ID   THD1_STAAS              Reviewed;         422 AA.
AC   Q3V7T4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Threonine dehydratase biosynthetic;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=SAS1966;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG43773.1; -; Genomic_DNA.
DR   RefSeq; YP_044076.1; -.
DR   GeneID; 2861792; -.
DR   GenomeReviews; BX571857_GR; SAS1966.
DR   KEGG; sas:SAS1966; -.
DR   HOGENOM; Q3V7T4; -.
DR   OMA; Q3V7T4; IFMPTTT.
DR   BioCyc; SAUR282459:SAS1966-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_0000234310.
FT   MOD_RES      56     56       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   422 AA;  46967 MW;  D57A860757C56CD5 CRC64;
     MTVKTTVSTK DIDEAFLRLK DIVKETPLQL DHYLSQKYDC KVYLKREDLQ WVRSFKLRGA
     YNAISVLSDE AKSKGITCAS AGNHAQGVAY TAKKLNLNAV IFMPVTTPLQ KVNQVKFFGN
     SNVEVVLTGD TFDHCLAEAL TYTSEHQMNF IDPFNNVHTI SGQGTLAKEM LEQSKTDNVN
     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
//