; NAD; Oxidoreductase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..341
FT /note="Malate dehydrogenase, mitochondrial"
FT /id="PRO_0000018623"
FT BINDING 36..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 145..147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 35711 MW; F27AC7D2680601C6 CRC64;
MFRSALVRSS ASAKQSLLRR SFSSGSVPER KVAILGAAGG IGQPLALLMK LNPLVSSLSL
YDIANTPGVA ADVGHINTRS QVVGYMGDDN LAKALEGADL VIIPAGVPRK PGMTRDDLFN
INAGIVKNLW SAIAKYCPHA LVNMISNPVN STVPIAAEIF KKAGMYDEKK LFGVTTLDVV
RVKTSYAGKA NVPVAEVNVP AIVGHAGVTI LPLFSQATPQ AILSGDALTV TTKRTQDGGT
EVEEAKAGKG SATLSMAYAG ALFADACLKG LNGVPDVVEC SYVQSTITEL PFFASKVRLG
KNGVEEVLDL GPLSDFEKEG LEALRPGIKS TIEKGVKFAN Q
