(data stored in SCRATCH zone)

SWISSPROT: D1CDW0_THET1

ID   D1CDW0_THET1            Unreviewed;       469 AA.
AC   D1CDW0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
GN   Name=leuC {ECO:0000256|HAMAP-Rule:MF_01026};
GN   OrderedLocusNames=Tter_0194 {ECO:0000313|EMBL:ACZ41116.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41116.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41116.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00326744}.
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_01026,
CC         ECO:0000256|SAAS:SAAS01116588};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01026};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01026};
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_01026, ECO:0000256|SAAS:SAAS00326733}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01026, ECO:0000256|SAAS:SAAS00326729}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC       type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01026,
CC       ECO:0000256|SAAS:SAAS00547538}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001825; ACZ41116.1; -; Genomic_DNA.
DR   RefSeq; WP_012874151.1; NC_013525.1.
DR   STRING; 525904.Tter_0194; -.
DR   EnsemblBacteria; ACZ41116; ACZ41116; Tter_0194.
DR   KEGG; ttr:Tter_0194; -.
DR   eggNOG; ENOG4105CQI; Bacteria.
DR   eggNOG; COG0065; LUCA.
DR   HOGENOM; HOG000226972; -.
DR   KO; K01703; -.
DR   OMA; FDHQVPA; -.
DR   OrthoDB; 749418at2; -.
DR   BioCyc; TTER525904:G1GGS-197-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000323; Chromosome 1.
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_01026; LeuC_type1; 1.
DR   InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
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; IPR033941; IPMI_cat.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR00170; leuC; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDW0.
DR   SWISS-2DPAGE; D1CDW0.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00319404};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00462403};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01026, ECO:0000256|SAAS:SAAS00326747};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS01079543};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS01079547};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00326736};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS01079535,
KW   ECO:0000313|EMBL:ACZ41116.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS01079498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN        8    458       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   METAL       348    348       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       408    408       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       411    411       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
SQ   SEQUENCE   469 AA;  51066 MW;  9F3B5A491D66BC27 CRC64;
     MAPRTLAEKV WEDHVVRRSP GEPDLLYIDL HLVHEVTSPQ AFEGLRLAGR KVRRPDLTLA
     TMDHNVPTTG LQFGITDPIS RAQVEALKKN CADFGIRLFG MGDPRQGIVH VIGPEQGLTQ
     PGMTIVCGDS HTSTHGAFGA LAFGIGTSEV EHVLATQCLW QRKPKMMAIE VNGELPIGVT
     AKDIILGIIE KIGVDGGNGH IIEYRGDTIR SLSMEQRMTI CNMSIEAGAR AGMIAPDDTT
     FKYIEGRPHA PKGKAWEKAL EYWQSLPTDE GAQFDKVVKL DASQLEPYVT WGTNPGQSVK
     ITGRVPDPSE AKTPAEREAM ERALKYMGLE PGTPMTEIKI DTVFIGSCTN ARIEDLRAAA
     KILNGRKVAK GVRAMVVPGS MQVKAQAERE GLDKIFKEAG FEWRDSGCSM CLGMNPDILE
     PGKRSASTSN RNFEGRQGPG GRTHLMSPIM AAAAAVAGHL VDVREWEVK
//

If you have problems or comments...

PBIL Back to PBIL home page