(data stored in ACNUC7421 zone)

SWISSPROT: D1CDW1_THET1

ID   D1CDW1_THET1            Unreviewed;       197 AA.
AC   D1CDW1;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000256|HAMAP-Rule:MF_01031};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01031};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01031};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01031};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01031};
GN   Name=leuD {ECO:0000256|HAMAP-Rule:MF_01031};
GN   OrderedLocusNames=Tter_0195 {ECO:0000313|EMBL:ACZ41117.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41117.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41117.1, 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_01031, ECO:0000256|SAAS:SAAS00682407}.
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_01031,
CC         ECO:0000256|SAAS:SAAS01124695};
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_01031, ECO:0000256|SAAS:SAAS00682398}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01031, ECO:0000256|SAAS:SAAS00682400}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01031, ECO:0000256|SAAS:SAAS00682390}.
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DR   EMBL; CP001825; ACZ41117.1; -; Genomic_DNA.
DR   RefSeq; WP_012874152.1; NC_013525.1.
DR   STRING; 525904.Tter_0195; -.
DR   EnsemblBacteria; ACZ41117; ACZ41117; Tter_0195.
DR   KEGG; ttr:Tter_0195; -.
DR   eggNOG; ENOG4105MQS; Bacteria.
DR   eggNOG; COG0066; LUCA.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OMA; AFTTHTG; -.
DR   OrthoDB; 1384217at2; -.
DR   BioCyc; TTER525904:G1GGS-198-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01577; IPMI_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033940; IPMI_Swivel.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   TIGRFAMs; TIGR00171; leuD; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDW1.
DR   SWISS-2DPAGE; D1CDW1.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01031,
KW   ECO:0000256|SAAS:SAAS00682409};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01031, ECO:0000256|SAAS:SAAS00682405};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01031,
KW   ECO:0000256|SAAS:SAAS00682406};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01031, ECO:0000256|SAAS:SAAS00710129,
KW   ECO:0000313|EMBL:ACZ41117.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN        1    117       Aconitase_C. {ECO:0000259|Pfam:PF00694}.
SQ   SEQUENCE   197 AA;  22212 MW;  58EC55AE55CCD0A0 CRC64;
     MKAINKVEGI VAPLDRPNID TDQIMPKQFL KRIERTGFGP FTFYDWRKEP DFILNRPEYQ
     NAKILATGPN FGCGSSREHA PWGLQDMGFD VIIAPSFADI FRNNCTKIGL LCVELPEDQV
     REIIKLALDN PGITGKVDME AQTVEVGTLR ANFNIDPFVK HRLLNGLDDI GLTLQHVADI
     DAYEARRPEF KPVTILS
//

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