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   03-AUG-2022, entry version 121.
DE   RecName: Full=Malate dehydrogenase 2 {ECO:0000250|UniProtKB:P61889};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:P61889};
GN   Name=mdh2 {ECO:0000250|UniProtKB:P61889}; OrderedLocusNames=aq_1665;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   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 aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:P61889}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000250|UniProtKB:P61889};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07547.1; -; Genomic_DNA.
DR   PIR; D70444; D70444.
DR   RefSeq; NP_214147.1; NC_000918.1.
DR   RefSeq; WP_010881084.1; NC_000918.1.
DR   AlphaFoldDB; O67581; -.
DR   SMR; O67581; -.
DR   STRING; 224324.aq_1665; -.
DR   EnsemblBacteria; AAC07547; AAC07547; aq_1665.
DR   KEGG; aae:aq_1665; -.
DR   PATRIC; fig|224324.8.peg.1288; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_0; -.
DR   InParanoid; O67581; -.
DR   OrthoDB; 870724at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..334
FT                   /note="Malate dehydrogenase 2"
FT                   /id="PRO_0000113423"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         19..25
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         136..138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
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