ID A0A1K1T4Y5_9PSEU Unreviewed; 346 AA.
AC A0A1K1T4Y5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01035};
DE EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01035};
DE AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01035};
DE AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01035};
DE Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01035};
GN Name=leuB {ECO:0000256|HAMAP-Rule:MF_01035};
GN ORFNames=SAMN04489730_8103 {ECO:0000313|EMBL:SFW91697.1};
OS Amycolatopsis australiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW91697.1, ECO:0000313|Proteomes:UP000182740};
RN [1] {ECO:0000313|EMBL:SFW91697.1, ECO:0000313|Proteomes:UP000182740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW91697.1,
RC ECO:0000313|Proteomes:UP000182740};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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_01035}.
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_01035};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01035};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01035};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01035};
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|HAMAP-
CC Rule:MF_01035}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01035}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01035}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01035}.
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DR EMBL; FPJG01000006; SFW91697.1; -; Genomic_DNA.
DR RefSeq; WP_072481177.1; NZ_FPJG01000006.1.
DR AlphaFoldDB; A0A1K1T4Y5; -.
DR STRING; 546364.SAMN04489730_8103; -.
DR OrthoDB; 5289857at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000182740; 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_01035; LeuB_type2; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR023698; LeuB_actb.
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|HAMAP-Rule:MF_01035};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01035};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01035};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01035}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01035};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01035};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01035};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01035};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01035}.
FT DOMAIN 2..334
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 272..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT SITE 128
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT SITE 179
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
SQ SEQUENCE 346 AA; 36621 MW; 7DA97AFCA8DD0F72 CRC64;
MRLAVIPGDG IGPEVVSEAL KVLGEVVPTA EITNYDLGAA RWHATGELLP ESVLGELRQH
DAILLGAVGD PTVPSGILER GLLLRLRFEM DHHVNLRPAR LYPGVRGPLA DAGDVDMVVV
REGTEGPYAG TGGLLRKDTE HEIATEVSVN TAFGIRRVVA DAFNRAEARP RKHLTLVHKT
NVLEYAGSLW SRIVEEVSLE HPEVTVAYSH VDAATIHLVT DPSRFDVIVT DNLFGDIITD
LAAAVTGGIG LAASGNLDIT RRNPSMFEPV HGSAPDIAGQ GLADPTAAVL SVALLLDHLG
QKEAARRIEA SVAFDLATRD QSSPGATQAI GDRLAALVSS NVRTAG
//