ID MDHG1_BRANA Reviewed; 358 AA.
AC Q43743; Q9T0L8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 13-SEP-2023, entry version 109.
DE RecName: Full=Malate dehydrogenase 1, glyoxysomal;
DE EC=1.1.1.37;
DE Flags: Precursor;
GN Name=MDH1;
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.
RC STRAIN=cv. Andor; TISSUE=Leaf;
RA Witt U., Rehberg S., Abel W.O.;
RT "A full-length cDNA coding for glyoxysomal malate dehydrogenase from
RT Brassica napus L.";
RL (er) Plant Gene Register PGR95-124(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Imhoff U., Voetz M., Wingender R., Schnabl H., Wolf N.;
RT "Two genes encoding microbody malate dehydrogenase from Brassica napus.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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: Glyoxysome.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
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DR EMBL; X92512; CAA63268.1; -; mRNA.
DR EMBL; AJ242712; CAB43994.1; -; Genomic_DNA.
DR PIR; T08015; T08015.
DR AlphaFoldDB; Q43743; -.
DR SMR; Q43743; -.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11540:SF52; MALATE DEHYDROGENASE 2, PEROXISOMAL; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00068; MDH; 1.
PE 2: Evidence at transcript level;
KW Glyoxylate bypass; Glyoxysome; NAD; Oxidoreductase; Peroxisome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..38
FT /note="Glyoxysome"
FT /evidence="ECO:0000255"
FT CHAIN 39..358
FT /note="Malate dehydrogenase 1, glyoxysomal"
FT /id="PRO_0000018636"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 53..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 162..164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 1..8
FT /note="MEFRGDAY -> MPH (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="M -> V (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="V -> G (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 151..152
FT /note="AK -> GG (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="L -> S (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="K -> T (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="R -> K (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="N -> H (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="E -> D (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="K -> H (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> V (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..279
FT /note="ATLSMAYAAAK -> SPLPIILAAP (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..311
FT /note="ELAFFA -> DYFLC (in Ref. 1; CAA63268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 37732 MW; DC94CBC76ACEEE4A CRC64;
MEFRGDAYKR IAMISAHLQP SFTPQMEAKN SVMGLESCRA KGGNPGFKVA ILGAAGGIGQ
SLSLLMKMNP LVSLLHLYDV VNAPGVTADV SHMDTGAVVR GFLGAKQLED ALTGMDLVII
PAGVPRKPGM TRDDLFKINA GIVRTLCEGV AKCCPNAIVN LISNPVNSTV AIAAEVFKKA
GTYDPKKLLG VTTLDVARAN TFVAEVLGLD PREVDVPVVG GHAGVTILPL LSQVKPPSSF
TPSEIEYLTN RIQNGGTEVV EAKAGAGSAT LSMAYAAAKF ADACLRGLRG DANVIECSFV
ASQVTELAFF ATKVRLGRTG AEEVFQLGPL NEYERVGLEK AKEELAGSIQ KGVDFIRK
//
