ID A0A257GWH8_9BURK Unreviewed; 480 AA.
AC A0A257GWH8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00011998};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998};
DE Flags: Fragment;
GN Name=leuC {ECO:0000313|EMBL:OYU42728.1};
GN ORFNames=CFE44_22375 {ECO:0000313|EMBL:OYU42728.1};
OS Burkholderiales bacterium PBB4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=2015566 {ECO:0000313|EMBL:OYU42728.1, ECO:0000313|Proteomes:UP000216392};
RN [1] {ECO:0000313|EMBL:OYU42728.1, ECO:0000313|Proteomes:UP000216392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBB4 {ECO:0000313|EMBL:OYU42728.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-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}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004729}.
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:OYU42728.1}.
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DR EMBL; NKIJ01000942; OYU42728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257GWH8; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000216392; Unassembled WGS sequence.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
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-UniPathway.
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};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000216392}.
FT DOMAIN 5..471
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OYU42728.1"
SQ SEQUENCE 480 AA; 51258 MW; 499C3618E3ACBB13 CRC64;
RTLYDKLWDD HVVHTEEDGT SILYIDRHLV HEVTSPQAFE GLRVAGRKVW RVSSIVATAD
HNTPTTGWEL GYDGITDPTS KEQVTTLDAN IQEFGSAAFF PFLSKRQGIV HVIGPENGAT
LPGMTVVCGD SHTSTHGAFG ALAHGIGTSE VEHVMATQTL LAKKAKNMLV KVEGNVAQGI
TAKDIVLAII GKIGTAGGTG YTIEFGGAAI RALSMEGRMT VCNMAIEAGA RAGLVAVDEK
TIEYVKGRPL APGANAASPE AAAVEWDQAV AFWKTLHSDA GAHFDTVVEL NASQIVPQVT
WGTSPEMVLG IDARVPDPDK EKDSNKRGAI ERALTYMGLE PGKALNDLFV DKVFIGSCTN
SRIEDMREAA AVVKHLGQKV AKNIKLAMVV PGSGLVKEQA EREGLHEIFK AAGFEWREPG
CSMCLAMNAD RLEPGERCAS TSNRNFEGRQ GAGGRTHLVS PAMAAAAAIH GHFVDIRKFS
//
