LEUD_METMA
ID LEUD_METMA Reviewed; 162 AA.
AC Q8PWT6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 25-MAY-2022, entry version 122.
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=MM_1490;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008384; AAM31186.1; -; Genomic_DNA.
DR RefSeq; WP_011033436.1; NC_003901.1.
DR AlphaFoldDB; Q8PWT6; -.
DR SMR; Q8PWT6; -.
DR STRING; 192952.MM_1490; -.
DR EnsemblBacteria; AAM31186; AAM31186; MM_1490.
DR GeneID; 24883223; -.
DR KEGG; mma:MM_1490; -.
DR PATRIC; fig|192952.21.peg.1722; -.
DR eggNOG; arCOG02230; Archaea.
DR HOGENOM; CLU_081378_1_1_2; -.
DR OMA; AKHAFEG; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000595; 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..162
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_0000141941"
SQ SEQUENCE 162 AA; 17810 MW; 78B1C5DE2287C363 CRC64;
MKGRAWKFGD DVDTDAVIPG RYLIFNTPGE LAKYTFEGVR PDFAKNVHEN DIVVAGSNFG
CGSSREHAPL ALKGSKVSCV IAKSFARIFF RNAINIGVPV LECPDTDKID DGDELEVDIS
TGVIQNRTKG ETYQATPLPD FVREIVDEGG LIEYARKLVS ER