MAO1_ECOLU
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 03-AUG-2022, entry version 72.
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}.
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DR EMBL; CU928163; CAR12936.1; -; Genomic_DNA.
DR RefSeq; WP_000433464.1; NC_011751.1.
DR RefSeq; YP_002412470.1; NC_011751.1.
DR AlphaFoldDB; B7N4P2; -.
DR SMR; B7N4P2; -.
DR STRING; 585056.ECUMN_1734; -.
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; QMWDPVY; -.
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; IPR046346; Aminiacid_DH-like_N_sf.
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 SUPFAM; SSF53223; SSF53223; 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 BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 247
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 270
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 418
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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
