(data stored in ACNUC29543 zone)

SWISSPROT: LEUC_ACIBT

ID   LEUC_ACIBT              Reviewed;         472 AA.
AC   A3M1S8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   16-JAN-2019, entry version 82.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
DE            Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
GN   Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026};
GN   OrderedLocusNames=A1S_0417;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000255|HAMAP-Rule:MF_01026}.
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:0000255|HAMAP-Rule:MF_01026};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01026}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC       Rule:MF_01026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC       type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
DR   EMBL; CP000521; ABO10872.2; -; Genomic_DNA.
DR   SMR; A3M1S8; -.
DR   EnsemblBacteria; ABO10872; ABO10872; A1S_0417.
DR   KEGG; acb:A1S_0417; -.
DR   HOGENOM; HOG000226972; -.
DR   KO; K01703; -.
DR   UniPathway; UPA00048; UER00071.
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; A3M1S8.
DR   SWISS-2DPAGE; A3M1S8.
KW   4Fe-4S; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Iron; Iron-sulfur;
KW   Leucine biosynthesis; Lyase; Metal-binding.
FT   CHAIN         1    472       3-isopropylmalate dehydratase large
FT                                subunit.
FT                                /FTId=PRO_1000063517.
FT   METAL       353    353       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       414    414       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       417    417       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
SQ   SEQUENCE   472 AA;  51016 MW;  983E8EEA7A98E38E CRC64;
     MAGKTLYDKL WDDHVVTQRD DGSCLLYIDR HLLHEVTSPQ AFEGLQLAGR QPWRLSANVA
     TPDHNVPTSK KERDQGIAGI EDDTSRIQVQ TLDDNCKAFN IVEFGINDIR QGIVHVVGPE
     QGLTLPGMTV VCGDSHTATH GAFGCLAHGI GTSEVEHVLA TQCLVQKKSK NMLVRVDGVL
     GKGVTPKDVV LAIIGKIGTA GGTGYAIEFG GQVFRDMSIE GRMTVCNMAI EAGARVGMVA
     VDEKTIEYVK GRSYAPKGEQ WDQAVAYWNT LHSDDDAVFD AVVELNGTEI EPQVSWGTSP
     EMVIPVSKAV PTLEQAKDDV QRNDWTRAYQ YMGLNAGQAL ADIQLDRVFI GSCTNSRIED
     IRAAAEVVKG RKVAPSIKQA MIVPGSGLVK QQAEKEGLDK IFLEAGFEWR EPGCSMCLAM
     NADKLQPGEH CASTSNRNFE GRQGNGGRTH LVSPAMAAAA AIAGHFVDVR SF
//

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