ID   MDH2_BURTA              Reviewed;         329 AA.
AC   Q2T4T8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Malate dehydrogenase 2;
DE            EC=1.1.1.37;
GN   Name=mdh2; OrderedLocusNames=BTH_II1617;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 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; CP000085; ABC35074.1; -; Genomic_DNA.
DR   RefSeq; YP_439811.1; -.
DR   GeneID; 3844557; -.
DR   GenomeReviews; CP000085_GR; BTH_II1617.
DR   KEGG; bte:BTH_II1617; -.
DR   TIGR; BTH_II1617; -.
DR   HOGENOM; Q2T4T8; -.
DR   OMA; Q2T4T8; FPDYRHA.
DR   BioCyc; BTHA271848:BTH_II1617-MON; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_01517; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR001236; Lactate/malate_DH.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010945; Malate_DH_SF1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23382; MDH_SF1; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   ProDom; PD003052; Mal_dehydrog; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    329       Malate dehydrogenase 2.
FT                                /FTId=PRO_0000292370.
FT   NP_BIND      12     18       NAD (By similarity).
FT   NP_BIND     130    132       NAD (By similarity).
FT   ACT_SITE    188    188       Proton acceptor (By similarity).
FT   BINDING      93     93       Substrate (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
FT   BINDING     106    106       NAD (By similarity).
FT   BINDING     113    113       NAD (By similarity).
FT   BINDING     132    132       Substrate (By similarity).
FT   BINDING     163    163       Substrate (By similarity).
SQ   SEQUENCE   329 AA;  36101 MW;  7771577BC065D687 CRC64;
     MNTEAKRIAV SGAAGQIAYS LLFRIAQGDL LGEDQPVILQ LLDLPQAYGA VQGVVMELQD
     CAFPLLKEIQ VATDPHAAFL NADYAFLVGS KPRTKGMERR DLLAENAAIF RTQGRALNEA
     ASRDVKVLVV GNPANTNASI LRRFAPDLPD DAISAMIRLD HNRAVSMLAQ RCNVDVDSIA
     DMVVWGNHSP TMFPDYRHAR IGRRLVKDLI NDENWYRESF IPKVAQRGTA IIEARGASSA
     ASAANAAIDQ MRDWIFGSDG RWVSMSVPSD GSYGIAPGLM FGVPVICDGG RYERVKDIGI
     DAFARQRIDL SVRELQEEAD VVNRLFADR
//