LEUC2_BRADU
ID LEUC2_BRADU Reviewed; 468 AA.
AC Q89X34;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=3-isopropylmalate dehydratase large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01026};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Alpha-IPM isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01026};
DE Short=IPMI 2 {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Isopropylmalate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01026};
GN Name=leuC2 {ECO:0000255|HAMAP-Rule:MF_01026}; OrderedLocusNames=blr0488;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(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; BA000040; BAC45753.1; -; Genomic_DNA.
DR RefSeq; NP_767128.1; NC_004463.1.
DR RefSeq; WP_011083319.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89X34; -.
DR SMR; Q89X34; -.
DR STRING; 224911.27348736; -.
DR EnsemblBacteria; BAC45753; BAC45753; BAC45753.
DR GeneID; 64020347; -.
DR KEGG; bja:blr0488; -.
DR PATRIC; fig|224911.44.peg.9023; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_5; -.
DR InParanoid; Q89X34; -.
DR OMA; CNMSIEM; -.
DR PhylomeDB; Q89X34; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000002526; 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..468
FT /note="3-isopropylmalate dehydratase large subunit 2"
FT /id="PRO_0000076712"
FT BINDING 349
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 409
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 412
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ SEQUENCE 468 AA; 50824 MW; 6C5B7960C7C1C0A5 CRC64;
MSKPTTLYDK IWNDHLVHEA DDGTCLLYID RHLVHEVTSP QAFEGLRATG RKVHAPEKTL
AVVDHNVPTT DRTKPNPDPE SIEQIKALAD NAREFGIEYY NEFDKRQGIV HVIGPEQGFT
LPGTTIVCGD SHTSTHGAFG ALAHGIGTSE VEHVLATQTL IQKKAKNMRV TVDGKLPDGV
TGKDIILAII GEIGTAGGTG YVLEYAGEAI RALSMEGRMT VCNMSIEGGA RAGLVAPDQK
AYDFLRDRPK APKGAAWDAA MRYWEKLRSD DGAHFDHELR LDAAKLPPIV TWGTSPEDVI
SVTGIVPDPD KIADEAKRLS KHRALKYMGL TAGTKITDIK LDRVFIGSCT NGRIEDLRAA
AKIAEGKQVS ASVNAMVVPG SGIVKEQAEA EGLDKIFIKA GFEWREPGCS MCLAMNPDKL
KPEERCASTS NRNFEGRQGF KGRTHLVSPA MAAAAAIAGH FVDVREWR
