(data stored in ACNUC7421 zone)

SWISSPROT: C4KKU6_SULIK

ID   C4KKU6_SULIK            Unreviewed;       415 AA.
AC   C4KKU6;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
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=M164_0277 {ECO:0000313|EMBL:ACR40911.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40911.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40911.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate. {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; CP001402; ACR40911.1; -; Genomic_DNA.
DR   RefSeq; WP_012735440.1; NC_012726.1.
DR   EnsemblBacteria; ACR40911; ACR40911; M164_0277.
DR   KEGG; sid:M164_0277; -.
DR   HOGENOM; HOG000226971; -.
DR   KO; K01703; -.
DR   OMA; CNMSIEM; -.
DR   OrthoDB; POG093Z03G6; -.
DR   BioCyc; SISL426118:GI01-279-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-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:UniProtKB-HAMAP.
DR   CDD; cd01583; IPMI; 1.
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; 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; IPR033941; IPMI_cat.
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   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KKU6.
DR   SWISS-2DPAGE; C4KKU6.
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-
KW   Rule:MF_01027};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
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};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01027}.
FT   DOMAIN       25    407       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   METAL       298    298       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01027}.
FT   METAL       356    356       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01027}.
FT   METAL       359    359       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01027}.
SQ   SEQUENCE   415 AA;  45150 MW;  7A1D3EF2E96E7B95 CRC64;
     MSAKTLTEKI LSRASGKDIS PGDVIEAKVD LVAFHDLTGY HVIEVMERAN MIKVFDKSKL
     VIAFDHLAPP PDVRSAEIQG YIRKFVKSEG IPNFYDINYG ILHEVMIEQY ANPGQVILAA
     DSHTTTSGAV GAFAQGMGAS DIAAAVITGK TWLVVPQPFK VVLEGKPAKW ITGKDVALKL
     LGDFKADYFN GMTLEIFVKD PLSFPMDYRA TVSNMGIEMN ADALMFIPDQ ETKRYIKEMR
     GYEPELVTPD NGAKYVDEYT IQLDEMEPLV AAPHSVDNVK VVNELEGTPV DQVYIGSCTN
     GRLSDFEIAA KIMKGKKVKS RCIAIPASYR MFKEALERGY IQTLVDAGCI VTYGTCGPCL
     GGHFGIAGPG ENIVSTSSRN FKGRMGSNEA KVYLSGPAVA AISALEGKIT DPRVI
//

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