ID A0A0A3IHD2_9BACI Unreviewed; 357 AA.
AC A0A0A3IHD2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=CD32_23440 {ECO:0000313|EMBL:KGR82233.1};
OS Lysinibacillus odysseyi 34hs-1 = NBRC 100172.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR82233.1, ECO:0000313|Proteomes:UP000030437};
RN [1] {ECO:0000313|EMBL:KGR82233.1, ECO:0000313|Proteomes:UP000030437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR82233.1,
RC ECO:0000313|Proteomes:UP000030437};
RA Zhang F., Wang G., Zhang L.;
RT "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172.";
RL Submitted (FEB-2014) 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}.
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:KGR82233.1}.
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DR EMBL; JPVP01000060; KGR82233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A3IHD2; -.
DR STRING; 1220589.CD32_23440; -.
DR eggNOG; COG0473; Bacteria.
DR Proteomes; UP000030437; 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000030437}.
FT DOMAIN 2..344
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 357 AA; 39079 MW; BC2B0AA951D57DC8 CRC64;
MKIAVIPGDG IGKEVMKEAL LVLETLQELE EDLSVDTTIF DWSSDNYMRT GKMMPEDGLS
ILSEYDAILF GAIGDKRVPD DVTVWELIMP IRKQFNQYVN FRPVKSLPGI TSPLVRADNI
DFAIFRENTE GEYSNSGGRL YMDKPQELAI QNTVMTKTGI TNIVSAACDY ALKYGKSTVT
SATKSNAVIH TMKFWDDCVA EQMKKYPELQ LQSYYIDALV AYFIERPQEF EVVVASNLFG
DILSDLGSAV IGGLGLSPSG NINPERIYPS MFEPVHGSAP DIAGRGIANP IAQIWSLALL
LGHLGRTDLE KVIVTAIEQV LEAGEVKTAD IGGAATTAEM GAAICEAVKS CFERRVV
//
