ID   A0A0C1D243_9SPHI        Unreviewed;       468 AA.
AC   A0A0C1D243;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   11-DEC-2019, entry version 30.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026};
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            Short=IPMI {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 and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00326744}.
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:0000256|HAMAP-Rule:MF_01026,
CC         ECO:0000256|SAAS:SAAS01116588};
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-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC       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. LeuC type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01026,
CC       ECO:0000256|SAAS:SAAS00547538}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIA90951.1}.
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DR   EMBL; JSYN01000037; KIA90951.1; -; Genomic_DNA.
DR   RefSeq; WP_039481933.1; NZ_JSYN01000037.1.
DR   EnsemblBacteria; KIA90951; KIA90951; OC25_23940.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000031246; Unassembled WGS sequence.
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: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-UniRule.
DR   CDD; cd01583; IPMI; 1.
DR   Gene3D; 3.30.499.10; -; 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; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR033941; IPMI_cat.
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, ECO:0000256|SAAS:SAAS00319404};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00462403};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00326747};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS01079543};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS01079547}; Isomerase {ECO:0000313|EMBL:KIA90951.1};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00326736};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS01079535,
KW   ECO:0000313|EMBL:KIA90951.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS01079498}.
FT   DOMAIN          7..456
FT                   /note="Aconitase"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   METAL           346
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   METAL           406
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   METAL           409
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-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
//