LEUD_ENDTX
ID LEUD_ENDTX Reviewed; 163 AA.
AC B1H0A5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=TGRD_454;
OS Endomicrobium trichonymphae.
OC Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC Endomicrobium.
OX NCBI_TaxID=1408204;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Complete genome of the uncultured termite group 1 bacteria in a single
RT host protist cell.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(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; AP009510; BAG13937.1; -; Genomic_DNA.
DR RefSeq; WP_015423463.1; NC_020419.1.
DR RefSeq; YP_001956398.1; NC_020419.1.
DR AlphaFoldDB; B1H0A5; -.
DR SMR; B1H0A5; -.
DR STRING; 471821.TGRD_454; -.
DR EnsemblBacteria; BAG13937; BAG13937; TGRD_454.
DR KEGG; rsd:TGRD_454; -.
DR PATRIC; fig|471821.5.peg.736; -.
DR HOGENOM; CLU_081378_1_1_0; -.
DR OMA; GLPIIEC; -.
DR OrthoDB; 1384217at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001691; Chromosome.
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_01032; LeuD_type2; 1.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR InterPro; IPR011824; LeuD/DmdB_bac.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR Pfam; PF00694; Aconitase_C; 1.
DR TIGRFAMs; TIGR02084; leud; 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..163
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_1000213374"
SQ SEQUENCE 163 AA; 17838 MW; 4B9DB9C3D04D7646 CRC64;
MSDIILKGKV HKYGSNVNTD EIIPARYLNT TDPTILSKYC MEDIDKNFVK NVKAGDIIVA
ENNFGCGSSR EHAPIAIKAS GISAVIANSF ARIFFRNSIN IGLPILESQK AVKAIENGDA
VEINLTKGII KNITKNESYQ SQPFPEFMQK VIKSGGLLGY IKS