(data stored in SCRATCH zone)

SWISSPROT: Q13S33_PARXL

ID   Q13S33_PARXL            Unreviewed;       469 AA.
AC   Q13S33;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 104.
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   ORFNames=Bxe_B2889 {ECO:0000313|EMBL:ABE33106.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33106.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33106.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33106.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., 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_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}.
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DR   EMBL; CP000271; ABE33106.1; -; Genomic_DNA.
DR   RefSeq; WP_011490489.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2889; -.
DR   EnsemblBacteria; ABE33106; ABE33106; Bxe_B2889.
DR   GeneID; 4006746; -.
DR   KEGG; bxb:DR64_5219; -.
DR   KEGG; bxe:Bxe_B2889; -.
DR   PATRIC; fig|266265.5.peg.4799; -.
DR   eggNOG; ENOG4105CQI; Bacteria.
DR   eggNOG; COG0065; LUCA.
DR   HOGENOM; HOG000226972; -.
DR   KO; K01703; -.
DR   OMA; FDHQVPA; -.
DR   OrthoDB; 749418at2; -.
DR   BioCyc; BXEN266265:BXE_RS22750-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001817; Chromosome 2.
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; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13S33.
DR   SWISS-2DPAGE; Q13S33.
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:UP000001817};
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:ABE33106.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS01079498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        7    460       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   METAL       347    347       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       410    410       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       413    413       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
SQ   SEQUENCE   469 AA;  50776 MW;  A19B3C63C6E41802 CRC64;
     MAQTLYDKLW NTHVVHTEED GTTILYIDRH LLHEVTSPQA FEGLKLAERP VWRISANLAV
     SDHNVPTTDR SHGIADPISR LQVDTLDSNC DAYGITQFKM NDLRQGIVHI IGPEQGATLP
     GMTIVCGDSH TSTHGAFGAL AHGIGTSEVE HVLATQTLLQ KKSKNMLVKV EGALPRGCTA
     KDIVLAIIGK IGTAGGTGYA IEFGGSTIRA LSMEGRMTVC NMAIEAGARA GMVAVDDTTI
     EYLKGRPFSP EGVEWNHAVE YWKQFKSDDG AQFDRVVELN AAEIVPQVTW GTSPEMVTAV
     DGRVPDPDRE KDPVKRDALE RALKYMALEP NAPIESIKPD KIFIGSCTNA RIEDIRAAAY
     VVKKLGRRVA PNIRLAMVVP GSGLVKAQAE REGLDKVFTD AGFEWREPGC SMCLAMNADR
     LEPGERCAST SNRNFEGRQG AGGRTHLVSP AMAAAAAIEG HFVDIRKLG
//

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