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Entry: A0A1A9RWJ3_9NEIS
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ID   A0A1A9RWJ3_9NEIS        Unreviewed;       469 AA.
AC   A0A1A9RWJ3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=A7P95_08470 {ECO:0000313|EMBL:OAM26781.1};
OS   Eikenella longinqua.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Eikenella.
OX   NCBI_TaxID=1795827 {ECO:0000313|EMBL:OAM26781.1, ECO:0000313|Proteomes:UP000077885};
RN   [1] {ECO:0000313|Proteomes:UP000077885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML02-A-017 {ECO:0000313|Proteomes:UP000077885};
RA   Bernier A.-M., Bernard K.;
RT   "Draft genome of Corynebacterium afermentans subsp. afermentans LCDC
RT   88199T.";
RL   Submitted (MAY-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|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|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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAM26781.1}.
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DR   EMBL; LXSL01000028; OAM26781.1; -; Genomic_DNA.
DR   RefSeq; WP_067593955.1; NZ_LXSL01000028.1.
DR   AlphaFoldDB; A0A1A9RWJ3; -.
DR   STRING; 1795827.A7P95_08470; -.
DR   OrthoDB; 9802769at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000077885; 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_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   NCBIfam; TIGR00170; leuC; 1.
DR   PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 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          8..460
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   BINDING         349
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   BINDING         410
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   BINDING         413
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   469 AA;  50495 MW;  1CCCF61FF870C99F CRC64;
     MSAQTLYDKL WNSHIVHEEE DGTVLLYIDR HLVHEVTSPQ AFEGLKMAGR KLWRIDSVVS
     TADHNTPTDH WDEGIKDPIS KLQVDTLDKN IKEFGALAYF PFMDKGQGIV HVMGPEQGAT
     LPGMTVVCGD SHTSTHGAFG ALAHGIGTSE VEHTMATQCI TAKKSKSMLI EVSGSLKPGV
     TAKDIALYII GQIGTAGGTG YAIEFSGETI RSLSMEGRMT LCNMAIEAGA RSGLVAVDDT
     TINYIQGRPL APKGKDWDKA VAYWRTLVSD QGAKFDKTYT FRAEDIEPQV TWGTSPEMVL
     SVDGKVPNPA DEADAVKRAG MERALEYMGL AAGTPLNEIP VDVVFIGSCT NSRIEDLREA
     AAVVKGRKKA DNVNRVLVVP GSGLVKEQAE KEGLDKIFTD AGFEWREPGC SMCLAMNADR
     LAPKERCAST SNRNFEGRQG NGGRTHLVSP AMAAAAAVAG HFVDGRQLA
//
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