ID C9RAX0_AMMDK Unreviewed; 421 AA.
AC C9RAX0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 23.
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=Adeg_0227;
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Ammonifex.
OX NCBI_TaxID=429009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4;
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) 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; CP001785; ACX51397.1; -; Genomic_DNA.
DR RefSeq; YP_003238247.1; NC_013385.1.
DR STRING; 429009.Adeg_0227; -.
DR EnsemblBacteria; ACX51397; ACX51397; Adeg_0227.
DR GeneID; 8490192; -.
DR KEGG; adg:Adeg_0227; -.
DR PATRIC; 20879964; VBIAmmDeg104956_0225.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226971; -.
DR KO; K01703; -.
DR BioCyc; ADEG429009:GHG1-263-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 299 299 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 359 359 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 362 362 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 421 AA; 45621 MW; 9E967C2AAF6F952E CRC64;
MGMTITEKIL AFHAGKEYVE PGEIVKCRVD VLLANDITAP LAIKEFERLK VPLFEPNALV
LVPDHFTPNK DIKSAEQAKT VREFARRHRI PHYFEVGRMG IEHCLLPEQG LVVAGDVVIG
ADSHTCTYGA LGAFATGVGS TDLAAAMALG ETWFRVPPSL KFVYTGKLKP WVGGKDLILY
TIGQIGVEGA LYCAMEFTGP VIEELSMDGR FTMCNMAVEA GAKNGIIAPD EKTAAYLEGR
ARRPYKFFQS DPDARYQAVY EFDVSRLEPQ VALPHSPANT RPVTEVTHIT IDQVVIGSCT
NGRLEDLRVA AQVLKGKKVH PYVRLIVIPG TQEIYRQALR EGLIEIFLEA GGAVSTPTCG
PCLGGHMGVL AKGERAVATT NRNFVGRMGH PESEVYLASP AVAAASAVLG RLAHPDEVVK
A
//
