ID   A0A2B6BVU8_BACAN        Unreviewed;       464 AA.
AC   A0A2B6BVU8;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   02-JUN-2021, entry version 4.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
GN   Name=leuC {ECO:0000256|HAMAP-Rule:MF_01026,
GN   ECO:0000313|EMBL:PGB49475.1};
GN   ORFNames=BASH2_04439 {ECO:0000313|EMBL:BAR77846.1}, COL95_25770
GN   {ECO:0000313|EMBL:PGB49475.1};
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392 {ECO:0000313|EMBL:PGB49475.1, ECO:0000313|Proteomes:UP000224851};
RN   [1] {ECO:0000313|EMBL:BAR77846.1, ECO:0000313|Proteomes:UP000217643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shikan-NIID {ECO:0000313|EMBL:BAR77846.1,
RC   ECO:0000313|Proteomes:UP000217643};
RA   Okutani A., Morikawa S., Inoue S.;
RT   "Bacillus anthracis whole genome sequence.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PGB49475.1, ECO:0000313|Proteomes:UP000224851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS072084 {ECO:0000313|EMBL:PGB49475.1,
RC   ECO:0000313|Proteomes:UP000224851};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|ARBA:ARBA00002695, ECO:0000256|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:0000256|ARBA:ARBA00000491,
CC         ECO:0000256|HAMAP-Rule:MF_01026};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01026};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00004729,
CC       ECO:0000256|HAMAP-Rule:MF_01026}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01026}.
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DR   EMBL; AP014833; BAR77846.1; -; Genomic_DNA.
DR   EMBL; NVHS01000074; PGB49475.1; -; Genomic_DNA.
DR   RefSeq; WP_000520131.1; NZ_WXXJ01000017.1.
DR   GeneID; 45021401; -.
DR   KEGG; banh:HYU01_07210; -.
DR   PATRIC; fig|1392.230.peg.1380; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000217643; Chromosome.
DR   Proteomes; UP000224851; Unassembled WGS sequence.
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:0009082; P:branched-chain amino acid biosynthetic process; 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; -; 1.
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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01026};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01026};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01026};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01026};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01026}.
FT   DOMAIN          7..447
FT                   /note="Aconitase"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   METAL           337
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   METAL           397
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   METAL           400
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   464 AA;  51517 MW;  40BB8BF064B62EC9 CRC64;
     MGKRLLDKLW ERHVVTTNEN GLDLLYIDLH LVHEVTSPQA FEGLRLTNRT VRRPDLTFAT
     MDHNIPTKDV WNITDRIAKQ QLDTLRENCK QFQVPLADIG DEEQGIVHVI GPELGLTQPG
     KTIVCGDSHT ATHGAFGALA FGIGTSEVEH VLATQTLWQR KPKAMGIELK GKLQKGVYAK
     DIILHLLSKY GVAVGTGYVM EFYGETIGTM EMEERMTLCN MAIEGGAKAG IIAPDEKTFA
     YVKGRKYAPR DYETFEKKWF ELYTDADAIY DLHISIDVTD LAPYVTWGTN PSMGVRIDEK
     LPEKHDVNDE RAFSYMGLIP GQSTYDIPVQ HVFIGSCTNS RLSDLEIAAS VVKGRKVKEG
     VRALVVPGSK RVRDAAMQKG LHHIFEEAGF EWREPGCSMC LGMNPDQVPE GEHCASTSNR
     NFEGRQGKGA RTHLVSPAMA AAAALYGHFV DIRKESYDGA ISYS
//