ID F0T2P4_SYNGF Unreviewed; 424 AA.
AC F0T2P4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 03-APR-2013, entry version 15.
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=Sgly_2154;
OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Syntrophobotulus.
OX NCBI_TaxID=645991;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR;
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002547; ADY56443.1; -; Genomic_DNA.
DR RefSeq; YP_004266444.1; NC_015172.1.
DR EnsemblBacteria; ADY56443; ADY56443; Sgly_2154.
DR GeneID; 10249346; -.
DR KEGG; sgy:Sgly_2154; -.
DR PATRIC; 47035195; VBISynGly105927_2310.
DR KO; K01703; -.
DR BioCyc; SGLY645991:GHJ4-2191-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: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 301 301 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 361 361 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 364 364 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 424 AA; 45756 MW; A0B2B0DA838800F2 CRC64;
MGMTISEKIL AAHAGVDRVV PGEIINAKLD IVLANDVTGP VAIREFRKLG IDQVFDRDKV
VLVPDHFTPN KDIASAEQCK IMRDFVREQE ITHYWESGRV GIEHCLLPEQ GVVLPGDLII
GADSHTCTYG ALGAFSTGVG STDLAAGMAT GEAWFKIPET IRFVFHGNQY QPWISGKDLI
LYIIGQIGVD GALYSAMEFA GEGIKALSMD NRLTISNMAI EAGAKAGLIE PDEITLAYVS
SRAKRPYKIY NSDSDAKYAQ VFDYQTKDIP LQVACPHLPE NTKSVDEVSG IKMDQVVIGS
CTNGRLEDLE IAARILKGNS VHPEIRCLVF PGTQEIMLEA MRRGYIETLI EAGAAVSTPT
CGPCLGGHMG ILAKGEKALS TTNRNFVGRM GHPGSEVYLC NPAVAAASAI KGEIVHPREV
VKNG
//
