(data stored in SCRATCH zone)

SWISSPROT: D5E9U8_METMS

ID   D5E9U8_METMS            Unreviewed;       413 AA.
AC   D5E9U8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 60.
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=Mmah_0418 {ECO:0000313|EMBL:ADE35949.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35949.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35949.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       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-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC       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 type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01027}.
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DR   EMBL; CP001994; ADE35949.1; -; Genomic_DNA.
DR   RefSeq; WP_013036892.1; NC_014002.1.
DR   EnsemblBacteria; ADE35949; ADE35949; Mmah_0418.
DR   GeneID; 8982555; -.
DR   KEGG; mmh:Mmah_0418; -.
DR   eggNOG; arCOG01698; Archaea.
DR   eggNOG; COG0065; LUCA.
DR   HOGENOM; HOG000226971; -.
DR   KO; K16792; -.
DR   OMA; IEHCLLP; -.
DR   OrthoDB; 15714at2157; -.
DR   BioCyc; MMAH547558:G1GHT-418-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001059; 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   Pfam; PF00330; Aconitase; 2.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01343; hacA_fam; 1.
DR   TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9U8.
DR   SWISS-2DPAGE; D5E9U8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01027, ECO:0000313|EMBL:ADE35949.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          6..283
FT                   /note="Aconitase"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          286..405
FT                   /note="Aconitase"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   METAL           297
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT   METAL           355
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT   METAL           358
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
SQ   SEQUENCE   413 AA;  43941 MW;  DB66000CA6975497 CRC64;
     MSTISEKIFS RAAGKEAKAN DFVIADIDYA MAHDGTSILA VRSFRQMEVE KVWDPSRIVI
     PFDHLAPANS DTTAGLQKDI RGWVRQQGIR NFYDIGNGIC HQVLPEKGFA MPGKLIVGAD
     SHSCTYGAFG AFGTGVGATD MAEIFASGKL WFRVPESIRI TAEGKLDDRV CAKDLTLKII
     GEVTASGATY KAVEFYGDAI ENLSMAGRMT LSNMAIEMGA KAGIVPPDAT TFEYLKNRAV
     SDYEPVYSDG DADYVAEYHI DVNSLEPQVA CPHEVDNVCG VSGIAGKKLD QAFIGTCTNG
     RLEDLEAAAE VLKGNEVAVR TIIIPASRQI MKEAASKGLI EIFLDAGATM GTPGCGPCLG
     GHMGVIGEGE VCISTANRNF RGRMGTGGYI YLASPATVAA SAIKGEITDP RNV
//

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