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Database: UniProt/TrEMBL
Entry: C7CML4_METED
LinkDB: C7CML4_METED
Original site: C7CML4_METED 
ID   C7CML4_METED            Unreviewed;       469 AA.
AC   C7CML4;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   26-NOV-2014, entry version 41.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00091369};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00091399};
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   ECO:0000313|EMBL:CAX27009.1};
GN   OrderedLocusNames=METDI5398 {ECO:0000313|EMBL:CAX27009.1};
OS   Methylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium
OS   dichloromethanicum (strain DM4)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=661410 {ECO:0000313|EMBL:CAX27009.1, ECO:0000313|Proteomes:UP000008070};
RN   [1] {ECO:0000313|Proteomes:UP000008070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5838 / DM4 {ECO:0000313|Proteomes:UP000008070};
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A.,
RA   Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C.,
RA   Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S.,
RA   Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G.,
RA   Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z.,
RA   Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J.,
RA   Medigue C., Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to
RT   investigate microbial metabolism of C1 compounds from natural and
RT   industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
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:SAAS00091401}.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate. {ECO:0000256|HAMAP-Rule:MF_01026,
CC       ECO:0000256|SAAS:SAAS00091406}.
CC   -!- COFACTOR:
CC       Note=Binds 1 4Fe-4S cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01026, ECO:0000256|SAAS:SAAS00091407};
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:SAAS00091405}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01026, ECO:0000256|SAAS:SAAS00091397}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC       type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01026}.
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DR   EMBL; FP103042; CAX27009.1; -; Genomic_DNA.
DR   RefSeq; YP_003070820.1; NC_012988.1.
DR   STRING; 661410.METDI5398; -.
DR   EnsemblBacteria; CAX27009; CAX27009; METDI5398.
DR   GeneID; 8194630; -.
DR   KEGG; mdi:METDI5398; -.
DR   PATRIC; 22529257; VBIMetExt143287_5135.
DR   eggNOG; COG0065; -.
DR   HOGENOM; HOG000226972; -.
DR   KO; K01703; -.
DR   OMA; QARAKTM; -.
DR   OrthoDB; EOG600DP5; -.
DR   BioCyc; MEXT661410:GJA1-5310-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
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; 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|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00033788};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00091270};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01026, ECO:0000256|SAAS:SAAS00091282};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008070};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00091327};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00091403};
KW   Isomerase {ECO:0000313|EMBL:CAX27009.1};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00091404};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00033784};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00091402}.
FT   METAL       349    349       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}.
FT   METAL       412    412       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
SQ   SEQUENCE   469 AA;  50606 MW;  704EEDB274D6952B CRC64;
     MTAPRTLYDK IWDDHVVDVE PDGSALLYID RHLVHEVTSP QAFEGLRVAG RTVRAPHKTL
     AVVDHNVQTS DRSKGIEDPE SRTQLEALAE NVRDFGIEFY DALDQRQGIV HIIGPEQGFT
     LPGQTIVCGD SHTSTHGAFG ALAHGIGTSE VEHVLATQTL IQRKAKNMRV TVDGTLPRGV
     SAKDIVLAII GEIGTAGGTG HVIEYAGEAI RALSMEGRMT ICNMSIEGGA RAGMVAPDET
     TYAYVNGRPK APKGAAFDAA RRYWESLATD EGAHFDREIR LDAANLPPLV SWGTSPEDIV
     SILGTVPDPA QIADENKRQS KEKALAYMGL TPGTRMTDVT LDRVFIGSCT NGRIEDLRIV
     AKMVEGRKVH DSVSAMVVPG SGLVKAQAEA EGIDRILKDA GFDWREPGCS MCLGMNPDKL
     RPGERCASTS NRNFEGRQGP RGRTHLVSPA MAAAAAVAGR FVDIREWRG
//
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