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LEUD_ALIB4
ID   LEUD_ALIB4              Reviewed;         166 AA.
AC   A8ETJ8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Abu_1012;
OS   Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Aliarcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018;
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA   Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the Epsilonproteobacterium
RT   Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(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_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; CP000361; ABV67272.1; -; Genomic_DNA.
DR   RefSeq; WP_004509201.1; NC_009850.1.
DR   AlphaFoldDB; A8ETJ8; -.
DR   SMR; A8ETJ8; -.
DR   STRING; 367737.Abu_1012; -.
DR   EnsemblBacteria; ABV67272; ABV67272; Abu_1012.
DR   GeneID; 56463259; -.
DR   KEGG; abu:Abu_1012; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_1_1_7; -.
DR   OMA; DDVNTDY; -.
DR   OrthoDB; 1384217at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001136; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..166
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_1000072962"
SQ   SEQUENCE   166 AA;  18223 MW;  D21F919D4E36128D CRC64;
     MNTITGKVWN FGANIDTDVI IAARYLNSSD PEHLAKYVME DADPEFPKKL KKGDIIVAGE
     NFGCGSSREH APIALKAAGI AAVVAPSFAR IFYRNAFNMG LPIFELPESL EIKEGEEISI
     NLDKGEITNN TTKKTYKFIP IPPFMQELIA TGGLINYAKA EMKKAI
 
 
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