ID   MDH_MORS5               Reviewed;         312 AA.
AC   P48364;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   13-SEP-2023, entry version 103.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
GN   Name=mdh;
OS   Moritella sp. (strain 5710).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=246794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8998993; DOI=10.1111/j.1574-6968.1996.tb08113.x;
RA   Ohkuma M., Ohtoko K., Takada N., Hamamoto T., Usami R., Kudo T.,
RA   Horikoshi K.;
RT   "Characterization of malate dehydrogenase from deep-sea psychrophilic
RT   Vibrio sp. strain no. 5710 and cloning of its gene.";
RL   FEMS Microbiol. Lett. 137:247-252(1996).
RN   [2]
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLN-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 35 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; D78194; BAA11301.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48364; -.
DR   SMR; P48364; -.
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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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_0000113316"
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="Q->H: Increases the thermal stability."
FT                   /evidence="ECO:0000269|PubMed:15043884"
SQ   SEQUENCE   312 AA;  31985 MW;  2C4A3253E5B5D2E6 CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPAGSDL SLYDIAPVTP GVAVDLSHIP TDVTIAGFAG
     MDPTDALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN LAGKCAEVCP NACIGIITNP
     VNTTVPIAAE VLKQAGVYDK RKLFGITTLD VIRSETFVSA LKGISLADVE VPVIGGHSGV
     TILPLLSQVK GVEFTAEEVV ALTARIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
     ALQGEKGIVE CTYVDGGSEH ATFFAQPVLL GKNGVEEVLA YGELSEFETN ARDAMLEELK
     ANITLGEEFV AG
//