LEUC_BUCUM
ID LEUC_BUCUM Reviewed; 444 AA.
AC Q9EVG8; Q99Q73; Q99QQ9; Q9AJ47; Q9AJ48; Q9AJ49; Q9AJ50; Q9AJ52;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 97.
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};
DE Flags: Fragment;
GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026};
OS Buchnera aphidicola subsp. Uroleucon ambrosiae.
OG Plasmid pLeu (pBAp1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118117;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11133977; DOI=10.1128/jb.183.2.785-790.2001;
RA Wernegreen J.J., Moran N.A.;
RT "Vertical transmission of biosynthetic plasmids in aphid endosymbionts
RT (Buchnera).";
RL J. Bacteriol. 183:785-790(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-436.
RC STRAIN=AL.012, AZ.026, AZ.180, DC.005, GA.039, GA2181, IL.014, IL2.17,
RC IN.018, KY.172, KY2.37, LA.013, MI.035, MN.001, MNb027, MS.040, NY.016,
RC OH.036, TN.173, TN2.38, UT.002, and VA.015;
RX PubMed=11156972; DOI=10.1093/genetics/157.2.477;
RA Funk D.J., Wernegreen J.J., Moran N.A.;
RT "Intraspecific variation in symbiont genomes: bottlenecks and the aphid-
RT Buchnera association.";
RL Genetics 157:477-489(2001).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC 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-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC 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 type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
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DR EMBL; AF197454; AAG31397.1; -; Genomic_DNA.
DR EMBL; AF196404; AAK21726.1; -; Genomic_DNA.
DR EMBL; AF196407; AAK21731.1; -; Genomic_DNA.
DR EMBL; AF196408; AAK21733.1; -; Genomic_DNA.
DR EMBL; AF196409; AAK21735.1; -; Genomic_DNA.
DR EMBL; AF196410; AAK21737.1; -; Genomic_DNA.
DR EMBL; AF196412; AAK21741.1; -; Genomic_DNA.
DR EMBL; AF196413; AAK21743.1; -; Genomic_DNA.
DR EMBL; AF196414; AAK21745.1; -; Genomic_DNA.
DR EMBL; AF196415; AAK21747.1; -; Genomic_DNA.
DR EMBL; AF196417; AAK21751.1; -; Genomic_DNA.
DR EMBL; AF196418; AAK21753.1; -; Genomic_DNA.
DR EMBL; AF196419; AAK21755.1; -; Genomic_DNA.
DR EMBL; AF196420; AAK21757.1; -; Genomic_DNA.
DR EMBL; AF196421; AAK21759.1; -; Genomic_DNA.
DR EMBL; AF196422; AAK21761.1; -; Genomic_DNA.
DR EMBL; AF196423; AAK21763.1; -; Genomic_DNA.
DR EMBL; AF196424; AAK21765.1; -; Genomic_DNA.
DR EMBL; AF196402; AAK21723.1; -; Genomic_DNA.
DR EMBL; AF196406; AAK21729.1; -; Genomic_DNA.
DR EMBL; AF196416; AAK21749.1; -; Genomic_DNA.
DR EMBL; AF196425; AAK21767.1; -; Genomic_DNA.
DR EMBL; AF196411; AAK21739.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EVG8; -.
DR SMR; Q9EVG8; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; -; 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 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;
KW 4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding; Plasmid.
FT CHAIN 1..>444
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076724"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 408
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 411
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT VARIANT 22..23
FT /note="GE -> RG (in strain: GA2181)"
FT VARIANT 47
FT /note="S -> N (in strain: MNb027)"
FT VARIANT 254
FT /note="L -> F (in strain: UT.002)"
FT VARIANT 312
FT /note="N -> K (in strain: OH.036)"
FT VARIANT 315
FT /note="L -> V (in strain: GA2181, MNb027, OH.036 and
FT UT.002)"
FT VARIANT 339
FT /note="S -> A (in strain: UT.002)"
FT CONFLICT 428
FT /note="T -> H (in Ref. 1; AAG31397)"
FT /evidence="ECO:0000305"
FT NON_TER 444
SQ SEQUENCE 444 AA; 49593 MW; CEA7649DEAEB38EA CRC64;
MTSKTLYQKI YDSHVVYEDK NGESILYIDL HLLHEVTSPQ AFDALRSKKR KVRQSKKTFA
TMDHNVSTKI QSISASGSMA KKQMEQLIKN CRDFNIPLYD INNPNQGIVH VIAPEKGMTL
PGMTIVCGDS HTSTHGAFGA LAFGIGTSEV EHVLATQTLK QKRFKNMKVE IIGKIPKFVT
AKDIILFIIG QLGSSSGTGY VIEFCGDVIK NISMEERMTI CNMAIEMGAK SGLIAPDEIT
YKYLKDKIYS PSGLFWEKSL DYWKFLKSDK NAHFDKCITL DISNLAPQIT WGTNPDQVIS
IDEKIPDYNN INSLLKKESA KSACEYMGLK SNTYLTNISI DRVFIGSCTN ARIEDLRAAS
KILKNRKIAK HVKAIVVPGS GSVKRKAEQE GLDKIFIDSG FEWRLPGCSM CLGMNKDRLN
FGERCASTSN RNFEGRQGRG GRTH
