ID   ILVA_STAES              Reviewed;         422 AA.
AC   Q8CNK9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=SE_1662;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO05261.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE015929; AAO05261.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_765217.1; NC_004461.1.
DR   RefSeq; WP_001830018.1; NC_004461.1.
DR   AlphaFoldDB; Q8CNK9; -.
DR   SMR; Q8CNK9; -.
DR   STRING; 176280.SE_1662; -.
DR   EnsemblBacteria; AAO05261; AAO05261; SE_1662.
DR   GeneID; 50018239; -.
DR   KEGG; sep:SE_1662; -.
DR   PATRIC; fig|176280.10.peg.1626; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_4_2_9; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001411; 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; 3.40.50.1100; -; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
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; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   SUPFAM; SSF55021; SSF55021; 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   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..422
FT                   /note="L-threonine dehydratase biosynthetic IlvA"
FT                   /id="PRO_0000234313"
FT   DOMAIN          339..413
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   BINDING         83
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..193
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         56
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  47381 MW;  E71A3D6AB3A101B8 CRC64;
     MTVRTKVSTK DIDEAYLRLK NIVKETPLQF DHYLSQKYNC NVYLKREDLQ WVRSFKLRGA
     YNAISVLSNE EKNKGITCAS AGNHAQGVAY TAKKLNLKAV IFMPVTTPRQ KINQVKFFGD
     SNVEIVLIGD TFDHCLAQAL NYTKQHKMNF IDPFNNVYTI AGQGTLAKEI LNQAEKEDKT
     FDYVFAAIGG GGLISGVSTY FKAHSPHTKI IGVEPTGASS MYQSVVINHS IVTLENIDKF
     VDGASVARVG DITFDIAKDK VDDYVQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEQ
     YKKQIENKTI VCIVSGGNND INRMKEIEER SLLFEEMKHY FILNFPQRPG ALREFVNDVL
     GPQDDITKFE YLKKTSQNTG TVIIGIQLKH HDDLIQLKDR VCQFDPSNIY INENKMLYSL
     LI