LEUC_BUCAP
ID LEUC_BUCAP Reviewed; 469 AA.
AC O85065;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
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}; OrderedLocusNames=BUsg_PL6;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OG Plasmid pLeu-Sg (pBSg1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=9873079; DOI=10.1007/pl00006447;
RA Baumann L., Baumann P., Moran N.A., Sandstroem J.P., Thao M.L.;
RT "Genetic characterization of plasmids containing genes encoding enzymes of
RT leucine biosynthesis in endosymbionts (Buchnera) of aphids.";
RL J. Mol. Evol. 48:77-85(1999).
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; AF041836; AAD12595.1; -; Genomic_DNA.
DR RefSeq; NP_047182.1; NC_001910.1.
DR AlphaFoldDB; O85065; -.
DR SMR; O85065; -.
DR OMA; CNMSIEM; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000416; Plasmid pLeu-Sg.
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; -; 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..469
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076721"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 407
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ SEQUENCE 469 AA; 52426 MW; 4094EC232646228B CRC64;
MKKTLYEKIY DAHIVHEEKN NISILYIDLH LLHEVTSPQA FDSLRMRNRS VRQPKKTFAT
MDHNVSTESK DINASGSMAK IQMQQLIKNC EEFNIALYDL NNPKQGIVHV IGPEQGLTLP
GSTIVCGDSH TSTHGAFGAL SFGIGTSEVE HVLVTQTLKQ QRFKNMKIKI VGKVKKFITA
KDIILFIIGK LGTSSGSGYV IEFCGDVIKK MNMEERMTIC NMAIEMGAKS ALIAPDETTY
LYLKNKRYSP KNKYWDSAIR YWKTLVTDEN ALFDKEFTFD ISDISPQVTW GTSPDQVLSI
NEKIPDFNSF KDSIKKDLAR SACNYMDLKP GSYLKNIKID KVFIGSCTNS RIEDLRSAAT
ILKNKKISKN IKAIVVPGSG SVKNQAEKEG LDKIFIDAGF EWRLPGCSMC LGMNNDKLSD
GERCASTSNR NFEGRQGRGG RTHLVSPIMA AAAIYGHFVD VRNLNSETN
