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 01-MAY-2013, entry version 35.
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.
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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; HCERPIV; -.
DR ProtClustDB; PRK13529; -.
DR BioCyc; ECOL585055:GJOM-1644-MONOMER; -.
DR GO; GO:0016619; F:malate dehydrogenase (oxaloacetate-decarboxylating) activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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.
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
//
