ILVA_ECOLI
ID ILVA_ECOLI Reviewed; 514 AA.
AC P04968; Q2M881;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
GN Name=ilvA; OrderedLocusNames=b3772, JW3745;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3315862; DOI=10.1016/0378-1119(87)90136-3;
RA Cox J.L., Cox B.J., Fidanza V., Calhoun D.H.;
RT "The complete nucleotide sequence of the ilvGMEDA cluster of Escherichia
RT coli K-12.";
RL Gene 56:185-198(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Garrison E., Harms E., Umbarger H.E.;
RL Submitted (AUG-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3550695; DOI=10.1093/nar/15.5.2137;
RA Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
RA Hatfield G.W.;
RT "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia
RT coli K-12.";
RL Nucleic Acids Res. 15:2137-2155(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-514.
RC STRAIN=K12;
RX PubMed=3003115; DOI=10.1016/s0021-9258(17)35955-0;
RA Wek R.C., Hatfield G.W.;
RT "Nucleotide sequence and in vivo expression of the ilvY and ilvC genes in
RT Escherichia coli K12. Transcription from divergent overlapping promoters.";
RL J. Biol. Chem. 261:2441-2450(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC STRAIN=K12;
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).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=13324101; DOI=10.1126/science.123.3202.848;
RA Umbarger H.E.;
RT "Evidence for a negative-feedback mechanism in the biosynthesis of
RT isoleucine.";
RL Science 123:848-848(1956).
RN [10]
RP FUNCTION AS A THREONINE DEHYDRATASE AND IN THE L-ISOLEUCINE BIOSYNTHESIS,
RP AND INDUCTION.
RX PubMed=13405870; DOI=10.1128/jb.73.1.105-112.1957;
RA Umbarger H.E., Brown B.;
RT "Threonine deamination in Escherichia coli. II. Evidence for two L-
RT threonine deaminases.";
RL J. Bacteriol. 73:105-112(1957).
RN [11]
RP REACTION MECHANISM, AND COFACTOR.
RX PubMed=5321308; DOI=10.1016/s0021-9258(18)97012-2;
RA Phillips A.T., Wood W.A.;
RT "The mechanism of action of 5'-adenylic acid-activated threonine
RT dehydrase.";
RL J. Biol. Chem. 240:4703-4709(1965).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP AND SUBUNIT.
RX PubMed=9562556; DOI=10.1016/s0969-2126(98)00048-3;
RA Gallagher D.T., Gilliland G.L., Xiao G., Zondlo J., Fisher K.E.,
RA Chinchilla D., Eisenstein E.;
RT "Structure and control of pyridoxal phosphate dependent allosteric
RT threonine deaminase.";
RL Structure 6:465-475(1998).
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.
CC {ECO:0000269|PubMed:13405870}.
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:0000269|PubMed:5321308};
CC -!- ACTIVITY REGULATION: Isoleucine allosterically inhibits whereas valine
CC allosterically activates this enzyme. {ECO:0000269|PubMed:13324101}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9562556}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:13405870}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; X04890; CAA28577.1; -; Genomic_DNA.
DR EMBL; K03503; AAA24014.1; -; Genomic_DNA.
DR EMBL; M10313; AAB59054.1; -; Genomic_DNA.
DR EMBL; M11689; AAA24027.1; -; Genomic_DNA.
DR EMBL; M32253; AAA24024.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67575.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77492.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77525.1; -; Genomic_DNA.
DR EMBL; M25497; AAA24015.1; -; Genomic_DNA.
DR PIR; B27310; DWECTS.
DR RefSeq; NP_418220.1; NC_000913.3.
DR RefSeq; WP_000785596.1; NZ_SSZK01000025.1.
DR PDB; 1TDJ; X-ray; 2.80 A; A=1-514.
DR PDBsum; 1TDJ; -.
DR AlphaFoldDB; P04968; -.
DR SMR; P04968; -.
DR BioGRID; 4259586; 18.
DR DIP; DIP-10018N; -.
DR IntAct; P04968; 10.
DR STRING; 511145.b3772; -.
DR jPOST; P04968; -.
DR PaxDb; P04968; -.
DR PRIDE; P04968; -.
DR EnsemblBacteria; AAC77492; AAC77492; b3772.
DR EnsemblBacteria; BAE77525; BAE77525; BAE77525.
DR GeneID; 948287; -.
DR KEGG; ecj:JW3745; -.
DR KEGG; eco:b3772; -.
DR PATRIC; fig|1411691.4.peg.2934; -.
DR EchoBASE; EB0488; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_6_0_6; -.
DR InParanoid; P04968; -.
DR OMA; VNFPQRA; -.
DR PhylomeDB; P04968; -.
DR BioCyc; EcoCyc:THREDEHYDSYN-MON; -.
DR BioCyc; MetaCyc:THREDEHYDSYN-MON; -.
DR BRENDA; 4.3.1.19; 2026.
DR UniPathway; UPA00047; UER00054.
DR EvolutionaryTrace; P04968; -.
DR PRO; PR:P04968; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016597; F:amino acid binding; IDA:EcoliWiki.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:EcoliWiki.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IDA:EcoCyc.
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; IDA: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 1: Evidence at protein level;
KW 3D-structure; 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_0000185573"
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:0000269|PubMed:9562556"
FT BINDING 188..192
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:9562556"
FT BINDING 315
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:9562556"
FT MOD_RES 62
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:9562556"
FT CONFLICT 120
FT /note="A -> R (in Ref. 2; AAA24014)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="A -> R (in Ref. 2; AAA24014/AAA67575)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="G -> C (in Ref. 2; AAA24014)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="A -> G (in Ref. 3; AAA24024)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> V (in Ref. 2; AAA24014)"
FT /evidence="ECO:0000305"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:1TDJ"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:1TDJ"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 360..370
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:1TDJ"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:1TDJ"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:1TDJ"
FT HELIX 506..511
FT /evidence="ECO:0007829|PDB:1TDJ"
SQ SEQUENCE 514 AA; 56195 MW; 9D389A0EDD8DE692 CRC64;
MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV KREDRQPVHS
FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR LGVKALIVMP TATADIKVDA
VRGFGGEVLL HGANFDEAKA KAIELSQQQG FTWVPPFDHP MVIAGQGTLA LELLQQDAHL
DRVFVPVGGG GLAAGVAVLI KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE
GVAVKRIGDE TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI
ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG SFLKFCQLLG
GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN DGGYSVVDLS DDEMAKLHVR
YMVGGRPSHP LQERLYSFEF PESPGALLRF LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE
LGDHEPDFET RLNELGYDCH DETNNPAFRF FLAG
