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Database: UniProt/TrEMBL
Entry: Q898T6_CLOTE
LinkDB: Q898T6_CLOTE
Original site: Q898T6_CLOTE 
ID   Q898T6_CLOTE            Unreviewed;       389 AA.
AC   Q898T6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   22-JAN-2014, entry version 91.
DE   SubName: Full=NAD-dependent malic enzyme;
DE            EC=1.1.1.38;
GN   OrderedLocusNames=CTC_00356;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of
RT   tetanus disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
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DR   EMBL; AE015927; AAO34993.1; -; Genomic_DNA.
DR   RefSeq; NP_781056.1; NC_004557.1.
DR   ProteinModelPortal; Q898T6; -.
DR   SMR; Q898T6; 2-382.
DR   STRING; 212717.CTC00356; -.
DR   EnsemblBacteria; AAO34993; AAO34993; CTC_00356.
DR   GeneID; 1059931; -.
DR   KEGG; ctc:CTC00356; -.
DR   PATRIC; 19508534; VBICloTet101274_0323.
DR   KO; K00027; -.
DR   OMA; CDINGAL; -.
DR   OrthoDB; EOG6QCD9W; -.
DR   ProtClustDB; CLSK911955; -.
DR   BioCyc; CTET212717:GJAM-313-MONOMER; -.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
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-EC.
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   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   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; Oxidoreductase.
FT   ACT_SITE     36     36       Proton donor (By similarity).
FT   ACT_SITE     91     91       Proton acceptor (By similarity).
FT   METAL       133    133       Divalent metal cation (By similarity).
FT   METAL       134    134       Divalent metal cation (By similarity).
FT   METAL       159    159       Divalent metal cation (By similarity).
SQ   SEQUENCE   389 AA;  42268 MW;  B89ECC08D413B72D CRC64;
     MDVKEMALKL HSEKKGKLEV VGKISVKNRE DLALAYTPGV AEPCVHISKD KNKVYEYTTK
     GNMVAVVTNG TAVLGLGNIG PEAALPVMEG KALLFKEFAN VDAFPICLDT EDPEEIIRTV
     KLMAPGFGGI NLEDIKAPEC FYIEERLKKE LDIPVFHDDQ HGTAIVVLAG IYNALKIVDK
     KLEEAKILIN GAGSAGIAIC KLLLNAGACN IVMCDINGSL VEGDENLNPA QKEIAKVTNK
     EKEKGKLVDV IKDKDIFIGV SGPKILTKEM VSTMAKDSIV FAMANPEPEI LPDEAKAGGA
     RVVATGRSDF PNQINNVLVF PGIFRGALDV KAREINEEMK IAAARGVANL IKEEDLNEEY
     IIPDPFNKEV AESVSKEVRR IAKEMNICK
//
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