ID   A0A0G4MT94_9PEZI        Unreviewed;       372 AA.
AC   A0A0G4MT94;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE            EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN   ORFNames=BN1708_007379 {ECO:0000313|EMBL:CRK37506.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK37506.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK37506.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK37506.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:18365, ChEBI:CHEBI:15361, ChEBI:CHEBI:15588,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.83;
CC         Evidence={ECO:0000256|ARBA:ARBA00001361};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR   EMBL; CVQH01024750; CRK37506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4MT94; -.
DR   STRING; 100787.A0A0G4MT94; -.
DR   OrthoDB; 143577at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR011829; TTC_DH.
DR   NCBIfam; TIGR02089; TTC; 1.
DR   PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT   DOMAIN          13..356
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   372 AA;  40063 MW;  677D97D0A61C740F CRC64;
     MSPSAVPARK SYSIASMGAD GIGPEVVDAG VEVLKALAET LDSFDLDFTD YDWSSETYKK
     TGKYIPDGGL EQLKKHDAIL FGAVGAPDVP DHISLWGLRL AICQPFQQYA NVRPTRVLPG
     TQSPLRNCKT GDLDWVIIRE NSEGEYAGQG GRSHRGELWE TATEVSIFTR HGVERLMRFA
     FETAQNRPRK LLTVVTKSNA QRNGMVLWDE VAAIVAKDFP DVTVDKMLVD AMTTRMVLKP
     ETLDTIVATN LHADILSDLA AALAGSIGIA PTSNLDPSRQ NPSMFEPIHG SAFDITGKGV
     ANPVATFWTA AEMLTWLGER QAADQLMACV EAVCQAGINT ADLGGSATTK EVTAAVIVEI
     KTKLGKATKA AQ
//