LEUC_BORPA
ID LEUC_BORPA Reviewed; 467 AA.
AC Q7W931;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=BPP1942;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE37242.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX640428; CAE37242.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_033446523.1; NC_002928.3.
DR AlphaFoldDB; Q7W931; -.
DR SMR; Q7W931; -.
DR EnsemblBacteria; CAE37242; CAE37242; BPP1942.
DR GeneID; 56478304; -.
DR GeneID; 66438381; -.
DR KEGG; bpa:BPP1942; -.
DR HOGENOM; CLU_006714_3_4_4; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001421; 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.
FT CHAIN 1..467
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076709"
FT BINDING 347
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"
SQ SEQUENCE 467 AA; 50586 MW; EA295C09C3215FA8 CRC64;
MAQTLYDKLW DAHVVHQESD GTCLLYIDRH LLHEVTSPQA FEGLALAGRQ PWRVGANLAV
ADHNVPTLNR AQGIEDPISR LQVDTLDDNC AKYGITEFRM NDLRQGIVHV IGPEQGATLP
GMTVVCGDSH TSTHGALGAL AFGIGTSEVE HVLATQTLLM KKAKSMQINV EGELPFGCTA
KDVVLHIIGI IGTAGGTGHA IEFSGSTIRG LSVEGRMTVC NMAIEAGARS GMVAVDDKTI
DYFRGRPFAP VGVLWDQAVG YWRTLHSDAG ARFDRVINVD ARDIKPQVTW GTSPEMVLPV
DGRVPDPDRE KDDVRRSGME RALEYMGLKP NTPLVDIRVD RVFIGSCTNS RIEDLRAAAV
VARGKRVAAN VRQAMVVPGS GLVKQQAERE GLDKIFIEAG FEWREPGCSM CLAMNADRLE
PGERCASTSN RNFEGRQGQG GRTHLVSPAM AAAAAVAGHF VDVRSFR
