ID A0A165K8D0_9BURK Unreviewed; 221 AA.
AC A0A165K8D0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000256|HAMAP-Rule:MF_01031};
DE EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01031};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01031};
DE Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01031};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01031};
GN Name=leuD {ECO:0000256|HAMAP-Rule:MF_01031};
GN ORFNames=A1D30_15250 {ECO:0000313|EMBL:KZT15171.1};
OS Acidovorax sp. GW101-3H11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT15171.1, ECO:0000313|Proteomes:UP000077219};
RN [1] {ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KZT15171.1, ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT15171.1,
RC ECO:0000313|Proteomes:UP000077219};
RX PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL Nature 557:503-509(2018).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000256|ARBA:ARBA00002695, ECO:0000256|HAMAP-Rule:MF_01031}.
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|ARBA:ARBA00000491,
CC ECO:0000256|HAMAP-Rule:MF_01031};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|ARBA:ARBA00004729,
CC ECO:0000256|HAMAP-Rule:MF_01031}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|ARBA:ARBA00011271,
CC ECO:0000256|HAMAP-Rule:MF_01031}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009845, ECO:0000256|HAMAP-Rule:MF_01031}.
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:KZT15171.1}.
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DR EMBL; LUKZ01000012; KZT15171.1; -; Genomic_DNA.
DR RefSeq; WP_063461164.1; NZ_LUKZ01000012.1.
DR AlphaFoldDB; A0A165K8D0; -.
DR STRING; 1813946.A1D30_15250; -.
DR OrthoDB; 9777465at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000077219; Unassembled WGS sequence.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
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_01031; LeuD_type1; 1.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR NCBIfam; TIGR00171; leuD; 1.
DR PANTHER; PTHR43345:SF5; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01031};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01031};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01031};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01031}.
FT DOMAIN 1..132
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 221 AA; 24991 MW; 75647ECADDF39FE3 CRC64;
MQKFTVHKGL VAPMDRENVD TDAIIPKQFL KSIKKTGFGP NLFDEWRYLD KGEPGIPESA
RKPNPDFVLN LPRYKGASIL IARKNFGCGS SREHAPWALD QFGFRAVIAP SFADIFFNNC
FKNGLLPIVL PEATVAQLFD EVAAFPGYQL TIDLERQVVV RQNRDEVVGE EIPFDVIAFR
KYCLLNGFDD IGLTLRKSDK IRAFEAERLA TKPWLAHTMV S
//
