ID   MAO2_RHIME              Reviewed;         761 AA.
AC   O30808;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=NADP-dependent malic enzyme;
DE            Short=NADP-ME;
DE            EC=1.1.1.40;
GN   Name=tme; OrderedLocusNames=R00394; ORFNames=SMc01126;
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   -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = pyruvate + CO(2) +
CC       NADPH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese.
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; AF017444; AAB82460.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC41831.1; -; Genomic_DNA.
DR   RefSeq; NP_384500.1; -.
DR   GeneID; 1232028; -.
DR   GenomeReviews; AL591688_GR; R00394.
DR   KEGG; sme:SMc01126; -.
DR   NMPDR; fig|266834.1.peg.1688; -.
DR   HOGENOM; O30808; -.
DR   OMA; O30808; RTEGMNQ.
DR   BioCyc; SMEL266834:SMC01126-MON; -.
DR   BRENDA; 1.1.1.40; 142.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (oxaloacetate-decarbox...; 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   Complete proteome; Metal-binding; Multifunctional enzyme; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    761       NADP-dependent malic enzyme.
FT                                /FTId=PRO_0000160246.
FT   REGION        1    437       Malic enzyme.
FT   REGION      438    761       Phosphate acetyltransferase.
FT   ACT_SITE    104    104       Proton donor (By similarity).
FT   ACT_SITE    172    172       Proton acceptor (By similarity).
FT   METAL       146    146       Divalent metal cation (By similarity).
FT   METAL       147    147       Divalent metal cation (By similarity).
FT   BINDING     172    172       NAD (By similarity).
FT   BINDING     297    297       NAD (By similarity).
FT   CONFLICT    228    228       L -> F (in Ref. 1; AAB82460).
FT   CONFLICT    609    636       DMPTSEELADIAEEAAGLAKRLGYVPRV -> KHADLRGAG
FT                                (in Ref. 1; AAB82460).
FT   CONFLICT    761    761       T -> TRRGSAESRKTAGTSSVAASPDG (in Ref. 1;
FT                                AAB82460).
SQ   SEQUENCE   761 AA;  82209 MW;  A342A5F41F39DBC7 CRC64;
     MPGIDKTDRA MTSVTAQEAL DFHSQGRPGK LEISPTKPMA TQRDLSLAYS PGVAVPVKAI
     ADDPATAYDY TARGNMVAVI SNGTAILGLG NLGALASKPV MEGKAVLFKR FADVDSIDLE
     VDTENVDEFV NCVRFLGPSF GGINLEDIKA PDCFIIEQRL REVMDIPVFH DDQHGTAIIA
     AAGLVNALTL TGRDFKTAKL VCNGAGAAAI ACIELIKAMG FNPENIILCD TKGVIYKGRT
     DGMNQWKSAH AVETDRRTLA EALDGADVFF GLSAKGALSA DMVRSMGARP IIFAMANPDP
     EITPEEVALI RDDAIVATGR SDYPNQVNNV LGFPYIFRGA LDVRASTIND AMKIAAAEAL
     ANLAKEDVPD DVAAAYQGNR PRFGPQYIIP VPFDPRLISA IPMAVAKAAM ETGVARKPIE
     DLKAYGQQLS ARRDPIASTL QRIVERVRRQ PKRIVFAEGE EVQMMRSAIA YANQQLGTAL
     LLGREEVMRE TAEREGIDLD RAGIQIVNAR LSKRVGAYTD FLYSRLQRKG YLFRDVQRLI
     NTDRNHFAAS MVALGDADGM VTGLTRNYST ALEDVRRCID PKPGHRVIGV SIALCRGRTV
     LVADTAVHDM PTSEELADIA EEAAGLAKRL GYVPRVAMLA YSTFGHPSGE RSERVREAVK
     ILDRRRVDFE YDGEMAADVA LNARVMEQYP FCRLSGTANV LVMPAFHSAS ISTKMLQELG
     GSTVIGPLLV GLDKSVQIAS MSAKDSDLVN LAAIAAYNAG T
//