ILVA_SALTY
ID ILVA_SALTY Reviewed; 514 AA.
AC P20506; Q9L6S8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=L-Threonine dehydratase biosynthetic IlvA;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
GN Name=ilvA; OrderedLocusNames=STM3905; ORFNames=STMD1.87;
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=3290055; DOI=10.1016/0378-1119(88)90528-8;
RA Taillon B.E., Little R., Lawther R.P.;
RT "Analysis of the functional domains of biosynthetic threonine deaminase by
RT comparison of the amino acid sequences of three wild-type alleles to the
RT amino acid sequence of biodegradative threonine deaminase.";
RL Gene 63:245-252(1988).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC STRAIN=LT2;
RX PubMed=2473940; DOI=10.1016/0378-1119(89)90166-2;
RA Lopes J.M., Lawther R.P.;
RT "Physical identification of an internal promoter, ilvAp, in the distal
RT portion of the ilvGMEDA operon.";
RL Gene 76:255-269(1989).
CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and
CC ammonia from threonine in a two-step reaction. The first step involved
CC a dehydration of threonine and a production of enamine intermediates
CC (aminocrotonate), which tautomerizes to its imine form (iminobutyrate).
CC Both intermediates are unstable and short-lived. The second step is the
CC nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-
CC ketobutyrate and free ammonia. In the low water environment of the
CC cell, the second step is accelerated by RidA (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Isoleucine allosterically inhibits whereas valine
CC allosterically activates this enzyme. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; M26670; AAA27150.1; -; Genomic_DNA.
DR EMBL; AF233324; AAF33479.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22755.1; -; Genomic_DNA.
DR EMBL; M25498; AAA27151.1; -; Genomic_DNA.
DR PIR; JT0278; DWEBTT.
DR RefSeq; NP_462796.1; NC_003197.2.
DR RefSeq; WP_001518457.1; NC_003197.2.
DR AlphaFoldDB; P20506; -.
DR SMR; P20506; -.
DR STRING; 99287.STM3905; -.
DR PaxDb; P20506; -.
DR EnsemblBacteria; AAL22755; AAL22755; STM3905.
DR GeneID; 1255431; -.
DR KEGG; stm:STM3905; -.
DR PATRIC; fig|99287.12.peg.4127; -.
DR HOGENOM; CLU_021152_6_1_6; -.
DR OMA; VNFPQRA; -.
DR PhylomeDB; P20506; -.
DR BioCyc; SENT99287:STM3905-MON; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR GO; GO:0006566; P:threonine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.1020.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
DR InterPro; IPR038110; TD_ACT-like_sf.
DR InterPro; IPR005787; Thr_deHydtase_biosynth.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Isoleucine biosynthesis; Lyase;
KW Pyridoxal phosphate; Reference proteome; Repeat.
FT CHAIN 1..514
FT /note="L-Threonine dehydratase biosynthetic IlvA"
FT /id="PRO_0000185580"
FT DOMAIN 339..411
FT /note="ACT-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT DOMAIN 434..504
FT /note="ACT-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT BINDING 89
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 188..192
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 71
FT /note="A -> T (in Ref. 1; AAA27150)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="F -> L (in Ref. 1; AAA27150)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> G (in Ref. 1; AAA27150)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="A -> T (in Ref. 1; AAA27150)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..353
FT /note="SFL -> NFP (in Ref. 1; AAA27150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 56253 MW; 136BC535F1F0035B CRC64;
MAESQPLSVA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV KREDRQPVHS
FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR LGVKSLIVMP KATADIKVDA
VRGFGGEVLL HGANFDEAKA KAIELAQQQG FTWVPPFDHP MVIAGQGTLA LELLQQDSHL
DRVFVPVGGG GLAAGVAVLI KQLMPQIKVI AVEAEDSACL KAALEAGHPV DLPRVGLFAE
GVAVKRIGDE TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI
AQHNIRGERL AHVLSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG SFLKFCQLLG
GRMVTEFNYR FADAKNACIF VGVRVSQGLE ERKEIITQLC DGGYSVVDLS DDEMAKLHVR
YMVGGRPSKP LQERLYSFEF PESPGALLKF LHTLGTHWNI SLFHYRSHGT DYGRVLAAFE
LGDHEPDFET RLHELGYECH DESNNPAFRF FLAG
