ID A0A1F3LX86_9BACT Unreviewed; 192 AA.
AC A0A1F3LX86;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00011998};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998};
GN ORFNames=A2X18_13850 {ECO:0000313|EMBL:OFY45018.1};
OS Bacteroidetes bacterium GWF2_40_14.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797347 {ECO:0000313|EMBL:OFY45018.1, ECO:0000313|Proteomes:UP000176561};
RN [1] {ECO:0000313|EMBL:OFY45018.1, ECO:0000313|Proteomes:UP000176561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004729}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|ARBA:ARBA00011271}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009845}.
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:OFY45018.1}.
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DR EMBL; MEOK01000001; OFY45018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3LX86; -.
DR STRING; 1797347.A2X18_13850; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000176561; Unassembled WGS sequence.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR NCBIfam; TIGR00171; leuD; 1.
DR PANTHER; PTHR43345:SF5; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT; 1.
DR PANTHER; PTHR43345; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 2-RELATED-RELATED; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 6..124
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 192 AA; 21810 MW; 6AB933E93CBB07F2 CRC64;
MSFSKFTILE SKPVLMPAEN IDTDQIIPAR FLKTTTRKGF GENLFHDWMY SKNGEKNPEF
ILNKENGKGK ILVAGRNFGC GSSREHAAWA IYDHGFRAVV SSFFADIFRN NALNNGLLPV
QVSPEFLQKI FETGESSLVV NLPEKTIKIS STGDCEYFEI NTYKQDCLIN GYDDIDFLLS
NKDAIEKFEQ NR
//
