ID   LEUD2_MANSM             Reviewed;         200 AA.
AC   Q65V08;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit 2 {ECO:0000255|HAMAP-Rule:MF_01031};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01031};
DE   AltName: Full=Alpha-IPM isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01031};
DE            Short=IPMI 2 {ECO:0000255|HAMAP-Rule:MF_01031};
DE   AltName: Full=Isopropylmalate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01031};
GN   Name=leuD2 {ECO:0000255|HAMAP-Rule:MF_01031}; OrderedLocusNames=MS0595;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(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_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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU37202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016827; AAU37202.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011199774.1; NC_006300.1.
DR   AlphaFoldDB; Q65V08; -.
DR   SMR; Q65V08; -.
DR   STRING; 221988.MS0595; -.
DR   EnsemblBacteria; AAU37202; AAU37202; MS0595.
DR   KEGG; msu:MS0595; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_0_3_6; -.
DR   OrthoDB; 1384217at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000607; 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..200
FT                   /note="3-isopropylmalate dehydratase small subunit 2"
FT                   /id="PRO_0000141834"
SQ   SEQUENCE   200 AA;  22667 MW;  115675590F782CAE CRC64;
     MAGLKQHSGL VVPLDAANVD TDAIIPKQFL QAITRVGFGK HLFHEWRYLD AEETQPNPEF
     VLNFPQYQGA SILLARKNLG CGSSREHAPW ALADYGFKVM IAPSFADIFY NNSLNNHMLP
     IKLSEQEVEE IFQWVWANPG KKIDVDLEAK TVTVGEKVYH FDLDEFRRHC LLEGLDNIGL
     TLQHEDAIAA YESKIPAFLR