ID   THD1_STAHJ              Reviewed;         422 AA.
AC   Q4L7U4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Threonine dehydratase biosynthetic;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=SH0972;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04281.1; -; Genomic_DNA.
DR   RefSeq; YP_252887.1; -.
DR   GeneID; 3482161; -.
DR   GenomeReviews; AP006716_GR; SH0972.
DR   KEGG; sha:SH0972; -.
DR   NMPDR; fig|279808.3.peg.1404; -.
DR   HOGENOM; Q4L7U4; -.
DR   OMA; Q4L7U4; IFMPTTT.
DR   BioCyc; SHAE279808:SH0972-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_0000234314.
FT   MOD_RES      56     56       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   422 AA;  46986 MW;  6CA7388A563960E0 CRC64;
     MTVKTTLNAK DVDNAYLRIK DVVKETPLQF DLYLSQKYDC NVYLKREDLQ WVRSFKLRGA
     YNAISVLTSE AKEKGITCAS AGNHAQGVAY TAKALNLKAV IFMPVTTPLQ KVNQVKFFGS
     KNVKIILTGD TFDDCLKEAL IYTEQNHMTF IDPFNNVDTI AGQGTLAKEI LNQSSNDSIT
     FDYLFAAIGG GGLISGISTY MNQYSPQTKI IGVEPSGASS MYESVVVQNK IVTLDHIDKF
     VDGASVARVG DITYDIAKKF VDDYIQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEQ
     YKEKIKGKTV VCVVSGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG ALKEFVNDVL
     GPQDDITKFE YLKKTSQNTG TVIIGIQLKN HDDLNQLKIN VHDFDPSNIY INENKMLYSL
     LI
//