LEUD_PYRAE
ID LEUD_PYRAE Reviewed; 161 AA.
AC Q8ZW36;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=3-isopropylmalate dehydratase small subunit;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE Short=IPMI;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leuD; OrderedLocusNames=PAE1991;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE009441; AAL63866.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZW36; -.
DR SMR; Q8ZW36; -.
DR STRING; 178306.PAE1991; -.
DR PRIDE; Q8ZW36; -.
DR EnsemblBacteria; AAL63866; AAL63866; PAE1991.
DR KEGG; pai:PAE1991; -.
DR PATRIC; fig|178306.9.peg.1471; -.
DR eggNOG; arCOG02230; Archaea.
DR HOGENOM; CLU_081378_1_1_2; -.
DR InParanoid; Q8ZW36; -.
DR OMA; GLPIIEC; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000002439; 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..161
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_0000141946"
SQ SEQUENCE 161 AA; 17175 MW; 440B9AA6AF3F45A2 CRC64;
MKIRGRALVY GDKIDTDVII PAKYLVYTDP ALLGQHAMEP LDPEFPKKAK GAVLVAGRAF
GMGSSREQAA LALKGAGVLA VVAESFARIF FRNAINVGLP VLQAPGIREK VKDGDEVELD
VEGGIVRNIT TGEVIVGKPL RGLPLEILKA GGLLNYLKNS R