LEUD_HYDS0
ID LEUD_HYDS0 Reviewed; 165 AA.
AC B4U7M0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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};
GN OrderedLocusNames=HY04AAS1_0441;
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC unclassified Hydrogenobaculum.
OX NCBI_TaxID=380749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y04AAS1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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_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; CP001130; ACG57131.1; -; Genomic_DNA.
DR RefSeq; WP_012513487.1; NC_011126.1.
DR AlphaFoldDB; B4U7M0; -.
DR SMR; B4U7M0; -.
DR STRING; 380749.HY04AAS1_0441; -.
DR EnsemblBacteria; ACG57131; ACG57131; HY04AAS1_0441.
DR KEGG; hya:HY04AAS1_0441; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_1_1_0; -.
DR OMA; GLPIIEC; -.
DR OrthoDB; 1384217at2; -.
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 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..165
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_1000135850"
SQ SEQUENCE 165 AA; 18275 MW; 5AB880EB1AD72455 CRC64;
MIIKGKIWKF KDNIDTDQII PARYLNTSDP LELASHVMED SEKPNFAKEH QEGDIIVAGK
NFGSGSSREH APIAIKYAGV PVVVAKSFAR IFFRNAINIG LPIVECKEAV DEAEDGDIFE
IDLENGIVKN VTKNKTYSST KFPEELMAIL RAGGLMEYAK SRLSS