ID LEUC_PYRIL Reviewed; 414 AA. AC A1RVH3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 99. 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=Pisl_1806; OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Pyrobaculum. OX NCBI_TaxID=384616; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4184 / JCM 9189 / GEO3; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.; RT "Complete sequence of Pyrobaculum islandicum DSM 4184."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000504; ABL88955.1; -; Genomic_DNA. DR RefSeq; WP_011763530.1; NC_008701.1. DR AlphaFoldDB; A1RVH3; -. DR SMR; A1RVH3; -. DR STRING; 384616.Pisl_1806; -. DR GeneID; 4616859; -. DR KEGG; pis:Pisl_1806; -. DR eggNOG; arCOG01698; Archaea. DR HOGENOM; CLU_006714_3_4_2; -. DR OrthoDB; 255at2157; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000002595; 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 Gene3D; 3.30.499.10; Aconitase, domain 3; 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 NCBIfam; TIGR01343; hacA_fam; 1. DR NCBIfam; TIGR02086; IPMI_arch; 1. DR PANTHER; PTHR43822:SF25; HOMOACONITASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00330; Aconitase; 2. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 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. FT CHAIN 1..414 FT /note="3-isopropylmalate dehydratase large subunit" FT /id="PRO_1000063654" FT BINDING 295 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027" FT BINDING 353 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027" FT BINDING 356 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027" SQ SEQUENCE 414 AA; 45069 MW; E524DE87B167F3E6 CRC64; MPTWTEYIFQ KKLGHTPSPG DVVEVVPDLV GFHDLTGYHV LEVLESMGKV EVFDKERVVV AFDHLSPPPT QRAAEIMVYI RKHVKALELP HFYDVGGGIL HQIILEKYAM PEYVIFAADS HTNTAGAVGA FAHGMGATDI AAALKLGKTW VVIPAPFRVD MKGEFPPGVM GKDVALHLLK QFGAEGFNGY SVEVFVEIPK AFPMDDRATV ANMSTEMGAD ALMFIPDVVT VDYLQRERGV SYKPPDLQPG RYVDKYVVEL SKLEPLVAAP YSVDNVKAVR EVEGVEVDQV FIGSCTNGRL SDFEIAARIL RRGRVKSRCI AIPASYTIFR KALELGYIDI LTKAGCVVTY GTCGPCLGGH FGVAGPGEVV VSTSNRNFKG RMGHPDSKVY LANPATAAAA ALEGKIVDPR PYLL //