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Database: UniProt
Entry: C6DDS6
LinkDB: C6DDS6
Original site: C6DDS6 
ID   MAO1_PECCP              Reviewed;         565 AA.
AC   C6DDS6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   01-OCT-2014, entry version 37.
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};
GN   OrderedLocusNames=PC1_1494;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum
RT   PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC       {ECO:0000255|HAMAP-Rule:MF_01619}.
CC   -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2).
CC       {ECO:0000255|HAMAP-Rule:MF_01619}.
CC   -!- COFACTOR: 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.
CC       {ECO:0000255|HAMAP-Rule:MF_01619}.
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DR   EMBL; CP001657; ACT12538.1; -; Genomic_DNA.
DR   RefSeq; WP_015839764.1; NC_012917.1.
DR   RefSeq; YP_003017074.1; NC_012917.1.
DR   ProteinModelPortal; C6DDS6; -.
DR   STRING; 561230.PC1_1494; -.
DR   PRIDE; C6DDS6; -.
DR   EnsemblBacteria; ACT12538; ACT12538; PC1_1494.
DR   GeneID; 8132435; -.
DR   KEGG; pct:PC1_1494; -.
DR   PATRIC; 20487636; VBIPecCar70489_1507.
DR   eggNOG; COG0281; -.
DR   HOGENOM; HOG000042487; -.
DR   KO; K00027; -.
DR   OMA; IQDNNET; -.
DR   OrthoDB; EOG6QVRGM; -.
DR   BioCyc; PCAR561230:GKCK-1536-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_1000215736.
FT   ACT_SITE    104    104       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01619}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01619}.
FT   METAL       246    246       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_01619}.
FT   METAL       247    247       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_01619}.
FT   METAL       270    270       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_01619}.
FT   BINDING     157    157       NAD. {ECO:0000255|HAMAP-Rule:MF_01619}.
FT   BINDING     270    270       NAD. {ECO:0000255|HAMAP-Rule:MF_01619}.
FT   BINDING     418    418       NAD. {ECO:0000255|HAMAP-Rule:MF_01619}.
FT   SITE        270    270       Important for activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01619}.
SQ   SEQUENCE   565 AA;  62745 MW;  8385BDCD7269CE35 CRC64;
     MELEYESKRP LHIPYAGPIL LEFPLLNKGS AFTEEERANF NLHGLLPEAV ETIEEQAERA
     WRQYQEFKHD IEKHVYLRNI QDTNETLFYR LLDGHLSEMM PIIYTPTVGE ACEHFSDIYR
     RARGLFISYP NRAHIDDMLQ NATKQNVKVI VVTDGERILG LGDQGIGGMG IPIGKLSLYT
     ACGGISPAYT LPVVLDVGTN NPQRLNDPLY MGWRHPRITD DEYYEFVDEF IQAVKRRWPN
     VLLQFEDFAQ KNATPLLNRY RDEICSFNDD IQGTAAVALG SLIAASRAAG TQLRDQTVAF
     LGAGSAGCGI AEQIIAQMKS EGLSDEEARA RVFMVDRFGL LTDKLPNLLD FQSKLVQKSE
     LLANWDCNSD AISLLEVVRN AKPTILIGVS GQPGLFTEEI IREMHKHCAR PIVMPLSNPT
     SRVEARPEDI IRWTEGAALV ATGSPFSPVN YQDKVFPIAQ CNNSYIFPGI GLGVLASGAK
     RITDGMLMAA SRALADCSPL ANNGEGALLP DLADIQQVSK RIALEVGKAA QLQGAAVVTS
     SDALQKAIEH NFWQPQYRSY KRTSF
//
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