ID   LEUD_DESVH              Reviewed;         167 AA.
AC   Q726X3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=DVU_2983;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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   -!- INTERACTION:
CC       Q726X3; Q726X4: leuC; NbExp=3; IntAct=EBI-10066099, EBI-10066095;
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01032}.
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DR   EMBL; AE017285; AAS97454.1; -; Genomic_DNA.
DR   RefSeq; WP_010940242.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_012194.1; NC_002937.3.
DR   AlphaFoldDB; Q726X3; -.
DR   SMR; Q726X3; -.
DR   IntAct; Q726X3; 1.
DR   STRING; 882.DVU_2983; -.
DR   PaxDb; Q726X3; -.
DR   EnsemblBacteria; AAS97454; AAS97454; DVU_2983.
DR   KEGG; dvu:DVU_2983; -.
DR   PATRIC; fig|882.5.peg.2700; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_1_1_7; -.
DR   OMA; GLPIIEC; -.
DR   PhylomeDB; Q726X3; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000002194; 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; IPR011827; LeuD_type2/HacB/DmdB.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   TIGRFAMs; TIGR02087; LEUD_arch; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..167
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_1000072966"
SQ   SEQUENCE   167 AA;  17810 MW;  9FB5C0AB7B42779E CRC64;
     MRYAGTAHKV GDHIDTDAII PARFLVTTDA QKLGENCMEG LEHGWVARVK SGDIMVGGRN
     FGCGSSREHA PIAILGAGMP VVVAHSFARI FYRNGFNMGL LLLEVGDDVD KIADGDDIEV
     DAASGVITNR TTGATITCAP VPQSMRELLD TGGLVPYVRA RLERENG