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 29-MAY-2013, entry version 30.
DE RecName: Full=NAD-dependent malic enzyme;
DE Short=NAD-ME;
DE EC=1.1.1.38;
GN Name=maeA; 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 -!- 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; CP001657; ACT12538.1; -; Genomic_DNA.
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; HCERPIV; -.
DR ProtClustDB; PRK13529; -.
DR BioCyc; PCAR561230:GKCK-1536-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_1000215736.
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; 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
//
