LEUC_LACLA
ID LEUC_LACLA Reviewed; 460 AA.
AC Q02142;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
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=LL1220;
GN ORFNames=L0075;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400210; DOI=10.1128/jb.174.20.6580-6589.1992;
RA Godon J.-J., Chopin M.-C., Ehrlich S.D.;
RT "Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp.
RT lactis.";
RL J. Bacteriol. 174:6580-6589(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
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.
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; U92974; AAB81915.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05318.1; -; Genomic_DNA.
DR PIR; D86777; D86777.
DR PIR; S35134; S35134.
DR RefSeq; NP_267376.1; NC_002662.1.
DR RefSeq; WP_003131128.1; NC_002662.1.
DR AlphaFoldDB; Q02142; -.
DR SMR; Q02142; -.
DR STRING; 272623.L0075; -.
DR PaxDb; Q02142; -.
DR EnsemblBacteria; AAK05318; AAK05318; L0075.
DR KEGG; lla:L0075; -.
DR PATRIC; fig|272623.7.peg.1319; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_9; -.
DR OMA; CNMSIEM; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000002196; 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: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;
KW Reference proteome.
FT CHAIN 1..460
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076753"
FT BINDING 339
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 399
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 402
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT CONFLICT 70
FT /note="D -> N (in Ref. 1; AAB81915)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="A -> D (in Ref. 1; AAB81915)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="T -> M (in Ref. 1; AAB81915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50491 MW; 3263EC48A2E9D877 CRC64;
MSGKTIFDKL WDQHVIAGNE GEPQLLYIDL HVIHEVTSPQ AFQGLREAGR RVRRKDLTYG
TLDHNVPTQD IFNIQDLISK KQIDTFTKNV KEFDVPAETH GGKGQGIVHM VAPESGRTQP
GKTIVCGDSH TATNGAFGAI AFGIGTSEVE HVLATQTIWQ VKPKRMKIEF QGHPQKGIYS
KDFILALIAK YGVDAGVGYA VEYSGDAISD LSMEERMTIC NMSIEFGAKI GLMNPDEKTY
DYVKGREHAP KNFDEAVSKW EKLVSDSDAQ YDKILSLDVS QLKPMVTWGT NPGMGLEFGE
KFPEINNDLN YERAYQYMDL KPGQTASAID LGYIFIGSCT NARLGDLEEA AKIIGDRHIA
DGLTGIVVPG SRPVKEAAEA QGLDKIFKEA GFEWREPGCS ACLGMNPDQI PEYVHCASTS
NRNFEGRQGH NARTHLCSPA MAAAAAIAGK FVDVRTLVTD
