ID   MAO1_ECOL6              Reviewed;         565 AA.
AC   Q8FHH1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=NAD-dependent malic enzyme;
DE            Short=NAD-ME;
DE            EC=1.1.1.38;
GN   Name=sfcA; OrderedLocusNames=c1912;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese
CC       (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
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DR   EMBL; AE014075; AAN80371.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_753809.1; -.
DR   HSSP; P23368; 1GZ3.
DR   GeneID; 1035818; -.
DR   GenomeReviews; AE014075_GR; c1912.
DR   KEGG; ecc:c1912; -.
DR   NMPDR; fig|199310.1.peg.1852; -.
DR   HOGENOM; Q8FHH1; -.
DR   OMA; Q8FHH1; IQDNNET.
DR   BRENDA; 1.1.1.38; 292881.
DR   GO; GO:0016619; F:malate dehydrogenase (oxaloacetate-decarbox...; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01619; -; 1.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N.
DR   InterPro; IPR012302; Malic_NAD_bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    565       NAD-dependent malic enzyme.
FT                                /FTId=PRO_0000160217.
FT   ACT_SITE    104    104       Proton donor (By similarity).
FT   ACT_SITE    175    175       Proton acceptor (By similarity).
FT   METAL       246    246       Divalent metal cation (By similarity).
FT   METAL       247    247       Divalent metal cation (By similarity).
FT   METAL       270    270       Divalent metal cation (By similarity).
FT   BINDING     157    157       NAD (By similarity).
FT   BINDING     270    270       NAD (By similarity).
FT   BINDING     418    418       NAD (By similarity).
FT   SITE        270    270       Important for activity (By similarity).
SQ   SEQUENCE   565 AA;  63202 MW;  E0F0F413E83F8F3A 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 SEMLAQYSPL VLNGEGLVLP ELKDIQKVSR AIAFAVGKMA QQQGVAVKTS
     AEALQQAIDD NFWHAEYRDY RRTSI
//