ID A0A1X0N4W5_9PSED Unreviewed; 474 AA.
AC A0A1X0N4W5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=BZK31_14350 {ECO:0000313|EMBL:ORC58596.1};
OS Pseudomonas floridensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1958950 {ECO:0000313|EMBL:ORC58596.1, ECO:0000313|Proteomes:UP000192815};
RN [1] {ECO:0000313|Proteomes:UP000192815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GEV388 {ECO:0000313|Proteomes:UP000192815};
RA Timilsina S., Vallad G.E., Jones J.B.;
RT "Pseudomonas floridae sp. nov., a novel pathogenic bacterial species
RT isolated from tomato.";
RL Submitted (FEB-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|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:ORC58596.1}.
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DR EMBL; MUIO01000054; ORC58596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0N4W5; -.
DR STRING; 1958950.BZK31_14350; -.
DR OrthoDB; 9802769at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000192815; 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..463
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 352
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"
FT BINDING 416
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ SEQUENCE 474 AA; 50933 MW; 5AFA833823EF720B CRC64;
MAGKTLYDKL WDSHLVKQRD DGSALIYIDR HIIHEVTSPQ AFEGLRLAGR KPWRIDSIIA
TPDHNVPTTS ERKGGIGAIE DQVSRLQVQT LDDNCDEYGI TEFKMNDPRQ GIVHVIGPEQ
GATLPGMSVV CGDSHTSTHG AFGALAHGIG TSEVEHVLAT QCLVAKKMKN MLVSVEGQLP
FGVTAKDIVL AVIGKIGTAG GNGYAIEFAG SAIRDLSIEG RMTICNMSIE AGARVGMVAT
DEKTVEYVKG RPFAPKGAEW DMAVEAWKDL VSDPDAVFDT VVRLDAAQIK PQVSWGTSPE
MVLAVDQNVP DPAQETDLVK RGSIERALKY MGLKANQPIT DIQLDRVFIG SCTNSRIEDL
RAAADVAKGR KVAATIKQAI VVPGSGLIKA QAEQEGLDKI FIEAGFEWRE PGCSMCLAMN
PDRLGSGEHC ASTSNRNFEG RQGAGGRTHL VSPAMAAAAA VNGRFIDVRD LIQH
//
