GenomeNet

Database: UniProt
Entry: B7L7H9
LinkDB: B7L7H9
Original site: B7L7H9 
ID   MAO1_ECO55              Reviewed;         565 AA.
AC   B7L7H9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   14-MAY-2014, entry version 40.
DE   RecName: Full=NAD-dependent malic enzyme;
DE            Short=NAD-ME;
DE            EC=1.1.1.38;
GN   Name=maeA; OrderedLocusNames=EC55989_1611;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
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.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   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: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC   -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2).
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.
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; CU928145; CAU97465.1; -; Genomic_DNA.
DR   RefSeq; YP_002402684.1; NC_011748.1.
DR   ProteinModelPortal; B7L7H9; -.
DR   SMR; B7L7H9; 15-564.
DR   STRING; 585055.EC55989_1611; -.
DR   EnsemblBacteria; CAU97465; CAU97465; EC55989_1611.
DR   GeneID; 7145456; -.
DR   KEGG; eck:EC55989_1611; -.
DR   PATRIC; 38476670; VBIEscCol113220_1642.
DR   eggNOG; COG0281; -.
DR   HOGENOM; HOG000042487; -.
DR   KO; K00027; -.
DR   OMA; IQDNNET; -.
DR   OrthoDB; EOG6QVRGM; -.
DR   BioCyc; ECOL585055:GJOM-1644-MONOMER; -.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_01619; NAD_malic_enz; 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   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; SM00919; Malic_M; 1.
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_1000185990.
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;  63179 MW;  FFD61313F708EF3A 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 AEMIISQTQR 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
//
DBGET integrated database retrieval system