ID   SDHD_OENOB              Reviewed;         433 AA.
AC   Q04G28;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Probable D-serine dehydratase;
DE            EC=4.3.1.18;
DE   AltName: Full=D-serine deaminase;
DE            Short=DSD;
GN   Name=dsdA; OrderedLocusNames=OEOE_0657;
OS   Oenococcus oeni (strain BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Lactobacillales; Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- CATALYTIC ACTIVITY: D-serine = pyruvate + NH(3).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       DsdA subfamily.
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DR   EMBL; CP000411; ABJ56594.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_810259.1; -.
DR   GeneID; 4416798; -.
DR   GenomeReviews; CP000411_GR; OEOE_0657.
DR   KEGG; ooe:OEOE_0657; -.
DR   NMPDR; fig|203123.1.peg.535; -.
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    433       Probable D-serine dehydratase.
FT                                /FTId=PRO_0000291734.
FT   MOD_RES     110    110       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   433 AA;  48272 MW;  C36355D401651420 CRC64;
     MTETLLKKKL NLNDQFLLNL KNYQEIFWKN PNYGDELPDL DVNRETIFQA NRRLERFAPY
     LESVFSDTKR SKGIIESPIQ RMDSIKDLLS VKGSLLIKRD DLMPVSGSIK SRGGIYEVLC
     FAEKIAIENG FDLKKDNYQD LRKDKYRKLF NQWRIEVAST GNLGLSVGLM ASTLGFKARI
     HMSHDATDWK INKLLQNGVE VKIYDDNFSN AVAAARVSSQ RDPYSYFIDD EGSKLLFAGY
     ATAGERVKKQ LSKMQIEVSK EHPLVVYLPA GVGGSPSGVA FGLKLQFADA VIPIFVEPTH
     MPSVLLGMAS GLNHDISVYD IGIDGKTAAD GLAVGRPSMI AGKYMKDKLF GIATVSDSDM
     FAYQGMLKKL ENIEVEPSAA VGIRGLIQSK EISEIPDSAT HMVWATGGSM VPKNTMHKYE
     DKAVRIFNTW KSE
//