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Database: UniProt
Entry: A0A0M2NIU0_9FIRM
LinkDB: A0A0M2NIU0_9FIRM
Original site: A0A0M2NIU0_9FIRM 
ID   A0A0M2NIU0_9FIRM        Unreviewed;       353 AA.
AC   A0A0M2NIU0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=CHK_2415 {ECO:0000313|EMBL:KKI50352.1};
OS   Christensenella hongkongensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC   Christensenella.
OX   NCBI_TaxID=270498 {ECO:0000313|EMBL:KKI50352.1, ECO:0000313|Proteomes:UP000034076};
RN   [1] {ECO:0000313|EMBL:KKI50352.1, ECO:0000313|Proteomes:UP000034076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKU16 {ECO:0000313|EMBL:KKI50352.1,
RC   ECO:0000313|Proteomes:UP000034076};
RA   Lau S.K., Teng J.L., Huang Y., Curreem S.O., Tsui S.K., Woo P.C.;
RT   "Draft genome sequence of bacteremic isolate Catabacter hongkongensis type
RT   strain HKU16T.";
RL   Submitted (APR-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:KKI50352.1}.
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DR   EMBL; LAYJ01000112; KKI50352.1; -; Genomic_DNA.
DR   RefSeq; WP_046444203.1; NZ_SMCZ01000001.1.
DR   AlphaFoldDB; A0A0M2NIU0; -.
DR   STRING; 270498.CHK_2415; -.
DR   PATRIC; fig|270498.16.peg.2164; -.
DR   OrthoDB; 9806254at2; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000034076; 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}; Reference proteome {ECO:0000313|Proteomes:UP000034076}.
FT   DOMAIN          4..348
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         76..89
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         135
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         278..290
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   SITE            142
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;  38590 MW;  118FAD9605A17975 CRC64;
     MEFTIAKISG DGIGPEISVE AVRVLNRIGE LYGHTFHFRD VDAGGIAIDK HGNPLPDSQL
     EICRQCDAVL LAAVGGEKWD NLPVDKRPEK GLLRLRGELG LFANLRPAII YNELKAACPL
     KDEIVGDNLD ILILRELTGD VYFGEKSGDD ITYSQDIMNY HDYEVERIAR LAFESARKRD
     KRLTSVDKAN VLSTSRLWRN TVTRVAKDYP DVELTHMYVD NAAMQLVRNP RQFDVVVTGN
     LFGDILTDEA SMITGSIGML PSASLGSTKL GMYEPIHGSA PDIAGQGKAN PIAMILSCAL
     MLRYSFDLEK EAQTIEASVK KVLAAGARTA DIAAGGEYVS TTEMSDLILA QLG
//
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