ID LEUD_SHEHH Reviewed; 201 AA.
AC B0TQM3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=Shal_0441;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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: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; CP000931; ABZ75016.1; -; Genomic_DNA.
DR RefSeq; WP_012275570.1; NC_010334.1.
DR AlphaFoldDB; B0TQM3; -.
DR SMR; B0TQM3; -.
DR STRING; 458817.Shal_0441; -.
DR KEGG; shl:Shal_0441; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_0_3_6; -.
DR OrthoDB; 9777465at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001317; Chromosome.
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; Aconitase, domain 4; 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 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; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Lyase.
FT CHAIN 1..201
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_1000084266"
SQ SEQUENCE 201 AA; 22037 MW; DAA32EB027FFF69E CRC64;
MQPFISHTGL AVILDSANVD TDQIIPKQFL SKVTRDGFGV HLFHDWRYLD EAGDKPNPDF
NLNQPRYKGA SILVSQENFG CGSSREHAPW ALADFGFKVI IAPSFADIFY GNSINNGLLP
VRLTDAEVKQ LMAEVEAKEG AEIDVDLQAL TVTSPSGALF HFEIAQSARH NLLNGLDAIG
LTLSHVDTIA NYEANIPSWR G
//
