LEUC_BUCAI
ID LEUC_BUCAI Reviewed; 471 AA.
AC P56934; Q9EVF9; Q9KGP8; Q9R6R3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=BUpL06;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OG Plasmid pLeu (pBAp1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10688696; DOI=10.1007/s002849910052;
RA Soler T., Latorre A., Sabater B., Silva F.J.;
RT "Molecular characterization of the Leucine plasmid from Buchnera
RT aphidicola, primary endosymbiont of the aphid Acyrthosiphon pisum.";
RL Curr. Microbiol. 40:264-268(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-448.
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).
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.
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=BAA95425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ006878; CAB56192.1; -; Genomic_DNA.
DR EMBL; AP001071; BAA95425.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF197457; AAG31406.1; -; Genomic_DNA.
DR RefSeq; NP_057970.1; NC_002253.1.
DR AlphaFoldDB; P56934; -.
DR SMR; P56934; -.
DR EnsemblBacteria; BAA95425; BAA95425; BAA95425.
DR KEGG; buc:BUpL06; -.
DR PATRIC; fig|107806.10.peg.12; -.
DR HOGENOM; CLU_006714_3_4_6; -.
DR OMA; CNMSIEM; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001806; Plasmid pLeu.
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;
KW Reference proteome.
FT CHAIN 1..471
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076715"
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"
FT CONFLICT 36
FT /note="T -> A (in Ref. 3; AAG31406)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="M -> V (in Ref. 1; CAB56192)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="G -> D (in Ref. 1; CAB56192)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="K -> E (in Ref. 1; CAB56192)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="G -> S (in Ref. 1; CAB56192)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="S -> N (in Ref. 1; CAB56192 and 3; AAG31406)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="T -> H (in Ref. 3; AAG31406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 52281 MW; EACEE7197EB89726 CRC64;
MKKTLYDKIY DSHIVYEEKN NTSLLYIDLH LLHEVTSPQA FDSLRDKNRK VRQPKKTFAT
MDHNVSTTSQ DINASGSMAK VQMQELIKNC SEFNISLYDI KNPNQGIVHV ISPEKGMTLP
GMTIVCGDSH TSTHGAFGAL SFGIGTSEVE HVLATQTLKQ QRFKNMKIEI TGEIQKFVTA
KDLILFIIGK LGSSGGAGYI IEFCGNVIEK MSMEERMTIC NMAIEIGAKS GLIAPDEVTF
SYLKNKMYAP RGVFWKKALN FWKNLKSDKN AFFDKVVNIN ISDLSPQITW GTNPDQVISI
DQKIPDFSSF DNLIKKDLAK SACKYMGLKI GTYLTNITVD KVFIGSCTNG RIEDLRAASK
ILKDKKIANN VKAIVVPGSG SVKREAENEG LDKIFISAGF EWRLPGCSMC LGMNKDRLND
GERCASTSNR NFEGRQGRGG RTHLVSPIMA AAAAVYGKFV DVRKLYNGEN N
