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Database: UniProt
Entry: B7MY25
LinkDB: B7MY25
Original site: B7MY25 
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   29-OCT-2014, entry version 36.
DE   RecName: Full=D-serine dehydratase {ECO:0000255|HAMAP-Rule:MF_01030};
DE            EC=4.3.1.18 {ECO:0000255|HAMAP-Rule:MF_01030};
DE   AltName: Full=D-serine deaminase {ECO:0000255|HAMAP-Rule:MF_01030};
DE            Short=DSD {ECO:0000255|HAMAP-Rule:MF_01030};
GN   Name=dsdA {ECO:0000255|HAMAP-Rule:MF_01030};
GN   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       {ECO:0000255|HAMAP-Rule:MF_01030}.
CC   -!- COFACTOR: Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_01030}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01030}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       DsdA subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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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; ESDPNCF; -.
DR   OrthoDB; EOG6HXJ23; -.
DR   BioCyc; ECOL585397:GJCU-2845-MONOMER; -.
DR   GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-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; TrpB-like_PLP-dep.
DR   PANTHER; PTHR10314:SF9; PTHR10314:SF9; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 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.
FT                                {ECO:0000255|HAMAP-Rule:MF_01030}.
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
//
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