LEUD_MOOTA
ID LEUD_MOOTA Reviewed; 166 AA.
AC Q2RG99;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000255|HAMAP-Rule:MF_01032};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01032};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01032};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01032};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01032};
GN Name=leuD {ECO:0000255|HAMAP-Rule:MF_01032}; OrderedLocusNames=Moth_2253;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000255|HAMAP-Rule:MF_01032}.
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:0000255|HAMAP-Rule:MF_01032};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_01032}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01032}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01032}.
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DR EMBL; CP000232; ABC20540.1; -; Genomic_DNA.
DR RefSeq; WP_011393736.1; NC_007644.1.
DR RefSeq; YP_431083.1; NC_007644.1.
DR AlphaFoldDB; Q2RG99; -.
DR SMR; Q2RG99; -.
DR STRING; 264732.Moth_2253; -.
DR EnsemblBacteria; ABC20540; ABC20540; Moth_2253.
DR KEGG; mta:Moth_2253; -.
DR PATRIC; fig|264732.11.peg.2452; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_1_1_9; -.
DR OMA; GLPIIEC; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.19.10; -; 1.
DR HAMAP; MF_01032; LeuD_type2; 1.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR Pfam; PF00694; Aconitase_C; 1.
DR TIGRFAMs; TIGR02087; LEUD_arch; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Lyase.
FT CHAIN 1..166
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_1000072969"
SQ SEQUENCE 166 AA; 17516 MW; 2EECE92402410E73 CRC64;
MIIQGKCHTF GNDIDTDAII PARYLNTTDP GELARHCMED ADPTFAGRVQ KGEIIVAGKN
FGCGSSREHA PVAIKAAGVA AVVAASFARI FYRNAINIGL PIFESPEAAA GIKAGDEVKI
DAGKGEIVNL TRGETYPVAP FPPFMQELIA AGGLMPYVAR KVKTSV