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LEUC2_DEIRA
ID   LEUC2_DEIRA             Reviewed;         431 AA.
AC   Q9RTI6;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01027};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027};
DE   AltName: Full=Alpha-IPM isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01027};
DE            Short=IPMI 2 {ECO:0000255|HAMAP-Rule:MF_01027};
DE   AltName: Full=Isopropylmalate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01027};
GN   Name=leuC2 {ECO:0000255|HAMAP-Rule:MF_01027}; OrderedLocusNames=DR_1778;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE000513; AAF11331.1; -; Genomic_DNA.
DR   PIR; H75354; H75354.
DR   RefSeq; NP_295501.1; NC_001263.1.
DR   RefSeq; WP_010888413.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RTI6; -.
DR   SMR; Q9RTI6; -.
DR   STRING; 243230.DR_1778; -.
DR   EnsemblBacteria; AAF11331; AAF11331; DR_1778.
DR   KEGG; dra:DR_1778; -.
DR   PATRIC; fig|243230.17.peg.1990; -.
DR   eggNOG; COG0065; Bacteria.
DR   HOGENOM; CLU_006714_3_4_0; -.
DR   InParanoid; Q9RTI6; -.
DR   OMA; GIEHCLL; -.
DR   OrthoDB; 749418at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000002524; Chromosome I.
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   Pfam; PF00330; Aconitase; 2.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01343; hacA_fam; 1.
DR   TIGRFAMs; TIGR02086; IPMI_arch; 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..431
FT                   /note="3-isopropylmalate dehydratase large subunit 2"
FT                   /id="PRO_0000076857"
FT   BINDING         301
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         361
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         364
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ   SEQUENCE   431 AA;  46177 MW;  2CAF9A57247AAE01 CRC64;
     MGMTIAEKML AAHSGHDTVV PGQLIECATD WVLCHEITTP AALRMLEERG MDRVFDPQKI
     VAVPDHSVPA MNIKAAKMYQ KLKSWVQEKG IEHFYDVGRG GIAHVVLENT GLMKPGQTLV
     SGDSHTCNAG ALGAFATGVG STDLAGAIYA GKVWFKVPET MLIRVTGKTN PGVTPKDIVL
     EVIKQIGADG ANYMVMEWVG DYIDQLDMEG RFTLTNMAIE AGGKTGIVAV DDTTRAYMQQ
     RGVSPEQYTE YQSDPDAKYK VVVEIDAAQV EPTVAYPHIP SNGRVAGSDR IRVTHAYVGS
     CTNGRITDLR DVARILKGRK VAQDVQMIVV PATQAIWKQA AQEGLLEIFV DAGASVSYPS
     CGACLGMHSG VLGPDDICIS SSNRNFVGRM GDPSAQIYLA SPATVAASAV EGFIADPRRY
     DAEGNDLNAA D
 
 
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