LEUC_RALSO
ID LEUC_RALSO Reviewed; 469 AA.
AC Q8XXX3;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026}; OrderedLocusNames=RSc1990;
GN ORFNames=RS03558;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000255|HAMAP-Rule:MF_01026}.
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:0000255|HAMAP-Rule:MF_01026};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01026};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
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DR EMBL; AL646052; CAD15692.1; -; Genomic_DNA.
DR RefSeq; WP_011001926.1; NC_003295.1.
DR AlphaFoldDB; Q8XXX3; -.
DR SMR; Q8XXX3; -.
DR STRING; 267608.RSc1990; -.
DR EnsemblBacteria; CAD15692; CAD15692; RSc1990.
DR GeneID; 60501506; -.
DR KEGG; rso:RSc1990; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_4; -.
DR OMA; CNMSIEM; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR033941; IPMI_cat.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00170; leuC; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..469
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076793"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 413
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ SEQUENCE 469 AA; 50796 MW; B451E96E44788AAE CRC64;
MAKTLYDKLW DDHVVHTEED GTTVLYIDRQ LLHEVTSPQA FEGLKLANRP VWRISANLAV
SDHNVPTTDR SHGIADPVSK LQVDTLDANC DSFGITQFKM TDKRQGIVHV IGPEQGATLP
GMTVVCGDSH TSTHGAFGAL AHGIGTSEVE HVLATQTLLA KKSKNMLVKV EGTLPRGCTA
KDIVLAIIGK IGTAGGTGYA MEFGGSAIRA LSMEGRMTVC NMAIEAGARA GMVGVDDITL
EYIKGRPFAP QGVEWEQAVA YWRSLHSDEG ARFDHVVELR AEEIRPQVSW GTSPEMVVSI
EDRVPDPDKE KDPVKRNAME RALEYMALQP NVAIGDIRID KVFIGSCTNS RIEDMRAAAW
VVQKLGKRIA SNVKLAMVVP GSGLVKEQAE REGLDKIFKA AGFEWREPGC SMCLAMNADR
LEPGERCAST SNRNFEGRQG AGGRTHLVSP AMAAAAALEG HFVDVRKLG
