ID   THD1_STAS1              Reviewed;         422 AA.
AC   Q49Z16;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Threonine dehydratase biosynthetic;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=SSP0817;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE17962.1; -; Genomic_DNA.
DR   RefSeq; YP_300907.1; -.
DR   GeneID; 3617339; -.
DR   GenomeReviews; AP008934_GR; SSP0817.
DR   KEGG; ssp:SSP0817; -.
DR   NMPDR; fig|342451.4.peg.1233; -.
DR   HOGENOM; Q49Z16; -.
DR   OMA; Q49Z16; IFMPTTT.
DR   BioCyc; SSAP342451:SSP0817-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_0000234315.
FT   MOD_RES      56     56       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   422 AA;  46840 MW;  4BADCC7143465109 CRC64;
     MTVKTTVSSK DIDEAYLQLK DIVKETPLQK DHYLSQKYDC KVYLKREDLQ WVRSFKLRGA
     YNAIIALDEA DRQNGITCAS AGNHAQGVAY TASKLNLNAV IFMPVTTPLQ KINQVKFFGG
     DNTEVVLTGD TFDDCLKEAL VYTEENKMNF IDPFNNIYTI AGQGTLAKEI LEQSKDNDIQ
     FDYLFAAIGG GGLISGVGTY FKTHSPETSI IGVEPAGAAS MYTSVVLENQ LVTLPDIDKF
     VDGASVARVG QITFDISKDI VDDYIQVHEG AVCSTILDMY SKQAIIAEPA GALSIAALDQ
     YQAEIKGKTV VCVVSGGNND INRMKEIEER SLLFEEMKHY FILNFPQRPG ALREFVNEVL
     GPKDDITKFE YLKKSSQNTG TVIIGIQLNN HKDLGHLKAN VDEFDKSNIY INENKMLYSL
     LI
//