LEUD_HELHP
ID LEUD_HELHP Reviewed; 165 AA.
AC Q7VH32;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=HH_1135;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77732.1; -; Genomic_DNA.
DR RefSeq; WP_011115975.1; NC_004917.1.
DR AlphaFoldDB; Q7VH32; -.
DR SMR; Q7VH32; -.
DR STRING; 235279.HH_1135; -.
DR EnsemblBacteria; AAP77732; AAP77732; HH_1135.
DR KEGG; hhe:HH_1135; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_1_1_7; -.
DR OMA; GLPIIEC; -.
DR OrthoDB; 1384217at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000002495; 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; IPR011824; LeuD/DmdB_bac.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR Pfam; PF00694; Aconitase_C; 1.
DR TIGRFAMs; TIGR02084; leud; 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..165
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_0000141925"
SQ SEQUENCE 165 AA; 18212 MW; 10A86E561452FB1C CRC64;
MKAQGFVHKY GDNVDTDVII PARYLNTADH KELANHCMED IDKDFVAKVK EGDIMVGGWN
FGCGSSREHA PIAIKASGIS CIIAKSFARI FYRNAINIGL AIIESEEVAQ SLENGDEVAI
DFDKGIITNC KNNQQFSTTP FPPFIQEIIN ANGYLNWISK QKANA
