ID   MDH2_AQUAE              Reviewed;         334 AA.
AC   O67581;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Malate dehydrogenase 2;
DE            EC=1.1.1.37;
GN   Name=mdh2; OrderedLocusNames=aq_1665;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
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DR   EMBL; AE000657; AAC07547.1; -; Genomic_DNA.
DR   PIR; D70444; D70444.
DR   RefSeq; NP_214147.1; -.
DR   HSSP; P80039; 1GV0.
DR   GeneID; 1193297; -.
DR   GenomeReviews; AE000657_GR; aq_1665.
DR   KEGG; aae:aq_1665; -.
DR   NMPDR; fig|224324.1.peg.1162; -.
DR   HOGENOM; O67581; -.
DR   OMA; O67581; EISANIR.
DR   BioCyc; AAEO224324:AQ_1665-MON; -.
DR   BRENDA; 1.1.1.37; 189781.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00487; -; 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; 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   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    334       Malate dehydrogenase 2.
FT                                /FTId=PRO_0000113423.
FT   NP_BIND      20     25       NAD (By similarity).
FT   NP_BIND     136    138       NAD (By similarity).
FT   ACT_SITE    193    193       Proton acceptor (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
FT   BINDING     113    113       NAD (By similarity).
FT   BINDING     138    138       Substrate (By similarity).
FT   BINDING     169    169       Substrate (By similarity).
SQ   SEQUENCE   334 AA;  36698 MW;  18E64807D16B7C96 CRC64;
     MKGKLINSFL MKKPKISVIG AGKVGENVAY LLTILGLGDV YLFARYKKGL EPAKAKALDL
     KQMAVLMDID INVKGISYDK EGFEELKGSD IVVITAGIPR REGMSREDLL YENLKILKKF
     TDAIKEYAKD SIIIVVSNPV DTLTYATIKL TGFEPRRVIG MAGVLDSARF KNFVKEKIGI
     SNADIRTLVL GTHGDLMVPV TSHSFIGDKP IEEVFSASEI DELIEKTRKG GAQIVSLMGT
     SAYYAPAASV VIMVESIIND RKRVMPCSVY VEGEAAKHYE IEGVCIGLPV VLGKKGVEDF
     ELVNLSGYEK RELLRSAKTL KEMVSLADKL LNEL
//