LEUD2_PYRAB
ID LEUD2_PYRAB Reviewed; 163 AA.
AC Q9V1I9; G8ZGE0;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=3-isopropylmalate dehydratase small subunit 2;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase 2;
DE Short=IPMI 2;
DE AltName: Full=Isopropylmalate isomerase 2;
GN Name=leuD2; Synonyms=leuD-2; OrderedLocusNames=PYRAB04380;
GN ORFNames=PAB0288;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49360.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69819.1; -; Genomic_DNA.
DR PIR; A75160; A75160.
DR RefSeq; WP_010867561.1; NC_000868.1.
DR AlphaFoldDB; Q9V1I9; -.
DR SMR; Q9V1I9; -.
DR STRING; 272844.PAB0288; -.
DR EnsemblBacteria; CAB49360; CAB49360; PAB0288.
DR GeneID; 1495332; -.
DR KEGG; pab:PAB0288; -.
DR PATRIC; fig|272844.11.peg.463; -.
DR eggNOG; arCOG02230; Archaea.
DR HOGENOM; CLU_081378_1_1_2; -.
DR OMA; ITPGRYN; -.
DR OrthoDB; 86621at2157; -.
DR PhylomeDB; Q9V1I9; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..163
FT /note="3-isopropylmalate dehydratase small subunit 2"
FT /id="PRO_0000141945"
SQ SEQUENCE 163 AA; 18010 MW; F759C5473A36B632 CRC64;
MITTGRVWKF WDNVSTDEIT PGRYNLTKDP QELARIAFIE VRPEFAEKVR RGDVVVGGKN
FGIGSSRESA ALALKAAGVS GIIAKSFGRI FYRNAVNLGI PLLIGDTDEL EDGDVITVNW
ETGEVRKNGQ TLQFEPLPGF LLEIVREGGI LEFIRRRGDL CIG
