ID F0K7L4_CLOAE Unreviewed; 422 AA.
AC F0K7L4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 03-APR-2013, entry version 16.
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=CEA_G3177;
OS Clostridium acetobutylicum (strain EA 2018).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=863638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EA 2018;
RX PubMed=21284892; DOI=10.1186/1471-2164-12-93;
RA Hu S., Zheng H., Gu Y., Zhao J., Zhang W., Yang Y., Wang S., Zhao G.,
RA Yang S., Jiang W.;
RT "Comparative genomic and transcriptomic analysis revealed genetic
RT characteristics related to solvent formation and xylose utilization in
RT Clostridium acetobutylicum EA 2018.";
RL BMC Genomics 12:93-93(2011).
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 2 subfamily.
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DR EMBL; CP002118; ADZ22214.1; -; Genomic_DNA.
DR RefSeq; YP_005672309.1; NC_017295.1.
DR ProteinModelPortal; F0K7L4; -.
DR EnsemblBacteria; ADZ22214; ADZ22214; CEA_G3177.
DR GeneID; 12233927; -.
DR KEGG; cay:CEA_G3177; -.
DR PATRIC; 47113356; VBICloAce167171_3208.
DR KO; K01703; -.
DR OMA; VIPFDHQ; -.
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: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_01027; LeuC_type2; 1; -.
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 InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR PANTHER; PTHR11670:SF6; PTHR11670:SF6; 1.
DR Pfam; PF00330; Aconitase; 2.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase_N; 1.
DR TIGRFAMs; TIGR01343; hacA_fam; 1.
DR TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR TIGRFAMs; TIGR02083; LEU2; 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; Leucine biosynthesis; Lyase; Metal-binding.
FT METAL 302 302 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 362 362 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 365 365 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 422 AA; 45528 MW; 58AD0FADF14D7B31 CRC64;
MKKPMTMTQK ILANHAGLDY VEAGQLITAN LDLVLGNDVT TPVAVKAFKT MGTNKVFDKK
KVAIVPDHFT PNKDIKSAEH CKMIRQFAKS KEIENYFEIG EMGIEHALIP EKGLAVPGDV
IIGADSHTCT YGALGVFSTG VGSTDMAVGM ATGKAWFKVP EAIKFVLKGK PAKWVSGKDI
ILHIIGMIGV DGALYKSMEY TGDGLEYLSM DDRFTIANMA IEAGAKNGIF PVDEKTIEYM
KGRSDRELKK FDADEDAEYS RVIEIDLSTL KPTVAFPHLP ENTKTIDQVG EVNVDQVVIG
SCTNGRMEDL RIAASILKGK KIKKGIRLIV FPGTQNIYLE AMEEGLVRTF IEAGGIVSTP
TCGPCLGGHM GILAEGERAI STTNRNFVGR MGHPKSEVYL ASPAVAAASA IAGKIVSPEE
VL
//
