LEUD_PSEPG
ID LEUD_PSEPG Reviewed; 214 AA.
AC B0KF82;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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};
GN OrderedLocusNames=PputGB1_1517;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
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; CP000926; ABY97422.1; -; Genomic_DNA.
DR RefSeq; WP_012271189.1; NC_010322.1.
DR AlphaFoldDB; B0KF82; -.
DR SMR; B0KF82; -.
DR STRING; 76869.PputGB1_1517; -.
DR EnsemblBacteria; ABY97422; ABY97422; PputGB1_1517.
DR KEGG; ppg:PputGB1_1517; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_0_3_6; -.
DR OMA; AFTTHTG; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000002157; 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; -; 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..214
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_1000084260"
SQ SEQUENCE 214 AA; 24225 MW; 200A415F6BEDB1DB CRC64;
MKAFTQHTGL VAPLDRANVD TDQIIPKQFL KSIKRTGFGP NLFDEWRYLD VGQPYQDNSK
RPVNQEFVLN HARYQGASVL LARENFGCGS SREHAPWALD EYGFRSIIAP SFADIFFNNS
FKNGLLPIIL SDEEVDELFK QVEANPGYQL TIDLQAQAVT RPDGKVLHFE IDAFRKHCLL
NGLDDIGLTL QDSDAIKAFE GKHRAGQPWL FRDA
