ID D3TBK5_ACIB4 Unreviewed; 163 AA.
AC D3TBK5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=Aboo_0128 {ECO:0000313|EMBL:ADD07940.1};
OS Aciduliprofundum boonei (strain DSM 19572 / T469).
OC Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD07940.1, ECO:0000313|Proteomes:UP000001400};
RN [1] {ECO:0000313|Proteomes:UP000001400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT "Complete sequence of Aciduliprofundum boonei T469.";
RL Submitted (FEB-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|HAMAP-Rule:MF_01032}.
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DR EMBL; CP001941; ADD07940.1; -; Genomic_DNA.
DR RefSeq; WP_012997044.1; NC_013926.1.
DR AlphaFoldDB; D3TBK5; -.
DR GeneID; 8827064; -.
DR KEGG; abi:Aboo_0128; -.
DR HOGENOM; CLU_081378_1_1_2; -.
DR OrthoDB; 6505at2157; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001400; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001400}.
FT DOMAIN 48..105
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 163 AA; 18369 MW; 682ED62648CA36DB CRC64;
MGRVWKYGDD VNTDVIFPGK YTYKIMSDEE MASHALEDLD PEFAKNVKPG DVIVAGKNWG
YGSSREQAVK CLKAAGIKAI IAESFARIYY RNCINLGLPA ITLKREEIEK FEAGDKVEVD
IENGIIINKT KGFEVHFPPF EGYVMDIIKA GGIIEYIRKN REN
//
