ID A0A109JNI8_9BRAD Unreviewed; 216 AA.
AC A0A109JNI8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00011998};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998};
GN ORFNames=AS156_11050 {ECO:0000313|EMBL:KWV52257.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV52257.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV52257.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV52257.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000256|ARBA:ARBA00002695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000256|ARBA:ARBA00000491};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004729}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|ARBA:ARBA00011271}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009845}.
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:KWV52257.1}.
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; LNCU01000084; KWV52257.1; -; Genomic_DNA.
DR RefSeq; WP_066510030.1; NZ_LNCU01000084.1.
DR AlphaFoldDB; A0A109JNI8; -.
DR OrthoDB; 9777465at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000057737; Unassembled WGS sequence.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR00171; leuD; 1.
DR PANTHER; PTHR43345:SF5; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT; 1.
DR PANTHER; PTHR43345; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 2-RELATED-RELATED; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 4..124
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 216 AA; 23543 MW; 87575DBE2E4596FA CRC64;
MPKPFNTLTA TAAPIMRSNI DTDVIIRIER LVGNSIRGTL GKWAFGSLRY LPDGSENPDF
ILNREPYRQA EILVTGPNFG CGSSREGAVW SLQEMGIRAV IGSGFGDIFF ANCFQNGILP
VVVDKVVVDS LAADIEATQG AGKVSIDLEA QTIVSPSGAR HTFEIDPRRR EGLLKGLDEV
ALTLQRDDEI RAFQASDRAA RPWIHFARTP ASRTSA
//