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Database: UniProt
Entry: A0A0J1DBR8_9BURK
LinkDB: A0A0J1DBR8_9BURK
Original site: A0A0J1DBR8_9BURK 
ID   A0A0J1DBR8_9BURK        Unreviewed;       205 AA.
AC   A0A0J1DBR8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00011998};
DE            EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998};
GN   ORFNames=AB595_12205 {ECO:0000313|EMBL:KLU36540.1};
OS   Massilia sp. WF1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU36540.1, ECO:0000313|Proteomes:UP000036336};
RN   [1] {ECO:0000313|Proteomes:UP000036336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA   Lou J., Gu H., Wang H., Xu J.;
RT   "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT   strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT   contaminated soil.";
RL   Submitted (JUN-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:KLU36540.1}.
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DR   EMBL; LELH02000012; KLU36540.1; -; Genomic_DNA.
DR   RefSeq; WP_047825177.1; NZ_LELH02000012.1.
DR   AlphaFoldDB; A0A0J1DBR8; -.
DR   PATRIC; fig|1406431.3.peg.1396; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000036336; 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   CDD; cd01577; IPMI_Swivel; 1.
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   InterPro; IPR033940; IPMI_Swivel.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036336}.
FT   DOMAIN          2..123
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   205 AA;  22640 MW;  01E6E4A418270BEA CRC64;
     MKPFSTIEAH AAPLMENSID TDVIVRIERI AKLKRGEFAP WAFEALRYRP DGSEEPGFIL
     NREPYRAAQV LLTGSNFGCG SSREMAVWAL QEFGIGCIIA PSFGDIFYGN CLQNGILPIR
     LDRAQVDLLA GGAARGETMT VDLRACTVSM ASTGTIAFRI PADQREALLS GLDEVDQTLG
     MTTAVDRFQQ RDRQLRPWAY DVHAQ
//
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