ID SDHD_ECO81 Reviewed; 442 AA.
AC B7MY25;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 29.
DE RecName: Full=D-serine dehydratase;
DE EC=4.3.1.18;
DE AltName: Full=D-serine deaminase;
DE Short=DSD;
GN Name=dsdA; OrderedLocusNames=ECED1_2813;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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.
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DR EMBL; CU928162; CAR08991.2; -; Genomic_DNA.
DR RefSeq; YP_002398721.1; NC_011745.1.
DR ProteinModelPortal; B7MY25; -.
DR EnsemblBacteria; CAR08991; CAR08991; ECED1_2813.
DR GeneID; 7140527; -.
DR KEGG; ecq:ECED1_2813; -.
DR PATRIC; 38489650; VBIEscCol8292_2818.
DR eggNOG; COG3048; -.
DR HOGENOM; HOG000218072; -.
DR KO; K01753; -.
DR OMA; HCLFAEP; -.
DR ProtClustDB; PRK02991; -.
DR BioCyc; ECOL585397:GJCU-2845-MONOMER; -.
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; D-Ser_dehydrat; 1; -.
DR InterPro; IPR011780; D_Ser_am_lyase.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
DR PANTHER; PTHR10314:SF9; PTHR10314:SF9; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 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.
FT /FTId=PRO_1000149388.
FT MOD_RES 118 118 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 442 AA; 47837 MW; 19AEB9B1CA573271 CRC64;
MENAKMNSLI AQYPLVEDLV ALKETTWFNP GTTSLAEGLP YVGLTEQDVQ DAHARLSRFA
PYLAKAFPET AAAGGIIESE 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 VSYQQLHGFS AEQLRNATHL
VWATGGGMVP EEEMNQYLAK GR
//
