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Database: UniProt
Entry: W3ANY8_9FIRM
LinkDB: W3ANY8_9FIRM
Original site: W3ANY8_9FIRM 
ID   W3ANY8_9FIRM            Unreviewed;       168 AA.
AC   W3ANY8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=UYO_1167 {ECO:0000313|EMBL:ETP72750.1};
OS   Lachnospiraceae bacterium JC7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP72750.1, ECO:0000313|Proteomes:UP000018967};
RN   [1] {ECO:0000313|EMBL:ETP72750.1, ECO:0000313|Proteomes:UP000018967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC7 {ECO:0000313|EMBL:ETP72750.1,
RC   ECO:0000313|Proteomes:UP000018967};
RA   Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA   O Cuiv P., Morrison M.;
RT   "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT   identified member of the bovine rumen core microbiota.";
RL   Submitted (JUL-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETP72750.1}.
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DR   EMBL; ALYD01000010; ETP72750.1; -; Genomic_DNA.
DR   AlphaFoldDB; W3ANY8; -.
DR   PATRIC; fig|1165092.3.peg.1162; -.
DR   OrthoDB; 9777465at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000018967; Unassembled WGS sequence.
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          56..105
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   168 AA;  17949 MW;  1958189132BFA687 CRC64;
     MKTKVTGKII VVGDNIDTDQ IYPGRFLAIT DPKEIGSHCL SGVDESIAPD FPQGGIVVAG
     RNFGCGSSRE HAPIALLNMG ASAILADSFA RIFFRNSINL GLLPVICKGI KDKVKDGQTL
     TLDIEAGTVT IEETGEVLQC EQLGDQAMKI LEAGGIKPMM RKRFGKSE
//
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