MDHM_EUCGU
ID MDHM_EUCGU Reviewed; 347 AA.
AC P46487;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Malate dehydrogenase, mitochondrial;
DE EC=1.1.1.37;
DE Flags: Precursor;
GN Name=MDH;
OS Eucalyptus gunnii (Cider gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=3933;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7770532; DOI=10.1104/pp.107.4.1455;
RA Poeydomenge O., Boudet A.M., Grima-Pettenati J., Marolda M.;
RT "Nucleotide sequence of a cDNA encoding mitochondrial malate dehydrogenase
RT from Eucalyptus.";
RL Plant Physiol. 107:1455-1456(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 Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
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; X78800; CAA55383.1; -; mRNA.
DR PIR; S44167; S44167.
DR AlphaFoldDB; P46487; -.
DR SMR; P46487; -.
DR PRIDE; P46487; -.
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:0006108; P:malate 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; IPR001252; Malate_DH_AS.
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.
DR PROSITE; PS00068; MDH; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; NAD; Oxidoreductase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..347
FT /note="Malate dehydrogenase, mitochondrial"
FT /id="PRO_0000018626"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 41..47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 36462 MW; 450F8254CCC84789 CRC64;
MRASMLRLIR SRSSSAAPRP HLLRRAYGSE SVPERKVAVL GAAGGIGQPL ALLMKLNPLV
SQLALYDIAG TPGVAADVGH INTRSEVAGY VGEEQLGQAL EGSDVVIIPA GVPRKPGMTR
DDLFNINAGI VKSLCTAIAK YCPNAVVNMI SNPVNSTVPI AAEIFKKAGT YNEKKLLGVT
TLDVVRAKTF YAGKAKVPVE EVNVPVVGGH AGITILPLFS QAVPKANLAD EDIKALTKRT
QDGGTEVVEA KAGKGSATLS MAYAGALFAD ACLKGLNGVP DVVECSFVQS SIITELPFFA
SKVKLGKNGV EEVLELGPMS DYEKQGLEIL IPELKASIEK GIKFANQ
