ID C7MMM0_CRYCD Unreviewed; 423 AA.
AC C7MMM0;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 01-MAY-2013, entry version 28.
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=Ccur_04370;
OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / 12-3).
OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales;
OC Coriobacterineae; Coriobacteriaceae; Cryptobacterium.
OX NCBI_TaxID=469378;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700683 / DSM 15641 / 12-3;
RX PubMed=21304644; DOI=10.40456/sigs.12260;
RA Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA Kuske C., Detter J.C., Han C., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D.,
RA Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Chen A.,
RA Palaniappan K., Chain P., D'haeseleer P., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Rohde M., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Cryptobacterium curtum type strain (12-
RT 3).";
RL Stand. Genomic Sci. 1:93-100(2009).
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; CP001682; ACU94160.1; -; Genomic_DNA.
DR RefSeq; YP_003150842.1; NC_013170.1.
DR STRING; 469378.Ccur_04370; -.
DR EnsemblBacteria; ACU94160; ACU94160; Ccur_04370.
DR GeneID; 8374645; -.
DR KEGG; ccu:Ccur_04370; -.
DR PATRIC; 21524687; VBICryCur116861_0421.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226971; -.
DR KO; K01703; -.
DR OMA; VIPFDHQ; -.
DR ProtClustDB; CLSK2555394; -.
DR BioCyc; CCUR469378:GH4Z-437-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.
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 303 303 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 363 363 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 366 366 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 423 AA; 44550 MW; A0353F5320509A32 CRC64;
MTAQPMTMAE KLLSAHAGVD SVQPGQLIDC AVDLVLANDI TAPLAIRAFH ELGVKNVFDP
QKIALVPDHS TPNKDIASAK LTKMMRDFAY EQEITHYYEV GCMGIEHALL PEQGVVGAGD
LVIGADSHTC TYGALGAFST GMGSTDVGVA FATGRAWFKV PQTIRINLEG SLASTVTAKD
AILHIIGRIG VDGALYQAME FHGGAIEGLS IEGRMTMANM AIEAGGKAGL FPVDTTTRAY
LDARTERPYT VYNPDEGAVY ARTITIDAAD IVPTVAFPHL PSNTRPVAEA RDVAIDQAVI
GSCTNGRIED MRAAAHVLNG RTVHPRVRCI VIPATQAVFK QCIDEGLTDI FVNAHCVVST
PTCGPCLGGH MGVLAPGERA IATTNRNFIG RMGDTTSEVY LASPAVAAAS AVAGHIALPD
DLD
//
