ILVA_CORGL
ID ILVA_CORGL Reviewed; 436 AA.
AC Q04513;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
GN Name=ilvA; OrderedLocusNames=Cgl2127, cg2334;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=1459955; DOI=10.1128/jb.174.24.8065-8072.1992;
RA Mockel B., Eggeling L., Sahm H.;
RT "Functional and structural analyses of threonine dehydratase from
RT Corynebacterium glutamicum.";
RL J. Bacteriol. 174:8065-8072(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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 -!- 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; L01508; AAA23303.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99520.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20464.1; -; Genomic_DNA.
DR PIR; A47044; A47044.
DR RefSeq; NP_601328.2; NC_003450.3.
DR RefSeq; WP_003862033.1; NC_006958.1.
DR AlphaFoldDB; Q04513; -.
DR SMR; Q04513; -.
DR STRING; 196627.cg2334; -.
DR KEGG; cgb:cg2334; -.
DR KEGG; cgl:Cgl2127; -.
DR PATRIC; fig|196627.13.peg.2065; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_11; -.
DR OMA; VNFPQRA; -.
DR BRENDA; 4.3.1.19; 960.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR011820; IlvA.
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; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR02079; THD1; 1.
DR PROSITE; PS51672; ACT_LIKE; 1.
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.
FT CHAIN 1..436
FT /note="L-threonine dehydratase biosynthetic IlvA"
FT /id="PRO_0000185572"
FT DOMAIN 353..427
FT /note="ACT-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT REGION 1..357
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 358..436
FT /note="Regulatory"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 203..207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 81..82
FT /note="LT -> SP (in Ref. 1; AAA23303)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> E (in Ref. 1; AAA23303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 46572 MW; 41EFD4F57FD5DB95 CRC64;
MSETYVSEKS PGVMASGAEL IRAADIQTAQ ARISSVIAPT PLQYCPRLSE ETGAEIYLKR
EDLQDVRSYK IRGALNSGAQ LTQEQRDAGI VAASAGNHAQ GVAYVCKSLG VQGRIYVPVQ
TPKQKRDRIM VHGGEFVSLV VTGNNFDEAS AAAHEDAERT GATLIEPFDA RNTVIGQGTV
AAEILSQLTS MGKSADHVMV PVGGGGLLAG VVSYMADMAP RTAIVGIEPA GAASMQAALH
NGGPITLETV DPFVDGAAVK RVGDLNYTIV EKNQGRVHMM SATEGAVCTE MLDLYQNEGI
IAEPAGALSI AGLKEMSFAP GSVVVCIISG GNNDVLRYAE IAERSLVHRG LKHYFLVNFP
QKPGQLRHFL EDILGPDDDI TLFEYLKRNN RETGTALVGI HLSEASGLDS LLERMEESAI
DSRRLEPGTP EYEYLT
