ID A0A136LF05_9BACT Unreviewed; 356 AA.
AC A0A136LF05;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
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=UZ18_ATM001000403 {ECO:0000313|EMBL:KXK20239.1};
OS Armatimonadetes bacterium OLB18.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1617424 {ECO:0000313|EMBL:KXK20239.1, ECO:0000313|Proteomes:UP000070351};
RN [1] {ECO:0000313|EMBL:KXK20239.1, ECO:0000313|Proteomes:UP000070351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB18 {ECO:0000313|EMBL:KXK20239.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KXK20239.1}.
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DR EMBL; JZQX01000076; KXK20239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136LF05; -.
DR STRING; 1617424.UZ18_ATM001000403; -.
DR PATRIC; fig|1617424.3.peg.434; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000070351; 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 4..351
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 280..292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT SITE 138
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT SITE 186
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
SQ SEQUENCE 356 AA; 38161 MW; 6676CE0007BF97C3 CRC64;
MSHKVAVLAG DGIGPEVIAE AVKVLRRVSS DVEFESALVG GAAYDDCGRP LPEATLDLCR
NADAVLLGAV GGPRWDAIEP VSLRPEVGAL LPLRRELNLY ANVRPAKTLG PLLSASPLKG
DRGLIDLVVV RELTGGIYFG TPRERRDEGR VAVDTAVYSQ HEVERIAARA FEIARARRKE
IVSVDKANVL ETSRLWRETV TRMAAENSDV KVSHMLIDNC AMQLIRDPRQ FDVILTENMF
GDILSDEASM ITGSLGLLPS ASLSDAKNGK VFGMYEPVHG SAPDIAGQGR ANPLAAILSA
AMMLRYSFGE GEGAARIDRA VESALEQGLR TADIFVEGTK LVSTSEMGDA VLNAIV
//
