ID   MAO1_RHIME              Reviewed;         770 AA.
AC   O30807;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=NAD-dependent malic enzyme;
DE            Short=NAD-ME;
DE            EC=1.1.1.39;
GN   Name=dme; OrderedLocusNames=R01837; ORFNames=SMc00169;
OS   Rhizobium meliloti (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=RCR2011 / SU47;
RX   MEDLINE=98204936; PubMed=9535928; DOI=10.1074/jbc.273.15.9330;
RA   Mitsch M.J., Voegele R.T., Cowie A., Oesteras M., Finan T.M.;
RT   "Chimeric structure of the NAD(P)+- and NADP+-dependent malic enzymes
RT   of Rhizobium (Sinorhizobium) meliloti.";
RL   J. Biol. Chem. 273:9330-9336(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   MEDLINE=21396507; PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.,
RA   Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA   Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont
RT   Sinorhizobium meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=99337474; PubMed=10407149; DOI=10.1016/S0167-4838(99)00112-0;
RA   Voegele R.T., Mitsch M.J., Finan T.M.;
RT   "Characterization of two members of a novel malic enzyme class.";
RL   Biochim. Biophys. Acta 1432:275-285(1999).
CC   -!- FUNCTION: Required for symbiotic nitrogen fixation. Plays a key
CC       role in the conversion of malate to acetyl-CoA for efficient
CC       tricarboxylic acid cycle function in nitrogen-fixating bacteria.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese
CC       (By similarity).
CC   -!- ENZYME REGULATION: Subject to substrate inhibition and shows
CC       allosteric regulation by acetyl-CoA.
CC   -!- SUBUNIT: Homooctamer.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the malic
CC       enzymes family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC       acetyltransferase and butyryltransferase family.
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DR   EMBL; AF017443; AAB82459.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC46416.1; -; Genomic_DNA.
DR   RefSeq; NP_385943.1; -.
DR   GeneID; 1233502; -.
DR   GenomeReviews; AL591688_GR; R01837.
DR   KEGG; sme:SMc00169; -.
DR   NMPDR; fig|266834.1.peg.3131; -.
DR   HOGENOM; O30807; -.
DR   OMA; O30807; PEGDPRY.
DR   BioCyc; SMEL266834:SMC00169-MON; -.
DR   BRENDA; 1.1.1.39; 142.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) acti...; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N.
DR   InterPro; IPR012302; Malic_NAD_bd.
DR   InterPro; IPR012188; ME_PTA.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR002505; PTA_PTB.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF036684; ME_PTA; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Complete proteome; Metal-binding;
KW   Multifunctional enzyme; NAD; Oxidoreductase.
FT   CHAIN         1    770       NAD-dependent malic enzyme.
FT                                /FTId=PRO_0000160245.
FT   REGION        1    440       Malic enzyme.
FT   REGION      441    770       Phosphate acetyltransferase.
FT   ACT_SITE    107    107       Proton acceptor (By similarity).
FT   METAL       149    149       Divalent metal cation (By similarity).
FT   METAL       150    150       Divalent metal cation (By similarity).
FT   BINDING     175    175       NAD (By similarity).
FT   BINDING     300    300       NAD (By similarity).
SQ   SEQUENCE   770 AA;  82865 MW;  8FF3E3DA2D923108 CRC64;
     MNTGDKAKSQ AVPASGDIDQ QALFFHRYPR PGKLEIQPTK PLGNQRDLAL AYSPGVAAPC
     LAIKDNPETA ADFTARANLV AVVSNGTAVL GLGNIGPLAS KPVMEGKAVL FKKFAGIDVF
     DIEIDAPTVD RMVDVISALE PTFGGINLED IKAPECFEVE RRLREKMEIP VFHDDQHGTA
     IIVAAAVLNG LELAGKDIAE AKIVASGAGA AALACLNLLV TLGARRENIW VHDIEGLVYK
     GREALMDEWK AVYAQESDNR VLADSIGGAD VFLGLSAAGV LKPELLARMA EKPLIMALAN
     PTPEIMPEVA RAARPDAMIC TGRSDFPNQV NNVLCFPHIF RGALDCGART INEEMKMAAV
     RAIAGLAREE PSDVAARAYS GETPVFGPDY LIPSPFDQRL ILRIAPAVAK AAAESGVATR
     PIQDFDAYLD KLNRFVFRSG FIMKPVFAAA KNAAKNRVIF AEGEDERVLR AAQVLLEEGT
     AKPILIGRPQ IIETRLRRYG LRIRPDVDFE VVNPEGDPRY RDYVDDYFAL VGRLGVIPEA
     ARTIVRTNTT VIGALAVKRG EADALICGVE GRYSRHLRDV SQIIGKRSGV LDFSALSLLI
     SQRGATFFTD TYVSFSPSAE EIAQTTVMAA NEIRRFGITP RAALVSHSNF GSRDSESAFK
     MRTALQLVRE LAPDLEVDGE MHGDSAISEV LRQRVMPDST LNGEANLLVF PNLDAANITL
     GVVKTMTDSL HVGPILLGSA LPAHILSPSV TSRGVVNMAA LAVVESSHPV
//