ID MAO1_ECOLU Reviewed; 565 AA. AC B7N4P2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 07-APR-2021, entry version 68. DE RecName: Full=NAD-dependent malic enzyme {ECO:0000255|HAMAP-Rule:MF_01619}; DE Short=NAD-ME {ECO:0000255|HAMAP-Rule:MF_01619}; DE EC=1.1.1.38 {ECO:0000255|HAMAP-Rule:MF_01619}; GN Name=maeA {ECO:0000255|HAMAP-Rule:MF_01619}; OrderedLocusNames=ECUMN_1734; OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMN026 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate; CC Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01619}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, CC ChEBI:CHEBI:16526; EC=1.1.1.38; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01619}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01619}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01619}; CC Note=Divalent metal cations. Prefers magnesium or manganese. CC {ECO:0000255|HAMAP-Rule:MF_01619}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01619}. CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000255|HAMAP- CC Rule:MF_01619}. 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; CU928163; CAR12936.1; -; Genomic_DNA. DR RefSeq; WP_000433464.1; NC_011751.1. DR RefSeq; YP_002412470.1; NC_011751.1. DR SMR; B7N4P2; -. DR EnsemblBacteria; CAR12936; CAR12936; ECUMN_1734. DR GeneID; 58462499; -. DR KEGG; eum:ECUMN_1734; -. DR PATRIC; fig|585056.7.peg.1921; -. DR HOGENOM; CLU_011405_5_2_6; -. DR OMA; WIREQMW; -. DR Proteomes; UP000007097; Chromosome. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-UniRule. 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-UniRule. DR Gene3D; 3.40.50.10380; -; 1. DR HAMAP; MF_01619; NAD_malic_enz; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR037062; Malic_N_dom_sf. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR023667; NAD_malic_enz_proteobac. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR PRINTS; PR00072; MALOXRDTASE. DR SMART; SM01274; malic; 1. 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; NAD; Oxidoreductase. FT CHAIN 1..565 FT /note="NAD-dependent malic enzyme" FT /id="PRO_1000185996" FT ACT_SITE 104 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT ACT_SITE 175 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT METAL 246 FT /note="Divalent metal cation" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT METAL 247 FT /note="Divalent metal cation" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT METAL 270 FT /note="Divalent metal cation" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT BINDING 157 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT BINDING 270 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT BINDING 418 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" FT SITE 270 FT /note="Important for activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619" SQ SEQUENCE 565 AA; 63163 MW; FFD2C913F7028F3A CRC64; MEPKTKKQRS LYIPYAGPVL LEFPLLNKGS AFSMEERRNF NLLGLLPEVV ETIEEQAERA WIQYQGFKTE IDKHIYLRNI QDTNETLFYR LVNNHLDEMM PVIYTPTVGA ACERFSEIYR RSRGVFISYQ NRHNMDDILQ NVPNHNIKVI VVTDGERILG LGDQGIGGMG IPIGKLSLYT ACGGISPAYT LPVVLDVGTN NQQLLNDPLY MGWRNPRITD DEYYEFVDEF IQAVKQRWPD VLLQFEDFAQ KNAMPLLNRY RNEICSFNDD IQGTAAVTVG TLIAASRAAG GQLSEKKIVF LGAGSAGCGI AEMIIAQTQR EGLSEEAARQ KVFMVDRFGL LTDKMPNLLP FQTKLVQKRE NLSDWDTDSD VLSLLDVVRN VKPDILIGVS GQTGLFTEEI IREMHKHCPR PIVMPLSNPT SRVEATPQDI IAWTEGNALV ATGSPFNPVV WKDKIYPIAQ CNNAFIFPGI GLGVIASGAS RITDEMLMSA SETLAQYSPL VLNGEGLVLP ELKDIQKVSR AIAFAVGKMA QQQGVAVKTS AEALQQAIDD NFWQAEYRDY RRTSI //