ID A0A0C1D243_9SPHI Unreviewed; 468 AA. AC A0A0C1D243; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 08-JUN-2016, entry version 13. DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00326738}; DE EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01026}; DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01026}; DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01026}; GN Name=leuC {ECO:0000256|HAMAP-Rule:MF_01026}; 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, ECO:0000313|Proteomes:UP000031246}; RN [1] {ECO:0000313|EMBL:KIA90951.1, ECO:0000313|Proteomes:UP000031246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA90951.1, RC ECO:0000313|Proteomes:UP000031246}; 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|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00326744}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000256|HAMAP-Rule:MF_01026, CC ECO:0000256|SAAS:SAAS00326728}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01026}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01026}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00326733}. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP- CC Rule:MF_01026, ECO:0000256|SAAS:SAAS00326729}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {ECO:0000256|SAAS:SAAS00571581}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC CC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01026, CC ECO:0000256|SAAS:SAAS00547538}. 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 RefSeq; WP_039481933.1; NZ_JSYN01000037.1. DR EnsemblBacteria; KIA90951; KIA90951; OC25_23940. DR Proteomes; UP000031246; Unassembled WGS sequence. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. 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; 2. 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|HAMAP-Rule:MF_01026, KW ECO:0000256|SAAS:SAAS00436230}; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026, KW ECO:0000256|SAAS:SAAS00462403}; KW Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP- KW Rule:MF_01026, ECO:0000256|SAAS:SAAS00462388}; KW Complete proteome {ECO:0000313|Proteomes:UP000031246}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00462345}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01026, KW ECO:0000256|SAAS:SAAS00462401}; KW Isomerase {ECO:0000313|EMBL:KIA90951.1}; KW Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026, KW ECO:0000256|SAAS:SAAS00462258}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00432333, KW ECO:0000313|EMBL:KIA90951.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01026, KW ECO:0000256|SAAS:SAAS00462425}; KW Reference proteome {ECO:0000313|Proteomes:UP000031246}. FT DOMAIN 7 456 Aconitase. {ECO:0000259|Pfam:PF00330}. FT METAL 346 346 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01026}. FT METAL 406 406 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01026}. FT METAL 409 409 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01026}. 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 //