ID A0A5A7PSB7_STRAF Unreviewed; 299 AA. AC A0A5A7PSB7; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 13-SEP-2023, entry version 16. DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405}; DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405}; GN ORFNames=STAS_11835 {ECO:0000313|EMBL:GER35556.1}; OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga. OX NCBI_TaxID=4170 {ECO:0000313|EMBL:GER35556.1, ECO:0000313|Proteomes:UP000325081}; RN [1] {ECO:0000313|Proteomes:UP000325081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. UVA1 {ECO:0000313|Proteomes:UP000325081}; RX PubMed=31522940; DOI=10.1016/j.cub.2019.07.086; RA Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y.M., Honaas L., RA Yang Z., Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P., RA Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M.S., RA Koo N., Laohavisit A., Lee Y.H., Lumba S., McCourt P., Mortimer J.C., RA Mutuku J.M., Nomura T., Sasaki-Sekimoto Y., Seto Y., Wang Y., Wakatake T., RA Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R.I., RA Nelson D.C., Schulman A.H., Timko M.P., dePamphilis C.W., Choi D., RA Shirasu K.; RT "Genome Sequence of Striga asiatica Provides Insight into the Evolution of RT Plant Parasitism."; RL Curr. Biol. 29:3041-3052.e4(2019). 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:0000256|ARBA:ARBA00000774, CC ECO:0000256|RuleBase:RU003405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC {ECO:0000256|ARBA:ARBA00008824}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GER35556.1}. 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; BKCP01004973; GER35556.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5A7PSB7; -. DR Proteomes; UP000325081; Unassembled WGS sequence. 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; 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:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology; KW NAD {ECO:0000256|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU003405}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}; KW Reference proteome {ECO:0000313|Proteomes:UP000325081}; KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}. FT DOMAIN 4..123 FT /note="Lactate/malate dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 125..292 FT /note="Lactate/malate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 155 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 59 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 72 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 95..97 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 97 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 131 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 206 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" SQ SEQUENCE 299 AA; 31935 MW; 66C1E0A395DE5F68 CRC64; MFPLVSSLNL YDIADVKGVA ADLSHCNTPS TVQDFTGASE LSGCLKDANV VVIPAGVPRK PGMTRDDLFN INANIVKSLV EAVADTCPDS FVHIISNPVN STVPIAAEVL KRKGVYDPKR LFGVTTLDVV RANMFVAEKK GLKLIDVDVP VVGGHAGITI LPLLSKTRPL TSYSPEEVAE LTGRIQNAGT EVVEAKAGAG STTLSMAYAA ARFLESSLRA LDGDTDVYEF AYVESSVVPE LPFFASRVKI GKEGVEGFVK KDLEGLTEYE SKGLEELKPE LKASIEKGVD FVRKQAMAA //