LEUD_BRUA4
ID LEUD_BRUA4 Reviewed; 201 AA.
AC A6X449;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Oant_3297;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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; CP000759; ABS16003.1; -; Genomic_DNA.
DR RefSeq; WP_012092735.1; NC_009668.1.
DR AlphaFoldDB; A6X449; -.
DR SMR; A6X449; -.
DR STRING; 439375.Oant_3297; -.
DR EnsemblBacteria; ABS16003; ABS16003; Oant_3297.
DR KEGG; oan:Oant_3297; -.
DR PATRIC; fig|439375.7.peg.3452; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_0_3_5; -.
DR OMA; AFTTHTG; -.
DR OrthoDB; 1384217at2; -.
DR PhylomeDB; A6X449; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000002301; Chromosome 2.
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..201
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_1000063800"
SQ SEQUENCE 201 AA; 22134 MW; C7B543943B528C2E CRC64;
MDKFTKLTGV AAPLPIVNID TDMIIPKDYL KTIKRTGLSK GLFAEMRFNE DGTENPDFVL
NKPGYRNAQI LVAGDNFGCG SSREHAPWAL LDFGIRCVIS TSFADIFYNN CFKNGILPIK
VAQEDLDKLM DDASRGANAT LTVDLEAKEI HGPDGGSISF DVDDFKRHCL LNGLDDIGLT
MEKAGSIDTF EAKRAELRPW A
