ID A0A066X0P0_COLSU Unreviewed; 371 AA.
AC A0A066X0P0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=CSUB01_02254 {ECO:0000313|EMBL:KDN62537.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN62537.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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}.
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:KDN62537.1}.
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DR EMBL; JMSE01001324; KDN62537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X0P0; -.
DR STRING; 1173701.A0A066X0P0; -.
DR eggNOG; KOG0785; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR OMA; MRFAFKL; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000027238; 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:UP000027238}.
FT DOMAIN 13..356
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 371 AA; 40324 MW; F4984C92F9D3E8BD CRC64;
MLPTALPARR TYSIASMGAD GIGPEVIEAG VEVLKVLADT LGTFELKFAD YDWSSETYKK
TGKYIPDGGL EQLKKHDAIL FGAVGAPDVP DHISLWGLRL AICQSFQQYA NVRPTRVLRG
TQSPLRNCAE GDLDWVIIRE NSEGEYAGQG GRSHRGFPWE TATEVSIFTR HGVERLIRFA
FETARGRPRK LLTFVTKSNA QRNGMVLWDE VVYEVAKDFP DVSLDKMLVD AMTTRMVLNP
KSLDTIVATN LHADILSDLA AALAGSIGIA PTSNLDPTRK HPSMFEPIHG SAFDITGKGV
ANPVATFWTA AEMLEWLGEK DAAAQLMECV ESVTGRGVVT ADLGGKATTK EVTSAVVNEI
KTSLGRSKNA Q
//
