(data stored in SCRATCH zone)

SWISSPROT: C8W661_DESAS

ID   C8W661_DESAS            Unreviewed;       420 AA.
AC   C8W661;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01027};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01027};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01027};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
GN   Name=leuC {ECO:0000256|HAMAP-Rule:MF_01027};
GN   OrderedLocusNames=Dtox_0596 {ECO:0000313|EMBL:ACV61516.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61516.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61516.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|HAMAP-Rule:MF_01027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC         Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC         EC=4.2.1.33; Evidence={ECO:0000256|HAMAP-Rule:MF_01027};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01027};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01027};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01027}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01027}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC       type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_01027}.
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DR   EMBL; CP001720; ACV61516.1; -; Genomic_DNA.
DR   RefSeq; WP_015756235.1; NC_013216.1.
DR   STRING; 485916.Dtox_0596; -.
DR   EnsemblBacteria; ACV61516; ACV61516; Dtox_0596.
DR   KEGG; dae:Dtox_0596; -.
DR   eggNOG; ENOG4105CQI; Bacteria.
DR   eggNOG; COG0065; LUCA.
DR   HOGENOM; HOG000226971; -.
DR   KO; K01703; -.
DR   OMA; IEHCLLP; -.
DR   OrthoDB; 749418at2; -.
DR   BioCyc; DACE485916:G1GFV-602-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   CDD; cd01583; IPMI; 1.
DR   Gene3D; 3.30.499.10; -; 1.
DR   HAMAP; MF_01027; LeuC_type2; 1.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR   InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR   InterPro; IPR033941; IPMI_cat.
DR   InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 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;
DR   PRODOM; C8W661.
DR   SWISS-2DPAGE; C8W661.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01027,
KW   ECO:0000256|SAAS:SAAS00319404};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01027};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01027, ECO:0000256|SAAS:SAAS01079543};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01027,
KW   ECO:0000256|SAAS:SAAS01079547};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01027,
KW   ECO:0000256|SAAS:SAAS01079535};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01027,
KW   ECO:0000256|SAAS:SAAS01079498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN        7    411       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   METAL       300    300       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01027}.
FT   METAL       360    360       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01027}.
FT   METAL       363    363       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01027}.
SQ   SEQUENCE   420 AA;  44617 MW;  83F28D56A1E2FF8B CRC64;
     MGMTVTEKIL AAHAGKDKVV PGELVNVKVD LALGNDITAP VAIKEFSKIG VDSVFDREKI
     ALVLDHFIPA KDIASAEQGK AVKNFAQKHG IVNFFDVGKM GIEHCLLPEQ GLVGPGDLVI
     GADSHTCTYG GLGAFSTGVG STDLAAAMAL GETWLKVPES MLFVFEGELR PWVGGKDLIL
     HIIGDIGVDG ALYKAMEFAG PAIEKLSMDG RLTMANMAIE AGGKNGIVAP DEITRAYVEG
     RVKKPYTFYK SDADAVYSDI RRYDASKIEP LVAFPHLPEN TRPVSQAGLV ELDQVVIGSC
     TNGRMEDLRL AAGVLKGKKV SDRIRLIVIP GTQQIYKQAM REGLIEIFID AGGAVSTPTC
     GPCLGGYMGI LAKGERSLAT TNRNFVGRMG SPESEVYLCN PAVAAASAIL GRIAGPWEVE
//

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