ID G2MSH1_9THEO Unreviewed; 418 AA.
AC G2MSH1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-APR-2013, entry version 13.
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; ORFNames=Thewi_0016;
OS Thermoanaerobacter wiegelii Rt8.B1.
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=697303;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rt8.B1;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Daligault H., Detter J.C.,
RA Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Pagani I., Hemme C., Woyke T.;
RT "Complete sequence of Thermoanaerobacter wiegelii Rt8.B1.";
RL Submitted (AUG-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; CP002991; AEM77532.1; -; Genomic_DNA.
DR RefSeq; YP_004818816.1; NC_015958.1.
DR EnsemblBacteria; AEM77532; AEM77532; Thewi_0016.
DR GeneID; 11082223; -.
DR KEGG; twi:Thewi_0016; -.
DR KO; K01703; -.
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; Iron; Iron-sulfur;
KW Leucine biosynthesis; Lyase; Metal-binding.
FT METAL 298 298 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 358 358 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 361 361 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 418 AA; 45658 MW; 9F6120574D31B861 CRC64;
MGLTLTQKIL SAKVGREVKP GELIEVDVDM VLGNDVTAPV AIKEFEKIGK EEVFDKTKIA
LVPDHFVPNK DIKSAEQVNI MRKFAKKHGI VNFFEVGQMG IEHALLPEKG LVLPGDVVIG
ADSHTCTYGA LTCFSTGVGS TDMAAAMATG KAWFKVPEAI KFVLKGNLQK WVSGKDVILY
IIGKIGVDGA LYKSMEFTGN IKALSMDDRF TIANMAIEAG AKNGIFDFDE ITEAYVKGRA
KREYKVFERD EDAEYSEVYE INLDEIRPQV AFPHLPENTR NIDEIGKVKI DQVVIGSCTN
GRMSDMEIAY KILKGKKVHP DVRLLIFPAT QEIYLECVKR GYIEEFIKAG AAVSTPTCGP
CLGGHMGILA KGERALATTN RNFVGRMGHP ESEVYLSSPA VAAASAIAGY IVSPEEVE
//
