ID A5FR41_DEHSB Unreviewed; 416 AA.
AC A5FR41;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 44.
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=DehaBAV1_0747;
OS Dehalococcoides sp. (strain BAV1).
OC Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=216389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAV1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S.,
RA Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Ritalahti K.M., Loeffler F., Richardson P.;
RT "Complete sequence of Dehalococcoides sp. BAV1.";
RL Submitted (MAY-2007) 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; CP000688; ABQ17331.1; -; Genomic_DNA.
DR RefSeq; YP_001214209.1; NC_009455.1.
DR ProteinModelPortal; A5FR41; -.
DR STRING; 216389.DehaBAV1_0747; -.
DR EnsemblBacteria; ABQ17331; ABQ17331; DehaBAV1_0747.
DR GeneID; 5132027; -.
DR KEGG; deb:DehaBAV1_0747; -.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226971; -.
DR KO; K01703; -.
DR OMA; VIPFDHQ; -.
DR ProtClustDB; PRK00402; -.
DR BioCyc; DSP216389:GH6D-798-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 297 297 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 357 357 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 360 360 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 416 AA; 44541 MW; 396D03EB62E50E1E CRC64;
MNLVEKILAA HCGKTQVSPG DFINAKVDLV LANDITAPIA IKEFKKVGVS KVFDSKKIVF
VPDHFVPNKD IASAEQVKMV REFAREQGIL FFECGKMGVE HVILHEQGLV LPGDIVVGAD
SHTCTYGALG AFTTGMGSTD IAAAMATGEV WMKVPQTIKF NYSGKLPKWI GGKDLILYTI
GQTGVDGALY SAMFFCGEAI EALSMENRFT MSNMAIEAGG KAGLFRVDEK TLEYVTPRAK
RQYTVYDNDA DASYAKTYNF DISKLEPQVS LPHSPANARP VSQIGKIKVD QVIIGSCTNG
RLEDLAVSAK LLKGNVVHPD LRTIVIPGSQ QVYLDALKAG YIETFINAGV AVSTPTCGPC
LGGHMGILAA GERCLATTNR NFVGRMGSPK SEVYLAGPAV AAATAIKGYI AHPDEI
//
