LEUD_STRMU
ID LEUD_STRMU Reviewed; 196 AA.
AC Q8DTG5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000255|HAMAP-Rule:MF_01031};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01031};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01031};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01031};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01031};
GN Name=leuD {ECO:0000255|HAMAP-Rule:MF_01031}; OrderedLocusNames=SMU_1381;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01031};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_01031}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01031}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01031}.
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DR EMBL; AE014133; AAN59048.1; -; Genomic_DNA.
DR RefSeq; NP_721742.1; NC_004350.2.
DR RefSeq; WP_002262705.1; NC_004350.2.
DR PDB; 2HCU; X-ray; 2.10 A; A=1-196.
DR PDBsum; 2HCU; -.
DR AlphaFoldDB; Q8DTG5; -.
DR SMR; Q8DTG5; -.
DR STRING; 210007.SMU_1381; -.
DR PRIDE; Q8DTG5; -.
DR EnsemblBacteria; AAN59048; AAN59048; SMU_1381.
DR GeneID; 66819204; -.
DR KEGG; smu:SMU_1381; -.
DR PATRIC; fig|210007.7.peg.1228; -.
DR eggNOG; COG0066; Bacteria.
DR HOGENOM; CLU_081378_0_3_9; -.
DR OMA; AFTTHTG; -.
DR PhylomeDB; Q8DTG5; -.
DR UniPathway; UPA00048; UER00071.
DR EvolutionaryTrace; Q8DTG5; -.
DR Proteomes; UP000002512; Chromosome.
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; -; 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 Pfam; PF00694; Aconitase_C; 1.
DR TIGRFAMs; TIGR00171; leuD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Leucine biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..196
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_0000141893"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2HCU"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2HCU"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2HCU"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2HCU"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:2HCU"
SQ SEQUENCE 196 AA; 22689 MW; E27F1A35FA9ED7FC CRC64;
MEEFTIYTGT TVPLMNDNID TDQILPKQFL KLIDKKGFGK YLMYEWRYLD NNYTENPDFI
FNQPEYREAS ILITGDNFGA GSSREHAAWA LADYGFKVIV AGSFGDIHYN NDLNNGILPI
IQPKEVRDKL AKLKPTDEVT VNLFEQKIYS PVGDFSFDID GEWKHKLLNG LDDIGITLQY
EDLIAQYEQN RPSYWH
