ID MDH_XYLFA Reviewed; 328 AA. AC Q9PE17; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 2. DT 27-MAR-2024, entry version 124. DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517}; DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517}; GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=XF_1211; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000255|HAMAP-Rule:MF_01517}. 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|HAMAP-Rule:MF_01517}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC {ECO:0000255|HAMAP-Rule:MF_01517}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF84021.1; Type=Erroneous initiation; Evidence={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; AE003849; AAF84021.1; ALT_INIT; Genomic_DNA. DR PIR; G82708; G82708. DR RefSeq; WP_031336891.1; NC_002488.3. DR AlphaFoldDB; Q9PE17; -. DR SMR; Q9PE17; -. DR STRING; 160492.XF_1211; -. DR KEGG; xfa:XF_1211; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_040727_2_0_6; -. DR Proteomes; UP000000812; Chromosome. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR CDD; cd01338; MDH_choloroplast_like; 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 HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01759; MalateDH-SF1; 1. DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1. DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 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. PE 3: Inferred from homology; KW NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1..328 FT /note="Malate dehydrogenase" FT /id="PRO_0000113406" FT ACT_SITE 189 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 11..17 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 94 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 100 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 107 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 114 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 131..133 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 133 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" SQ SEQUENCE 328 AA; 35488 MW; 5758E3764AB37C9E CRC64; MKSLVRVAVT GAAGQIGYSL LFRIAAGEMF GKDRPVILQM LELPDEKAQA ALKGVMMELE DCAFPLLAGM VGTDNPDIAF KDADVALLVG SRPRGPGMER KDLLMENAKI FTAQGAALNK VARRDVKVLV VGNPANTNAY IAMKSAPDLN PKHFTAMLRL DHNRALSQLS TKLSKPVANI EKLIVWGNHS PTMYPDYRFA TADGTPIIEA INDQAWNANS FIPTVSKRGA AIIEVRGLSS AASAANAAID HMRDWLLGSN GKWITMGVPS DGSYGIPEGM IFGFPVTTTN GEYSIVKDLP IDTFSKTYID KTLAELEEER ASIAHLLR //