LEUC1_DEIRA
ID LEUC1_DEIRA Reviewed; 434 AA.
AC Q9RTY9;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=3-isopropylmalate dehydratase large subunit 1 {ECO:0000255|HAMAP-Rule:MF_01027};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027};
DE AltName: Full=Alpha-IPM isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01027};
DE Short=IPMI 1 {ECO:0000255|HAMAP-Rule:MF_01027};
DE AltName: Full=Isopropylmalate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01027};
GN Name=leuC1 {ECO:0000255|HAMAP-Rule:MF_01027}; OrderedLocusNames=DR_1610;
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; AAF11172.1; -; Genomic_DNA.
DR PIR; D75373; D75373.
DR RefSeq; NP_295333.1; NC_001263.1.
DR RefSeq; WP_010888248.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RTY9; -.
DR SMR; Q9RTY9; -.
DR STRING; 243230.DR_1610; -.
DR EnsemblBacteria; AAF11172; AAF11172; DR_1610.
DR KEGG; dra:DR_1610; -.
DR PATRIC; fig|243230.17.peg.1815; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_0; -.
DR InParanoid; Q9RTY9; -.
DR OMA; GCGPCMG; -.
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 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 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 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..434
FT /note="3-isopropylmalate dehydratase large subunit 1"
FT /id="PRO_0000076856"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 368
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 371
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ SEQUENCE 434 AA; 45540 MW; 5F1A9EA570E4B17D CRC64;
MTTGAPPFSG SSPQTTRPQT VAEKILSQRG SAAVYAGDLA VVEVDQVMVV DSIAQSFIER
MERDLGAVPK YPERVSIVVD HVAPASTVSV AQAQKEAREY AAKTGVRLFD VGRGICHQVL
MEEKLAQPGW IVLGSDSHST TYGAVAAFGS GMGATDIALA AASGKTWLRV PESVKVTLTG
DLRPGVTAKD VALEMIRVLG ADGATYQSVE IHAGDRFTRG ERMTLANLCV EAGAKAGLVV
PGGEILTDYG YDVPAWVYPD EGAAYAREVE IDLSALHPRM SAPSEVDNVH DVAELRGLKV
DQVFIGTCTN GRIEDLHAAA EVLRGRRVDP TTRLLVIPAS SQVMEEALQD GTLLTLQRAG
AVLGTPGCGP CMGRHQGVLA PGEVCVSTSN RNFIGRMGDK DAHIYLASPA VAAATAVMGR
VALPEDVAQV AASA
