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 27-MAR-2024, entry version 200. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b3772; -. DR EnsemblBacteria; AAC77492; AAC77492; b3772. 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; TRFEYTK; -. DR OrthoDB; 9811476at2; -. DR PhylomeDB; P04968; -. DR BioCyc; EcoCyc:THREDEHYDSYN-MONOMER; -. DR BioCyc; MetaCyc:THREDEHYDSYN-MONOMER; -. 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 CDD; cd04906; ACT_ThrD-I_1; 1. DR CDD; cd04907; ACT_ThrD-I_2; 1. DR CDD; cd01562; Thr-dehyd; 1. DR Gene3D; 3.40.50.1100; -; 2. DR InterPro; IPR045865; ACT-like_dom_sf. 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; IPR001926; TrpB-like_PALP. DR InterPro; IPR036052; TrpB-like_PALP_sf. DR NCBIfam; TIGR01124; ilvA_2Cterm; 1. DR PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00291; PALP; 1. DR Pfam; PF00585; Thr_dehydrat_C; 2. DR SUPFAM; SSF55021; ACT-like; 2. DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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 //