ID A0A0N1HCB1_9ACTN Unreviewed; 359 AA.
AC A0A0N1HCB1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-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=OV320_0164 {ECO:0000313|EMBL:KPI31756.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI31756.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI31756.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI31756.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC Evidence={ECO:0000256|ARBA:ARBA00000624};
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:KPI31756.1}.
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DR EMBL; LJCX01000010; KPI31756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1HCB1; -.
DR PATRIC; fig|1592329.3.peg.176; -.
DR Proteomes; UP000037870; Unassembled WGS sequence.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:RHEA.
DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Lyase {ECO:0000313|EMBL:KPI31756.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000037870}.
FT DOMAIN 8..353
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 359 AA; 38448 MW; 81038F18B6A7C491 CRC64;
MTAPRTFRIA GIPADGVGTE VVAAGRAVLD ALAADSGAFA FEWQEFPWGC GYYERTGKMM
DDDGLEQLKD FDAIYFGAVG WPNVPDHISL WGLRLKICQN FDQWANVRPV HFLPGVQSPL
RKADDTELDW VVVRENSEGE YAGLGGRNLG GRGPGGEVAV QSALFTEVGC ERIMRFAFDL
ARTRSRRKVS SVTKSNAQQY GMVLWDDVFK RVALDYPDVE TESVLVDAMS AKFVLKPEDL
SVVVASNLNA DILSDLGSAL AGSLGLAASA NLNPERRFPS MFEPVHGSAP DIAGQGLANP
IGAVGSAALM LEHFGLPEQA ARLNKAIETT TAAGILTRDV GGTASTEDVT KALIDALNV
//
