ID   MDH_MORS2               Reviewed;         312 AA.
AC   Q7X3X5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
GN   Name=mdh;
OS   Moritella sp. (strain 2D2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella; unclassified Moritella.
OX   NCBI_TaxID=215801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   HIS-229.
RX   PubMed=15043884; DOI=10.1016/j.femsle.2004.02.004;
RA   Saito R., Nakayama A.;
RT   "Differences in malate dehydrogenases from the obligately piezophilic deep-
RT   sea bacterium Moritella sp. strain 2D2 and the psychrophilic bacterium
RT   Moritella sp. strain 5710.";
RL   FEMS Microbiol. Lett. 233:165-172(2004).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
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:0000269|PubMed:15043884};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5-10.0 for malate dehydrogenation, and 7.5-8.0 for
CC         oxaloacetate reduction.;
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AB097559; BAC77301.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7X3X5; -.
DR   SMR; Q7X3X5; -.
DR   BRENDA; 1.1.1.37; 7318.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01516; Malate_dehydrog_1; 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; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010097; Malate_DH_type1.
DR   InterPro; IPR023958; Malate_DH_type1_bac.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..312
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113315"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         229
FT                   /note="H->Q: Decreases the thermal stability."
FT                   /evidence="ECO:0000269|PubMed:15043884"
SQ   SEQUENCE   312 AA;  31941 MW;  DA8A42A7C8F5DB1B CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPAGSEL SLYDIAPVTP GVAVDLSHIP TDVTITGFSG
     IDPTAALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN LASKCAEVCP TACIGIITNP
     VNTTVPIAAE VLKQAGVYDK RKLFGITTLD VIRSETFVSA LKGISLADVA VPVIGGHSGA
     TILPLLSQVK GVEFTAEEIA TLTTRIQNAG TEVVEAKAGG GSATLSMGHA AARFGLSLVR
     ALQGEKGIVE CTYVDGGSEH ATFFAQPVLL GKNGVEEVLA YGDLSDFETN ARDAMLEELK
     ANITLGEEFV AG