ID A0A0C1D243_9SPHI Unreviewed; 468 AA. AC A0A0C1D243; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 29-APR-2015, entry version 2. DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|SAAS:SAAS00091369}; DE EC=4.2.1.33 {ECO:0000256|SAAS:SAAS00091399}; GN ORFNames=OC25_23940 {ECO:0000313|EMBL:KIA90951.1}; OS Pedobacter kyungheensis. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA90951.1}; RN [1] {ECO:0000313|EMBL:KIA90951.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA90951.1}; RA Anderson B.M., Newman J.D.; RT "Pedobacter Kyungheensis."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000256|SAAS:SAAS00091401}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000256|SAAS:SAAS00091406}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|SAAS:SAAS00168894}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000256|SAAS:SAAS00168894}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000256|SAAS:SAAS00091405}. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. CC {ECO:0000256|SAAS:SAAS00091397}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIA90951.1}. 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; JSYN01000037; KIA90951.1; -; Genomic_DNA. DR UniPathway; UPA00048; UER00071. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 1. 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; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR PANTHER; PTHR11670; PTHR11670; 1. 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 {ECO:0000256|SAAS:SAAS00041964}; KW Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00091270}; KW Branched-chain amino acid biosynthesis KW {ECO:0000256|SAAS:SAAS00091282}; KW Iron {ECO:0000256|SAAS:SAAS00091327}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00091403}; KW Isomerase {ECO:0000313|EMBL:KIA90951.1}; KW Leucine biosynthesis {ECO:0000256|SAAS:SAAS00091404}; KW Lyase {ECO:0000256|SAAS:SAAS00033784, ECO:0000313|EMBL:KIA90951.1}; KW Metal-binding {ECO:0000256|SAAS:SAAS00091402}. SQ SEQUENCE 468 AA; 50789 MW; 49E657205A062BB6 CRC64; MSKTLVEKIW DAHVVKSEEG FPDILYIDTH LIHEVTSPQA FDGLRKRGLP VFRPKQTVAT ADHNVPTLNQ LLPIKEELSR YQVDMLTKNC AEFGVELYGL GHPFQGIVHV IGPELGITLP GKTMVCGDSH TSTHGAFGAI AFGIGTSQVE QVFATQCLLQ SKPKTMKIEV NGELGKGVGA KDIILYIIAQ ISAAGGTGYF IEYAGSAIES LSMEARMTIC NMSIEMGARG GLIAPDQITF DYIKGREFAP AGEEWDKALA YWKTLYSDAD AKFDSVLTFN AADIAPMITY GTNPGMGMGI QEHIPATAAQ PETEKVSYKK ALDYMGFDDD AALIGKPIDY VFIGSCTNSR IEDLREVANF VKDKHKAENV TVWIVPGSKQ VEQQAKNEGL DKIFEAAGFQ LREPGCSACL GMNEDKIPAG KYCVSTSNRN FEGRQGQNAR TLLASPLTAA AAAVTGKITD VREMLEKA //