ID C7CML4_METED Unreviewed; 469 AA.
AC C7CML4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 29.
DE RecName: Full=3-isopropylmalate dehydratase large subunit;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leuC; OrderedLocusNames=METDI5398;
OS Methylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium
OS dichloromethanicum (strain DM4)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=661410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5838 / DM4;
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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC isopropylmalate.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD (By similarity).
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC type 1 subfamily.
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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; DIRQGIV; -.
DR ProtClustDB; PRK05478; -.
DR BioCyc; MEXT661410:GJA1-5310-MONOMER; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA: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: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; Aconitase_N; 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; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW Iron-sulfur; Isomerase; Leucine biosynthesis; Lyase; Metal-binding.
FT METAL 349 349 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 409 409 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 412 412 Iron-sulfur (4Fe-4S) (By similarity).
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
//
