ID D6K202_9ACTN Unreviewed; 197 AA.
AC D6K202;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=SSTG_03599 {ECO:0000313|EMBL:EFF93280.2};
OS Streptomyces sp. e14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF93280.2, ECO:0000313|Proteomes:UP000004704};
RN [1] {ECO:0000313|EMBL:EFF93280.2, ECO:0000313|Proteomes:UP000004704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain e14.";
RL Submitted (OCT-2009) 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|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}.
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DR EMBL; GG753626; EFF93280.2; -; Genomic_DNA.
DR RefSeq; WP_009190824.1; NZ_GG753626.1.
DR AlphaFoldDB; D6K202; -.
DR STRING; 645465.SSTG_03599; -.
DR eggNOG; COG0066; Bacteria.
DR OrthoDB; 9777465at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000004704; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004704}.
FT DOMAIN 1..117
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 197 AA; 22139 MW; 6B685625894AB99D CRC64;
MEAFTTHTGR AVPLRRSNVD TDQIIPAHWL KKVTRDGFED GLFEAWRKDP EFVLNRPERQ
GATVLVAGPD FGTGSSREHA VWALQNYGFK TVISARFADI FRGNSLKNGL LTVVLDQKVV
DALWELVESD PSAEITVDLV AREVRAEGIT AAFELDENSR WRLLNGLDDI SITLQNEEDI
AAYEAKRPSF KPRTLQV
//
