ID SDHD2_ECOL5 Reviewed; 442 AA. AC Q0T953; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=D-serine dehydratase 2; DE EC=4.3.1.18; DE AltName: Full=D-serine deaminase 2; DE Short=DSD 2; GN Name=dsdA2; OrderedLocusNames=ECP_4590; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). CC -!- CATALYTIC ACTIVITY: D-serine = pyruvate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. CC DsdA subfamily. 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; CP000247; ABG72526.1; -; Genomic_DNA. DR RefSeq; YP_672427.1; -. DR GeneID; 4189078; -. DR GenomeReviews; CP000247_GR; ECP_4590. DR KEGG; ecp:ECP_4590; -. DR NMPDR; fig|340197.3.peg.812; -. DR HOGENOM; Q0T953; -. DR OMA; Q0T953; DHPLFVY. DR BioCyc; ECOL362663:ECP_4590-MON; -. DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:EC. DR GO; GO:0016836; F:hydro-lyase activity; IEA:HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:HAMAP. DR HAMAP; MF_01030; -; 1. DR InterPro; IPR011780; D_Ser_am_lyase. DR InterPro; IPR001926; PyrdxlP-dep_enz_bsu. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR PANTHER; PTHR10314:SF9; D_Ser_am_lyase; 1. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR02035; D_Ser_am_lyase; 1. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Pyridoxal phosphate. FT CHAIN 1 442 D-serine dehydratase 2. FT /FTId=PRO_0000291730. FT MOD_RES 118 118 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 442 AA; 47881 MW; 9EE4AFA3FCC96D7F CRC64; MENAKMNSLI AQYPLVKDLV ALKETTWFNP GTTSLAEGLP YVGLTEQDVQ DAHARLSRFA PYLAKAFPET AATGGIIESE LVAIPAMQKR LEKEYQQPIS GQLLLKKDSH LPISGSIKAR GGIYEVLAHA EKLALEAGLL TLEDDYSKLL SPEFKQFFSQ YSIAVGSTGN LGLSIGIMSA RIGFKVTVHM SADARAWKKA KLRSHGVTVV EYEQDYGVAV EEGRKAAQSD PNCFFIDDEN SRTLFLGYSV AGQRLKAQFA QQGRIVDADN PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH CFFAEPTHSP CMLLGVHTGL HDQISVQDIG IDNLTAADGL AVGRASGFVG RAMERLLDGF YTLSDQTMYD MLGWLAQEEG IRLEPSALAG MAGPQRVCAS VSYQQMHGFS AEQLRNATHL VWATGGGMVP EEEMEQYLAK GH //