LEUD_DECAR
ID LEUD_DECAR Reviewed; 212 AA.
AC Q47HR2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000255|HAMAP-Rule:MF_01031};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01031};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01031};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01031};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01031};
GN Name=leuD {ECO:0000255|HAMAP-Rule:MF_01031}; OrderedLocusNames=Daro_0863;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000255|HAMAP-Rule:MF_01031}.
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_01031};
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_01031}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01031}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01031}.
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DR EMBL; CP000089; AAZ45619.1; -; Genomic_DNA.
DR RefSeq; WP_011286628.1; NC_007298.1.
DR AlphaFoldDB; Q47HR2; -.
DR SMR; Q47HR2; -.
DR STRING; 159087.Daro_0863; -.
DR EnsemblBacteria; AAZ45619; AAZ45619; Daro_0863.
DR KEGG; dar:Daro_0863; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_0_3_4; -.
DR OMA; AFTTHTG; -.
DR OrthoDB; 1384217at2; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR HAMAP; MF_01031; LeuD_type1; 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 Pfam; PF00694; Aconitase_C; 1.
DR TIGRFAMs; TIGR00171; leuD; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Lyase.
FT CHAIN 1..212
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_0000141817"
SQ SEQUENCE 212 AA; 23881 MW; 14867E45F541756A CRC64;
MDKFVRLEGL VAPLDRSNVD TDAIIPKQFL KSIKRSGFGP NAFDEWRYMD VGQPGQDNTG
RPKNPNFVLN QPRYQGAEVL LTRANFGCGS SREHAPWALL DFGFKAIIAE SFADIFFNNC
FKNGILPIVL PAAEIEALFQ QVEATPGYKL VVDLSAQAVV RPDGHGIPFQ IDAFRKECLL
NGWDDIGLTL RHAEKIREFE AKRRVDQPWL FS
