LEUC_WOLSU
ID LEUC_WOLSU Reviewed; 422 AA.
AC Q7M9Z9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01027};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01027};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01027};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01027};
GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01027}; OrderedLocusNames=WS0559;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000255|HAMAP-Rule:MF_01027}.
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_01027};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01027};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01027};
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_01027}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01027}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}.
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DR EMBL; BX571658; CAE09693.1; -; Genomic_DNA.
DR RefSeq; WP_011138493.1; NC_005090.1.
DR AlphaFoldDB; Q7M9Z9; -.
DR SMR; Q7M9Z9; -.
DR STRING; 273121.WS0559; -.
DR EnsemblBacteria; CAE09693; CAE09693; WS0559.
DR KEGG; wsu:WS0559; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_7; -.
DR OMA; GIEHCLL; -.
DR OrthoDB; 749418at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000422; 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_01027; LeuC_type2; 1.
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; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01343; hacA_fam; 1.
DR TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR TIGRFAMs; TIGR02083; LEU2; 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..422
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076863"
FT BINDING 303
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 363
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 366
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ SEQUENCE 422 AA; 45745 MW; C0BAFB8412893D40 CRC64;
MGQTLTEKIF SAHTNKQVSA GEIIESPIDM VIGNDITTPL SIRAFEESGA TKLANPDGFC
IVMDHFIPAK DIASANQARI SRDFAKKHQL KHYFDERDMG IEHAILPEKG LVLPGDVIIG
ADSHTCTHGA LGAFATGMGS TDLAYAMITG KNWFKVPPSI RVVFKGKLQE HVYGKDLILE
IIRQIGVDGA LYKALEFQGD TIEQLSMDDR FSLCNMAIEA GAKNGIIAAD SITKEFLASR
KSLRAEPKYY QADADALYEQ TIEIDVEKLE PVIAYPFLPS NGKSISQAVK DDLKIDQAFI
GSCTNGRLSD LRIAAQILKG KRVHPDVRLI ITPGTQQIYK DAHQEGLIDT LLEAGALISN
PTCGACLGGY MGILGDNERC VSTTNRNFVG RMGARSSEVY LANSAVAAAS ALKGKITDPR
KL
