ID A0A401GMX4_9APHY Unreviewed; 334 AA.
AC A0A401GMX4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
GN ORFNames=SCP_0505720 {ECO:0000313|EMBL:GBE83519.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE83519.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE83519.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
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 ECO:0000256|RuleBase:RU003405};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBE83519.1}.
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DR EMBL; BFAD01000005; GBE83519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401GMX4; -.
DR STRING; 139825.A0A401GMX4; -.
DR InParanoid; A0A401GMX4; -.
DR OrthoDB; 5059897at2759; -.
DR Proteomes; UP000287166; Unassembled WGS sequence.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate 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; IPR001252; Malate_DH_AS.
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.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU003405};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000287166};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU003405}.
FT DOMAIN 3..146
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 148..328
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 180
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 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 118..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 334 AA; 34381 MW; 130620D0075C7BF5 CRC64;
MTKAVVLGAA GGIGQPLSLL LKTNPLVKEL SLYDIVHAPG VAVDLSHIAT PAKVEGFLPP
NDGLKKALTG ADIVVIPAGV PRKPGMTRDD LFKINAGIVR DLATGIATVA PKAFVLVISN
PVNSTVPIVV EVFKKHGVFD PRRIFGVTTL DVVRASTFVS EILGDLSLTP SVSVPVVGGH
SGVTIVPLLS QSTHSLPAGF AQSSLEALTN RIQFGGDEVV KAKDGAGSAT LSMAYAGAEF
AGKVLRALKG EKGIVAPSFI NLAADKTGGA ALQKELGKDL EYFSAPVELG PEGVVKINGL
GKLSDYEKGL IAAALPELET NIDTGVSFIS PAKL
//