ID   A0A0C1D243_9SPHI        Unreviewed;       468 AA.
AC   A0A0C1D243;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   06-JUL-2016, entry version 14.
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   -!- 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. LeuC
CC       type 1 subfamily. {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}.
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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-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
//