ID   THD1_STAA8              Reviewed;         422 AA.
AC   Q2FWJ9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Threonine dehydratase biosynthetic;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=SAOUHSC_02289;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC8325 genome.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of alpha-ketobutyrate from
CC       threonine in a two-step reaction. The first step is a dehydration
CC       of threonine, followed by rehydration and liberation of ammonia
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH(3).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
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DR   EMBL; CP000253; ABD31327.1; -; Genomic_DNA.
DR   RefSeq; YP_500771.1; -.
DR   GeneID; 3919164; -.
DR   GenomeReviews; CP000253_GR; SAOUHSC_02289.
DR   KEGG; sao:SAOUHSC_02289; -.
DR   HOGENOM; Q2FWJ9; -.
DR   OMA; Q2FWJ9; IFMPTTT.
DR   BioCyc; SAUR93061:SAOUHSC_02289-MON; -.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001926; PyrdxlP-dep_enz_bsu.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001721; Thr_deHydtase_C.
DR   InterPro; IPR011820; Threonine_deHydtase.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 1.
DR   TIGRFAMs; TIGR02079; THD1; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Isoleucine biosynthesis; Lyase;
KW   Pyridoxal phosphate.
FT   CHAIN         1    422       Threonine dehydratase biosynthetic.
FT                                /FTId=PRO_0000287209.
FT   MOD_RES      56     56       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   422 AA;  46937 MW;  A1A085175DA56D90 CRC64;
     MTVKTTVSTK DIDEAFLRLK DIVKETPLQL DHYLSQKYDC KVYLKREDLQ WVRSFKLRGA
     YNAISVLSDE AKSKGITCAS AGNHAQGVAY TAKKLNLNAV IFMPVTTPLQ KVNQVKFFGN
     SNVEVVLTGD TFDHCLAEAL TYTSEHQMNF IDPFNNVHTI SGQGTLAKEM LEQAKSDNVN
     FDYLFAAIGG GGLISGISTY FKTYSPTTKI IGVEPSGASS MYESVVVNNQ VVTLPNIDKF
     VDGASVARVG DITFEIAKEN VDDYVQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEN
     YKDHIKGKTV VCVISGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG ALREFVNDVL
     GPQDDITKFE YLKKSSQNTG TVIIGIQLKD HDDLIQLKQR VNHFDPSNIY INENKMLYSL
     LI
//