LEUC1_THEMA
ID LEUC1_THEMA Reviewed; 418 AA.
AC Q9WYC7;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=TM_0291;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(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; AE000512; AAD35379.1; -; Genomic_DNA.
DR PIR; C72394; C72394.
DR RefSeq; NP_228103.1; NC_000853.1.
DR RefSeq; WP_004083007.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYC7; -.
DR SMR; Q9WYC7; -.
DR STRING; 243274.THEMA_03270; -.
DR PRIDE; Q9WYC7; -.
DR EnsemblBacteria; AAD35379; AAD35379; TM_0291.
DR KEGG; tma:TM0291; -.
DR eggNOG; COG0065; Bacteria.
DR InParanoid; Q9WYC7; -.
DR OMA; GCGPCMG; -.
DR OrthoDB; 749418at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000008183; 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 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..418
FT /note="3-isopropylmalate dehydratase large subunit 1"
FT /id="PRO_0000076860"
FT BINDING 298
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 358
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"
SQ SEQUENCE 418 AA; 45447 MW; 18D41B4BFAA825BF CRC64;
MGKTLAEKIF SEHVGRDVKA GEIVLARVDI AMAQDGTGPL MINEFRELGF KEVKVPKAFL
FIDHASPSPR KELSNSQKMM REFGKEMGVK VFDAGDGISH QILAEKYVKP GDLVAGADSH
TCTAGGLGAF GTGMGSTDVA IIFGLGQNWF KVPETIKVVV NGKLQDGVYA KDIILEIARI
LGSDGATYKA LEFHGSCIEN MNVEDRLTIS NMAVEVGAKA GLMPSDEKTR EFLKKMGREE
DFRELKADPD AVYETEIEID ATTLEPLVSL PHYVDNVRKV SEVEKEKIKI DQVFIGTCTN
GRLQDLEIAL KILEKHGKHP DVRLIVGPAS RKVYMDALEK GIIKKFVELG AAVIPPGCGP
CVGIHMGVLG DGERVLSTQN RNFKGRMGNP NAEIYLASPA TAAATAVTGY ITDPRRFI
