ID A0A095AMW7_LEUME Unreviewed; 542 AA. AC A0A095AMW7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 11-NOV-2015, entry version 6. DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KGB50834.1}; DE EC=1.1.1.38 {ECO:0000313|EMBL:KGB50834.1}; GN ORFNames=LH61_04880 {ECO:0000313|EMBL:KGB50834.1}; OS Leuconostoc mesenteroides P45. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=1429888 {ECO:0000313|EMBL:KGB50834.1}; RN [1] {ECO:0000313|EMBL:KGB50834.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P45 {ECO:0000313|EMBL:KGB50834.1}; RA Riveros-Mckay F., Campos I., Giles-Gomez M., Bolivar F., Escalante A.; RT "Genome sequence of Leuconostoc mesenteroides P45 isolated from RT pulque, a traditional Mexican alcoholic fermented beverage."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3}; CC Note=Divalent metal cations. Prefers magnesium or manganese. CC {ECO:0000256|PIRSR:PIRSR000106-3}; CC -!- SIMILARITY: Belongs to the malic enzymes family. CC {ECO:0000256|RuleBase:RU003427}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGB50834.1}. 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; JRGZ01000002; KGB50834.1; -; Genomic_DNA. DR RefSeq; WP_036091081.1; NZ_JRGZ01000002.1. DR EnsemblBacteria; KGB50834; KGB50834; LH61_04880. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10380; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR PRINTS; PR00072; MALOXRDTASE. DR SMART; SM00919; Malic_M; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00331; MALIC_ENZYMES; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3, KW ECO:0000256|RuleBase:RU003427}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003427, KW ECO:0000313|EMBL:KGB50834.1}. FT ACT_SITE 92 92 Proton donor. {ECO:0000256|PIRSR: FT PIRSR000106-1}. FT ACT_SITE 165 165 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000106-1}. FT METAL 236 236 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. FT METAL 237 237 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. FT METAL 260 260 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. SQ SEQUENCE 542 AA; 59205 MW; F2B6A27F7E2AA86E CRC64; MNTTGYDILR NPFLNKGTAF SEAERQQLGL TGTLPSQIQT IEEQAEQAYK QFQAKSPLLE KRIFLMNLFN ENVTLFYHLM DQHVSEFMPI VYDPVVAESI EQYNEIYTNP QNAAFLSVDR PEDVENALKN AAAGRDIKLV VVTDAEGILG MGDWGVNGVD IAVGKLMVYT AAAGIDPATV LPVSIDAGTN NKELLHNPLY LGNKHERIAG EQYLEFIDKF VTAEQNLFPE SLLHWEDFGR SNAQVILDKY KESIATFNDD IQGTGMIVLA GIFGALNISK QKLVDQKFVT FGAGTAGMGI VNQIFSELKQ AGLSDDEARN HFYLVDKQGL LFDDTEGLTA AQKPFTRSRK EFVNPEQLIN LETIVKELHP TVLIGTSTQP GTFTETIVKS MAENTERPII FPLSNPTKLA EATAEDLIKW TGGKALVATG IPAADVDYKG VTYKIGQGNN ALIYPGLGFG LVASTAKLLT QETISAAIHA LGGLVDTDEP GAAVLPPVSN LTDFSQKIAE ITAQSVVNQG LNREKIVDPK QAVQDAKWSA EY //