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LEUD_SULMW
ID   LEUD_SULMW              Reviewed;         195 AA.
AC   A8Z5R9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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}; OrderedLocusNames=SMGWSS_041;
OS   Sulcia muelleri (strain GWSS).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Candidatus Sulcia.
OX   NCBI_TaxID=444179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GWSS;
RX   PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA   McCutcheon J.P., Moran N.A.;
RT   "Parallel genomic evolution and metabolic interdependence in an ancient
RT   symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007).
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; CP000770; ABS30470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8Z5R9; -.
DR   SMR; A8Z5R9; -.
DR   STRING; 444179.SMGWSS_041; -.
DR   EnsemblBacteria; ABS30470; ABS30470; SMGWSS_041.
DR   KEGG; smg:SMGWSS_041; -.
DR   HOGENOM; CLU_081378_0_3_10; -.
DR   OMA; FEVNGIN; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000781; 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; Reference proteome.
FT   CHAIN           1..195
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_1000084273"
SQ   SEQUENCE   195 AA;  22985 MW;  3B75AE0983C39D59 CRC64;
     MEKFITLFST AVPLFIDNID TDQIIPARFL KLTTKSDFGK NLFRDWRYDS NGKIKKNFIL
     NKKKYSGNIL ITGKNFGCGS SREHAAWAIR DYGFKVVISN IFADIFKQNA LNNGLLTIEL
     KKDFINLIYK KIFLNPNILF EINLEQQYVK FENNKELFKI DDFKKKCFIN GYDDIELLFS
     IKKKIEIFEK KNIYN
 
 
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