(data stored in ACNUC7421 zone)

SWISSPROT: Q13S32_PARXL

ID   Q13S32_PARXL            Unreviewed;       217 AA.
AC   Q13S32;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 90.
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   ORFNames=Bxe_B2888 {ECO:0000313|EMBL:ABE33107.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33107.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33107.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33107.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate. {ECO:0000256|HAMAP-Rule:MF_01031,
CC       ECO:0000256|SAAS:SAAS00682397}.
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000271; ABE33107.1; -; Genomic_DNA.
DR   RefSeq; WP_011490490.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13S32; -.
DR   STRING; 266265.Bxe_B2888; -.
DR   EnsemblBacteria; ABE33107; ABE33107; Bxe_B2888.
DR   GeneID; 4006747; -.
DR   KEGG; bxb:DR64_5217; -.
DR   KEGG; bxe:Bxe_B2888; -.
DR   PATRIC; fig|266265.5.peg.4801; -.
DR   eggNOG; ENOG4105MQS; Bacteria.
DR   eggNOG; COG0066; LUCA.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OMA; AFTTHTG; -.
DR   OrthoDB; POG091H02FJ; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP.
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   SUPFAM; SSF52016; SSF52016; 1.
DR   TIGRFAMs; TIGR00171; leuD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13S32.
DR   SWISS-2DPAGE; Q13S32.
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:UP000001817};
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:ABE33107.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        1    132       Aconitase_C. {ECO:0000259|Pfam:PF00694}.
SQ   SEQUENCE   217 AA;  24665 MW;  3AD8B450B0C45633 CRC64;
     MEKFIVHTGV VAPLDRENVD TDAIIPKQFL KSIKRTGFGP NAFDEWRYLD HGEPGQDNSQ
     RPLNPDFVLN QPRYQGASVL LARKNFGCGS SREHAPWALE QYGFRALIAP SFADIFYNNC
     FKNGVLPIVL TEQQVDHLFN ETYAFNGFKL TVDLEAQVVR TADGGTEYPF EVAAFRKYCL
     LNGFDDIGLT LRHADKIRQF EAERIAKQPW LAHRIVG
//

If you have problems or comments...

PBIL Back to PBIL home page