ID A0A1G9EEF3_9CLOT Unreviewed; 420 AA.
AC A0A1G9EEF3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01027};
DE EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01027};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
DE Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01027};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
GN Name=leuC {ECO:0000256|HAMAP-Rule:MF_01027};
GN ORFNames=SAMN05660472_01938 {ECO:0000313|EMBL:SDK74522.1};
OS Natronincola ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Natronincola.
OX NCBI_TaxID=393762 {ECO:0000313|EMBL:SDK74522.1, ECO:0000313|Proteomes:UP000198718};
RN [1] {ECO:0000313|EMBL:SDK74522.1, ECO:0000313|Proteomes:UP000198718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18346 {ECO:0000313|EMBL:SDK74522.1,
RC ECO:0000313|Proteomes:UP000198718};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|HAMAP-Rule:MF_01027}.
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|HAMAP-Rule:MF_01027};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01027};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01027};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC Rule:MF_01027}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC Rule:MF_01027}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01027}.
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DR EMBL; FNFP01000003; SDK74522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9EEF3; -.
DR STRING; 393762.SAMN05660472_01938; -.
DR OrthoDB; 9802769at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000198718; 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:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR HAMAP; MF_01027; LeuC_type2; 1.
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; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
DR NCBIfam; TIGR01343; hacA_fam; 1.
DR NCBIfam; TIGR02086; IPMI_arch; 1.
DR NCBIfam; TIGR02083; LEU2; 1.
DR PANTHER; PTHR43822:SF2; 3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 2.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01027};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01027};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01027}; Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01027};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01027}; Reference proteome {ECO:0000313|Proteomes:UP000198718}.
FT DOMAIN 8..284
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 288..411
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 300
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 360
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 363
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
SQ SEQUENCE 420 AA; 45171 MW; 591EE50A91C60278 CRC64;
MGMTMTQKIL AAHAGLDTVK AGQLIEANLD LVLGNDITTP VAVKEFTRIG VKEVFDKSKV
AIVPDHFTPN KDIKTAEQCK MIREFAHEKE VENYFEIGEM GIEHGLIPEK GLVVPGDVAI
GADSHTCTYG ALGAFSTGIG STDMAAGMAT GKCWFKVPSA LKFVLKGKPS KWVSGKDIIL
HIIGMIGVDG ALYKSMEFVG EGVKNLSMDD RFSMANMAIE AGGKNGIFMV DDKTLEYVKQ
HSSKEYTIYT ADEDAVYDET YEIDLATIRP TVAFPHLPDN TRSIDVVGDV KIDQVVIGSC
TNGRIEDLRV AAEILKDKKV AKGVRVIVFP VTQKVYLQAL QEGLIETFIK ANVVVSTPTC
GPCLGGHMGI LAKGERAIAT TNRNFVGRMG HPESEVYLAS PAVAAASALT GKITNPEDVA
//
