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Database: UniProt
Entry: A0A0F2S7Q4_9FIRM
LinkDB: A0A0F2S7Q4_9FIRM
Original site: A0A0F2S7Q4_9FIRM 
ID   A0A0F2S7Q4_9FIRM        Unreviewed;       353 AA.
AC   A0A0F2S7Q4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000256|HAMAP-Rule:MF_01033};
GN   ORFNames=VR66_26530 {ECO:0000313|EMBL:KJS46220.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS46220.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS46220.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS46220.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CC       {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC         ECO:0000256|RuleBase:RU004445};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC         ECO:0000256|RuleBase:RU004445};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000256|ARBA:ARBA00004762,
CC       ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008319, ECO:0000256|HAMAP-Rule:MF_01033}.
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:KJS46220.1}.
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DR   EMBL; LADV01000330; KJS46220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2S7Q4; -.
DR   PATRIC; fig|1629714.3.peg.1513; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000033503; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   NCBIfam; TIGR00169; leuB; 1.
DR   PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 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:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01033};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01033};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01033};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01033};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01033};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01033};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01033}.
FT   DOMAIN          3..348
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         75..88
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         277..289
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   SITE            141
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   SITE            188
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
SQ   SEQUENCE   353 AA;  37923 MW;  C7141B5912D63614 CRC64;
     MPNVLVLPGD GIGLEITPEA VKVLEAVLKG RSTQLNFEYG LIGGAGIDAV GKALPDETLA
     AAKAADAILM GSVGGPKWDT LPAPQRPELG GLLPIRKALG LFANIRPVKM LPMLTDASTL
     RTEVVENVDL VVLRELTGGL YFGEKGRGTN PRSAYDTLVY TEEEIRRIVE LGFQMAAKRR
     GRLCSVDKAN VLESSRFWRE ITVEVAKDFP EVELSHMYVD NAAMQLVRWP AQFDVIVTEN
     MFGDILTDLA SMLLGSIGMI PSASMNGSKG LYEPAHGSAP DIAGQNIANP LATILSGALM
     LRYSFGLEDE ALMIEGAIER VLQEGYRTAD LAKPGDKVLG TIEMGNAVVE ALK
//
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