ID THD2_STAA3 Reviewed; 346 AA. AC Q2FH01; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Threonine dehydratase catabolic; DE EC=4.3.1.19; DE AltName: Full=Threonine deaminase; GN Name=tdcB; OrderedLocusNames=SAUSA300_1330; OS Staphylococcus aureus (strain USA300). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). CC -!- FUNCTION: Acts on both serine and threonine, and properly CC considered as a hydroxy amino acid deaminase (By similarity). CC -!- CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via CC propanoate pathway; propanoate from L-threonine: step 1/4. CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000255; ABD20948.1; -; Genomic_DNA. DR RefSeq; YP_494027.1; -. DR GeneID; 3913061; -. DR GenomeReviews; CP000255_GR; SAUSA300_1330. DR KEGG; saa:SAUSA300_1330; -. DR HOGENOM; Q2FH01; -. DR OMA; Q2FH01; IRGALNF. 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:0006520; P:amino acid metabolic process; IEA:InterPro. DR InterPro; IPR001926; PyrdxlP-dep_enz_bsu. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR005789; Thr_deHydtase_2. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01127; ilvA_1Cterm; 1. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Pyridoxal phosphate. FT CHAIN 1 346 Threonine dehydratase catabolic. FT /FTId=PRO_0000287334. FT MOD_RES 64 64 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 346 AA; 37306 MW; A69CB839024C9C5F CRC64; MTTNTVTLQT AHIVSLGDIE EAKASIKPFI RRTPLIKSMY LSQSITKGNV FLKLENMQFT GSFKFRGASN KINHLTDEQK EKGIIAASAG NHAQGVALTA KLLGIDATIV MPETAPQAKQ QATKGYGAKV ILKGKNFNET RLYMEELAKE NGMTIVHPYD DKFVMAGQGT IGLEILDDIW NVNTVIVPVG GGGLIAGIAT ALKSFNPSIH IIGVQSENVH GMAESFYKRD LTEHRVDSTI ADGCDVKVPG EQTYEVVKHL VDEFILVTEE EIEHAMKDLM QRAKIITEGA GALPTAAILS GKINNKWLED KNVVALVSGG NVDLTRVSGV IEHGLNIADT SKGVVG //