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Database: UniProt
Entry: D4LZ47_9FIRM
LinkDB: D4LZ47_9FIRM
Original site: D4LZ47_9FIRM 
ID   D4LZ47_9FIRM            Unreviewed;       159 AA.
AC   D4LZ47;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000256|HAMAP-Rule:MF_01032};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01032};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01032};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01032};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01032};
GN   Name=leuD {ECO:0000256|HAMAP-Rule:MF_01032};
GN   ORFNames=RTO_25910 {ECO:0000313|EMBL:CBL27057.1};
OS   [Ruminococcus] torques L2-14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Mediterraneibacter.
OX   NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL27057.1, ECO:0000313|Proteomes:UP000008956};
RN   [1] {ECO:0000313|EMBL:CBL27057.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL27057.1,
RC   ECO:0000313|Proteomes:UP000008956};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus torques L2-14.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL27057.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL27057.1,
RC   ECO:0000313|Proteomes:UP000008956};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_01032};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01032}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01032}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009869, ECO:0000256|HAMAP-Rule:MF_01032}.
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DR   EMBL; FP929055; CBL27057.1; -; Genomic_DNA.
DR   RefSeq; WP_015529635.1; NC_021015.1.
DR   AlphaFoldDB; D4LZ47; -.
DR   STRING; 33039.ERS852502_01351; -.
DR   GeneID; 83694201; -.
DR   KEGG; rto:RTO_25910; -.
DR   PATRIC; fig|657313.3.peg.2471; -.
DR   HOGENOM; CLU_081378_1_1_9; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000008956; 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; Aconitase, domain 4; 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   NCBIfam; TIGR02087; LEUD_arch; 1.
DR   PANTHER; PTHR43345:SF2; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 1-RELATED; 1.
DR   PANTHER; PTHR43345; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 2-RELATED-RELATED; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01032};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01032};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01032};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01032}.
FT   DOMAIN          47..99
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   159 AA;  17435 MW;  DF21916AA114029A CRC64;
     MEKGTIFKFH NDLDTDQIIA SQYLLLPNLD EMKSHTFESL DPDFAKKVKP GDFVVGGENF
     GCGSSREQAP GVLKALGVQA VIAKSFARIF YRNAINIGLP VIVCKELPDE VKTGDTMELR
     MSDGTAEANG KTYSCTKLPE YMQNILNQGG LIASLNKED
//
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