LEUC1_SALTY
ID LEUC1_SALTY Reviewed; 466 AA.
AC P15717;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=3-isopropylmalate dehydratase large subunit 1 {ECO:0000255|HAMAP-Rule:MF_01026};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026, ECO:0000269|PubMed:7026530};
DE AltName: Full=Alpha-IPM isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01026};
DE Short=IPMI 1 {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Isopropylmalate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01026};
GN Name=leuC1 {ECO:0000255|HAMAP-Rule:MF_01026}; Synonyms=leuC;
GN OrderedLocusNames=STM0111;
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].
RC STRAIN=LT2;
RX PubMed=2190189; DOI=10.1093/nar/18.10.3072;
RA Rosenthal E.R., Calvo J.M.;
RT "The nucleotide sequence of leuC from Salmonella typhimurium.";
RL Nucleic Acids Res. 18:3072-3072(1990).
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_01026, 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_01026,
CC ECO:0000269|PubMed:7026530};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01026};
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_01026}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01026, ECO:0000269|PubMed:7026530}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
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DR EMBL; X51476; CAA35840.1; -; Genomic_DNA.
DR EMBL; M31047; AAA27155.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19075.1; -; Genomic_DNA.
DR PIR; S10171; S10171.
DR RefSeq; NP_459116.1; NC_003197.2.
DR RefSeq; WP_001140629.1; NC_003197.2.
DR AlphaFoldDB; P15717; -.
DR SMR; P15717; -.
DR STRING; 99287.STM0111; -.
DR PaxDb; P15717; -.
DR EnsemblBacteria; AAL19075; AAL19075; STM0111.
DR GeneID; 1251629; -.
DR KEGG; stm:STM0111; -.
DR PATRIC; fig|99287.12.peg.117; -.
DR HOGENOM; CLU_006714_3_4_6; -.
DR OMA; CNMSIEM; -.
DR PhylomeDB; P15717; -.
DR BioCyc; SENT99287:STM0111-MON; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR033941; IPMI_cat.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00170; leuC; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..466
FT /note="3-isopropylmalate dehydratase large subunit 1"
FT /id="PRO_0000076803"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 407
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT CONFLICT 38..54
FT /note="PQAFDGLRAHHRPVRQP -> RRRLTVCARTIAGTSA (in Ref. 1;
FT CAA35840/AAA27155)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="S -> P (in Ref. 1; CAA35840/AAA27155)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> P (in Ref. 1; CAA35840/AAA27155)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..365
FT /note="AKGR -> GQRA (in Ref. 1; CAA35840/AAA27155)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..385
FT /note="PGVQALVVPGSGPVKAQ -> GRAGAGGAGFRSGESA (in Ref. 1;
FT CAA35840/AAA27155)"
FT /evidence="ECO:0000305"
FT CONFLICT 411..413
FT /note="LAM -> VAV (in Ref. 1; CAA35840/AAA27155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 49786 MW; 34D5FABBA17CC51C CRC64;
MAKTLYEKLF DAHVVFEAPN ETPLLYIDRH LVHEVTSPQA FDGLRAHHRP VRQPGKTFAT
MDHNVSTQTK DINASGEMAR IQMQELIKNC NEFGVELYDL NHPYQGIVHV MGPEQGVTLP
GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ GRAKTMKIEV TGNAAPGITA
KDIVLAIIGK TGSAGGTGHV VEFCGDAIRA LSMEGRMTLC NMAIEMGAKA GLVAPDETTF
NYVKGRLHAP KGRDFDEAVE YWKTLKTDDG ATFDTVVALR AEEIAPQVTW GTNPGQVISV
TDIIPDPASF SDPVERASAE KALAYMGLQP GVPLTDVAID KVFIGSCTNS RIEDLRAAAE
VAKGRKVAPG VQALVVPGSG PVKAQAEAEG LDKIFIEAGF EWRLPGCSMC LAMNNDRLNP
GERCASTSNR NFEGRQGRGG RTHLVSPAMA AAAAVTGHFA DIRSIK
