ID MDH_PSEMZ Reviewed; 23 AA. AC P85920; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 1. DT 03-AUG-2022, entry version 19. DE RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:P61889}; DE EC=1.1.1.37; DE Flags: Fragments; OS Pseudotsuga menziesii (Douglas-fir) (Abies menziesii). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; OC Pseudotsuga. OX NCBI_TaxID=3357; RN [1] {ECO:0000305} RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004; RA Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.; RT "A proteomics approach to identify proteins differentially expressed in RT Douglas-fir seedlings infected by Phellinus sulphurascens."; RL J. Proteomics 71:425-438(2008). 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:0000250|UniProtKB:P61889, ECO:0000255|PROSITE- CC ProRule:PRU10004}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P61889}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC {ECO:0000255}. 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 AlphaFoldDB; P85920; -. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN <1..>23 FT /note="Malate dehydrogenase" FT /id="PRO_0000397957" FT BINDING 7 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 23 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889, FT ECO:0000255|PROSITE-ProRule:PRU10004" FT NON_CONS 12..13 FT /evidence="ECO:0000303|PubMed:18602030" FT NON_TER 1 FT /evidence="ECO:0000303|PubMed:18602030" FT NON_TER 23 FT /evidence="ECO:0000303|PubMed:18602030" SQ SEQUENCE 23 AA; 2520 MW; 020A52B09ADE4B08 CRC64; DDLFNINAGI VKLFGVTTLD VVR //