ID MDH2_RHOFD Reviewed; 334 AA. AC Q21VT3; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Malate dehydrogenase 2; DE EC=1.1.1.37; GN Name=mdh2; OrderedLocusNames=Rfer_2403; OS Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Rhodoferax. OX NCBI_TaxID=338969; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM RT 15236."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to CC oxaloacetate (By similarity). CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000267; ABD70120.1; -; Genomic_DNA. DR RefSeq; YP_523651.1; -. DR GeneID; 3962073; -. DR GenomeReviews; CP000267_GR; Rfer_2403. DR KEGG; rfr:Rfer_2403; -. DR NMPDR; fig|338969.3.peg.2508; -. DR HOGENOM; Q21VT3; -. DR OMA; Q21VT3; VIGRHAN. DR BioCyc; RFER338969:RFER_2403-MON; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP. DR HAMAP; MF_01517; -; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR001236; Lactate/malate_DH. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR001252; Malate_DH_AS. DR InterPro; IPR010945; Malate_DH_SF1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR23382; MDH_SF1; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR ProDom; PD003052; Mal_dehydrog; 1. DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1. DR PROSITE; PS00068; MDH; FALSE_NEG. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1 334 Malate dehydrogenase 2. FT /FTId=PRO_0000294404. FT NP_BIND 12 18 NAD (By similarity). FT NP_BIND 130 132 NAD (By similarity). FT ACT_SITE 191 191 Proton acceptor (By similarity). FT BINDING 93 93 Substrate (By similarity). FT BINDING 99 99 Substrate (By similarity). FT BINDING 106 106 NAD (By similarity). FT BINDING 113 113 NAD (By similarity). FT BINDING 132 132 Substrate (By similarity). FT BINDING 166 166 Substrate (By similarity). SQ SEQUENCE 334 AA; 35806 MW; ED1746FB0D5A4D6C CRC64; MNQAPVRVTV TGAAGRVAYA LLFRIASGDM LGADQPVQLV LFDLPHAMKA MQGVVMELED CAFPLLTEII ATDDPVLAFS DTQIALLVSA RPRAVGAERL EVLADNAKIF AAQGAVIGRH ANPDCKVLVV GNPCNTNACV AMKAAQKFSR IPARNFAALL RLDHNRALAQ LALKTGRPVG GVKRLAVWGN HSPTVYADDR FTTIDGDSVP AIIDNIAWHH DTLVRTVDKR GEAILAARGL YAEASAASAA IDQMRDWWLG TRGEWTTMGV VSDGAYGVPA GLVFGFPVIT DCRDYRIVPG LAVDAFARGM IDVNVRELTA ELEIVKPLLP ELFG //