ID A0A0F7SE22_9BASI Unreviewed; 340 AA.
AC A0A0F7SE22;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 Name=SSCI85690.1 {ECO:0000313|EMBL:CDW99828.1};
GN ORFNames=SPSC_02646 {ECO:0000313|EMBL:CDU24017.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDW99828.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|EMBL:CDU24017.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SscI8 {ECO:0000313|EMBL:CDU24017.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW99828.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman J.Paul.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) 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 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}.
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DR EMBL; LK056664; CDU24017.1; -; Genomic_DNA.
DR EMBL; CCFA01005204; CDW99828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7SE22; -.
DR STRING; 49012.A0A0F7SE22; -.
DR OrthoDB; 5059897at2759; -.
DR Proteomes; UP000242770; 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:SF73; MALATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU003405}.
FT DOMAIN 26..166
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 168..333
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 30..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 138..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 340 AA; 35567 MW; 48D0112A28C6EC54 CRC64;
MFARQALRSA SAARSFSTSA ANNRAVAVLG ASGGIGQPLS LLLKQNPLVT DLRLYDVRLA
PGVAADISHV NTPSTTTGYQ ADQLGEALKD VEVIVIPAGV PRKPGMTRDD LFNTNASIVR
DLAKKAAEVA PKAHLLIISN PVNSTVPIVA EVFKKAGVYD PKKLYGVTTL DVTRASTFLS
GISGKKPSET IVPVVGGHSG VTIVPLLSQA NGSDAVAKGE QYEKLVHRIQ FGGDEVVKAK
DGAGSATLSM AYAAAVFSDS LLKALNGEKG IKECAYVESP LYKDQGATFF ASPVTLGKDG
VEEIHSVGKV SAEEEKLLEA AIPELAKNIK KGVDWYAASP
//
