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Database: UniProt
Entry: A0A1X6MP42_9APHY
LinkDB: A0A1X6MP42_9APHY
Original site: A0A1X6MP42_9APHY 
ID   A0A1X6MP42_9APHY        Unreviewed;       326 AA.
AC   A0A1X6MP42;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN   ORFNames=POSPLADRAFT_1060977 {ECO:0000313|EMBL:OSX57903.1};
OS   Postia placenta MAD-698-R-SB12.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX57903.1, ECO:0000313|Proteomes:UP000194127};
RN   [1] {ECO:0000313|EMBL:OSX57903.1, ECO:0000313|Proteomes:UP000194127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX57903.1,
RC   ECO:0000313|Proteomes:UP000194127};
RG   DOE Joint Genome Institute;
RA   Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA   Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA   Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA   Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT   "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000774};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
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DR   EMBL; KZ110606; OSX57903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6MP42; -.
DR   STRING; 670580.A0A1X6MP42; -.
DR   OrthoDB; 5059897at2759; -.
DR   Proteomes; UP000194127; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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   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; IPR010097; Malate_DH_type1.
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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194127};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          3..138
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          140..320
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         8..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         87
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         110..112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   326 AA;  33380 MW;  CCCFDC654CAB4B7F CRC64;
     MSKAVVLGAA GGIGQPLALL LKSNPLVKEL ALFDIVNTPG VAADLSHIST PAKVSGYLPP
     DDGLKKALTG ADIVVIPAGV PRKPGINAGI VRDLATGIAT AAPKASILVI SNPVNSTVPI
     VVEVLKKHGV FDPKKVFGVT TLDVVRAQTF AAEVLGDLSL ASKLTVPVVG GHSGVTIVPL
     FSQSSTPLPS GFTKSDLEAL TTRVQFGGDE VVKAKDGAGS ATLSMAYAGA EFAEKVLRAL
     NGEKGIVAPS FVHLSADKEG GEAVKKEIGQ DLEYFSVRVQ LGPGGVEKLH GLGSITEYER
     SLVQAAVPDL ASNIDKGVSF IASPKL
//
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