ID   MAOX_MYCTU              Reviewed;         548 AA.
AC   P71880;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=Putative malate oxidoreductase [NAD];
DE            EC=1.1.1.38;
DE   AltName: Full=Malic enzyme;
GN   Name=mez; OrderedLocusNames=Rv2332, MT2394;
GN   ORFNames=MTCY3G12.02c, MTCY98.01;
OS   Mycobacterium tuberculosis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   MEDLINE=22206494; PubMed=12218036;
RX   DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX842579; CAB02059.2; -; Genomic_DNA.
DR   EMBL; AE000516; AAK46686.1; -; Genomic_DNA.
DR   PIR; E70705; E70705.
DR   RefSeq; NP_216848.2; -.
DR   RefSeq; NP_336872.1; -.
DR   HSSP; P27443; 1LLQ.
DR   GeneID; 887962; -.
DR   GeneID; 924018; -.
DR   GenomeReviews; AE000516_GR; MT2394.
DR   GenomeReviews; AL123456_GR; Rv2332.
DR   KEGG; mtc:MT2394; -.
DR   KEGG; mtu:Rv2332; -.
DR   TIGR; MT2394; -.
DR   TubercuList; Rv2332; -.
DR   HOGENOM; P71880; -.
DR   LinkHub; P71880; -.
DR   GO; GO:0016619; F:malate dehydrogenase (oxaloacetate-decarbox...; IEA:EC.
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   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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    548       Putative malate oxidoreductase [NAD].
FT                                /FTId=PRO_0000160248.
FT   ACT_SITE     96     96       Proton donor (By similarity).
FT   ACT_SITE    169    169       Proton acceptor (By similarity).
FT   METAL       240    240       Divalent metal cation (By similarity).
FT   METAL       241    241       Divalent metal cation (By similarity).
FT   METAL       264    264       Divalent metal cation (By similarity).
FT   BINDING     264    264       NAD (By similarity).
FT   BINDING     410    410       NAD (By similarity).
FT   SITE        264    264       Important for activity (By similarity).
SQ   SEQUENCE   548 AA;  59423 MW;  407248FE6BDFC875 CRC64;
     MSDARVPRIP AALSAPSLNR GVGFTHAQRR RLGLTGRLPS AVLTLDQQAE RVWHQLQSLA
     TELGRNLLLE QLHYRHEVLY FKVLADHLPE LMPVVYTPTV GEAIQRFSDE YRGQRGLFLS
     IDEPDEIEEA FNTLGLGPED VDLIVCTDAE AILGIGDWGV GGIQIAVGKL ALYTAGGGVD
     PRRCLAVSLD VGTDNEQLLA DPFYLGNRHA RRRGREYDEF VSRYIETAQR LFPRAILHFE
     DFGPANARKI LDTYGTDYCV FNDDMQGTGA VVLAAVYSGL KVTGIPLRDQ TIVVFGAGTA
     GMGIADQIRD AMVADGATLE QAVSQIWPID RPGLLFDDMD DLRDFQVPYA KNRHQLGVAV
     GDRVGLSDAI KIASPTILLG CSTVYGAFTK EVVEAMTASC KHPMIFPLSN PTSRMEAIPA
     DVLAWSNGRA LLATGSPVAP VEFDETTYVI GQANNVLAFP GIGLGVIVAG ARLITRRMLH
     AAAKAIAHQA NPTNPGDSLL PDVQNLRAIS TTVAEAVYRA AVQDGVASRT HDDVRQAIVD
     TMWLPAYD
//