ID A0A0B2BPF7_9ACTN Unreviewed; 354 AA.
AC A0A0B2BPF7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=CLV56_3574 {ECO:0000313|EMBL:PJJ54070.1};
OS Mumia flava.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Mumia.
OX NCBI_TaxID=1348852 {ECO:0000313|EMBL:PJJ54070.1, ECO:0000313|Proteomes:UP000230842};
RN [1] {ECO:0000313|EMBL:PJJ54070.1, ECO:0000313|Proteomes:UP000230842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27763 {ECO:0000313|EMBL:PJJ54070.1,
RC ECO:0000313|Proteomes:UP000230842};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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}.
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:PJJ54070.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PGEZ01000002; PJJ54070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2BPF7; -.
DR OrthoDB; 5289857at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000230842; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000230842}.
FT DOMAIN 6..343
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 283..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT SITE 140
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT SITE 190
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
SQ SEQUENCE 354 AA; 37483 MW; 05F2AF6ADCA63944 CRC64;
MTRSFSLAVI PGDGIGPEVV SEALRVLDET ARIHGFSFTQ TPYELGAERY LETGEVLTDE
TLAEIRGHDV ILLGAIGGRP GDPRIPAGLL ERNLLLRLRF ELDHYVNLRP TKTYPGVATP
LRDPGEVDFV VVREGTEGPY TGNGGRLRAG TRHEVATEVS LNTAYGVERV VRDAFRRAQS
RRKKLTLVHK TNVLVHAGGL WSRVVDEVAP EFPDVTVDYL HVDAATIFMT TDPARFDVIV
TDNLFGDIIT DLAGAISGGI GLAASGNVNP DGTAPSMFEP VHGSAPDIAG QGKADPTAAI
GSVALMLDHL GLPEAAAAID AAIMADITER TGPRTTKEVG EAIAARVAGD VAGA
//
