LEUD1_SALTY
ID LEUD1_SALTY Reviewed; 201 AA.
AC P04787;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=3-isopropylmalate dehydratase small subunit 1 {ECO:0000255|HAMAP-Rule:MF_01031};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01031, ECO:0000269|PubMed:7026530};
DE AltName: Full=Alpha-IPM isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01031};
DE Short=IPMI 1 {ECO:0000255|HAMAP-Rule:MF_01031};
DE AltName: Full=Isopropylmalate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01031};
GN Name=leuD1 {ECO:0000255|HAMAP-Rule:MF_01031}; Synonyms=leuD;
GN OrderedLocusNames=STM0110;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2993799; DOI=10.1007/bf00330763;
RA Friedberg D., Rosenthal E.R., Jones J.W., Calvo J.M.;
RT "Characterization of the 3' end of the leucine operon of Salmonella
RT typhimurium.";
RL Mol. Gen. Genet. 199:486-494(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=LT2;
RX PubMed=7026530; DOI=10.1128/jb.148.1.210-219.1981;
RA Fultz P.N., Kemper J.;
RT "Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed
RT of two different subunits.";
RL J. Bacteriol. 148:210-219(1981).
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, ECO:0000269|PubMed:7026530}.
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 ECO:0000269|PubMed:7026530};
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, ECO:0000269|PubMed:7026530}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01031, ECO:0000305}.
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DR EMBL; X02528; CAA26364.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19074.1; -; Genomic_DNA.
DR PIR; S07306; S07306.
DR RefSeq; NP_459115.1; NC_003197.2.
DR RefSeq; WP_000818267.1; NC_003197.2.
DR AlphaFoldDB; P04787; -.
DR SMR; P04787; -.
DR STRING; 99287.STM0110; -.
DR PaxDb; P04787; -.
DR PRIDE; P04787; -.
DR EnsemblBacteria; AAL19074; AAL19074; STM0110.
DR GeneID; 1251628; -.
DR KEGG; stm:STM0110; -.
DR PATRIC; fig|99287.12.peg.116; -.
DR HOGENOM; CLU_081378_0_3_6; -.
DR OMA; AFTTHTG; -.
DR PhylomeDB; P04787; -.
DR BioCyc; SENT99287:STM0110-MON; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001014; 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 Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..201
FT /note="3-isopropylmalate dehydratase small subunit 1"
FT /id="PRO_0000141875"
SQ SEQUENCE 201 AA; 22506 MW; D2A2254F19B8B549 CRC64;
MAEKFTQHTG LVVPLDAANV DTDAIIPKQF LQKVTRTGFG AHLFNDWRFL DEKGQQPNPE
FVLNFPEYQG ASILLARENF GCGSSREHAP WALTDYGFKV VIAPSFADIF YGNSFNNQLL
PVTLSDAQVD ELFALVKANP GIKFEVDLEA QVVKAGDKTY SFKIDDFRRH CMLNGLDSIG
LTLQHEDAIA AYENKQPAFM R
