ID A0A0F2LAU3_9CREN Unreviewed; 164 AA.
AC A0A0F2LAU3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=TU35_05000 {ECO:0000313|EMBL:KJR73590.1};
OS Thermoproteus sp. AZ2.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=1609232 {ECO:0000313|EMBL:KJR73590.1, ECO:0000313|Proteomes:UP000033636};
RN [1] {ECO:0000313|EMBL:KJR73590.1, ECO:0000313|Proteomes:UP000033636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-2015) 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|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:KJR73590.1}.
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DR EMBL; JZWT01000041; KJR73590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2LAU3; -.
DR PATRIC; fig|1609232.3.peg.1355; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000033636; 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 49..102
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 164 AA; 17457 MW; F24BFF160BC0F74B CRC64;
MEIRGRALVY GDKIDTDIII PARYLVYTDP AILGQHAMEP LDPDFPKKAK GAIIIAGRAF
GMGSSREQAA TALKGAGVAA VVAESFARIF FRNAINTGLP VLQAPARGKV REGDEVLIRL
EAGEVVNLTT GEVIKGKPLT GLALEILKAG GLVEYLKYIA KQQA
//
