(data stored in ACNUC7421 zone)

SWISSPROT: Q13R19_PARXL

ID   Q13R19_PARXL            Unreviewed;       210 AA.
AC   Q13R19;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 84.
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_B2521 {ECO:0000313|EMBL:ABE33470.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33470.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33470.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33470.1,
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; ABE33470.1; -; Genomic_DNA.
DR   RefSeq; WP_011490838.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13R19; -.
DR   STRING; 266265.Bxe_B2521; -.
DR   EnsemblBacteria; ABE33470; ABE33470; Bxe_B2521.
DR   GeneID; 4006983; -.
DR   KEGG; bxb:DR64_4848; -.
DR   KEGG; bxe:Bxe_B2521; -.
DR   PATRIC; fig|266265.5.peg.5185; -.
DR   eggNOG; ENOG4105MQS; Bacteria.
DR   eggNOG; COG0066; LUCA.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OMA; HAVWALI; -.
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; Q13R19.
DR   SWISS-2DPAGE; Q13R19.
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:ABE33470.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        2    132       Aconitase_C. {ECO:0000259|Pfam:PF00694}.
SQ   SEQUENCE   210 AA;  23463 MW;  E1C5BCB3BF6CCA3D CRC64;
     MEPLVCHEGL VVPLDRDNVD TDAIIPKQFM KSIARTGFGP YLFDEWRYRD PGHYGKPAAE
     RTPEPGFALN QQRYAGASVL LTRRNFGCGS SREHAPWALH QFGFRVLVAE SFADIFFNNC
     CKNGLLPVRL DAALIGRLME TVEAAHGYRL RVDLAAQTLT APDGECWRFD IPPALRTLLL
     EGLDETGATL AFADAIRAFE AVQLERSPWL
//

If you have problems or comments...

PBIL Back to PBIL home page