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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //