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Database: UniProt
Entry: A0A172WE66_BUCSC
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ID   A0A172WE66_BUCSC        Unreviewed;       465 AA.
AC   A0A172WE66;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 35.
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=XW81_02545 {ECO:0000313|EMBL:ANF17251.1};
OS   Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118110 {ECO:0000313|EMBL:ANF17251.1, ECO:0000313|Proteomes:UP000077654};
RN   [1] {ECO:0000313|EMBL:ANF17251.1, ECO:0000313|Proteomes:UP000077654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC {ECO:0000313|EMBL:ANF17251.1,
RC   ECO:0000313|Proteomes:UP000077654};
RA   Zhang Y.;
RT   "Buchnera aphidicola assembly.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|ARBA:ARBA00002695, ECO:0000256|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:0000256|ARBA:ARBA00000491,
CC         ECO:0000256|HAMAP-Rule:MF_01026};
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-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|ARBA:ARBA00004729,
CC       ECO:0000256|HAMAP-Rule:MF_01026}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01026}.
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DR   EMBL; CP011299; ANF17251.1; -; Genomic_DNA.
DR   RefSeq; WP_075474377.1; NZ_CP011299.1.
DR   AlphaFoldDB; A0A172WE66; -.
DR   STRING; 118110.XW81_02545; -.
DR   PATRIC; fig|118110.3.peg.504; -.
DR   OMA; CNMSIEM; -.
DR   OrthoDB; 9802769at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000077654; Chromosome.
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:0016853; F:isomerase activity; 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; Aconitase, domain 3; 2.
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   NCBIfam; TIGR00170; leuC; 1.
DR   PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01026};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01026};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01026}; Isomerase {ECO:0000313|EMBL:ANF17251.1};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01026};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01026}; Reference proteome {ECO:0000313|Proteomes:UP000077654}.
FT   DOMAIN          8..457
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   BINDING         347
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   BINDING         407
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   BINDING         410
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   465 AA;  51807 MW;  40C0B10B3FCD8E3A CRC64;
     MKKTLYQKLY DAHIVCEEKD HLPILYIDLH LIHEVTSPQA FCEMRSKNRF VRQPNKTFAV
     MDHNVPTISR NLELSTVIAK KQMNELIKNC EEFNIKLFDL SNPNQGIVHV VGPEQGMILP
     GMTIVCGDSH TSTHGAFGTL SFGIGTSEVE HVLSTQTLKQ DRFKSMKIEL NGNINYGTTA
     KDIILFIIRR LGISCGSGYV IEFSGSLIPH LSMESRMTIC NMVIEMGAKS GIIAPDKVTV
     EYLKNRTYVP KGKDWNCALL YWNTLKSDLG ANFDKKVVLD ISSVSPQVTW GTNPSQTISI
     DEKIPELLSY YDVIERNSAE QSLQYMGLEP GMYLTDVSID KVFIGSCTNS RIEDLRDVAN
     IVKHKCISDT VHAIIVPGSG TVKRQAEEEG LDKIFVNAGF EWRHSGCSMC LAMNGDCLKS
     KERCASTSNR NFEGRQGRGG RTHLVSPIMA AAAALFGHFV DVRKL
//
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