ID   SDHD_COLP3              Reviewed;         443 AA.
AC   Q47V69;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=CPS_4659;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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.
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; CP000083; AAZ26608.1; -; Genomic_DNA.
DR   RefSeq; YP_271303.1; -.
DR   GeneID; 3520861; -.
DR   GenomeReviews; CP000083_GR; CPS_4659.
DR   KEGG; cps:CPS_4659; -.
DR   NMPDR; fig|167879.3.peg.3937; -.
DR   TIGR; CPS_4659; -.
DR   HOGENOM; Q47V69; -.
DR   OMA; Q47V69; DHPLFVY.
DR   BioCyc; CPSY167879:CPS_4659-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    443       Probable D-serine dehydratase.
FT                                /FTId=PRO_0000291724.
FT   MOD_RES     118    118       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   443 AA;  48450 MW;  CD37FF43949757BD CRC64;
     MNNDNIAQLI ADFPLIEKMV ELKEVSWFNP NITSLQEGLP YVGLDNNNIQ DASDRLARFA
     PYMVKAFPET AITNGIIESD VVEISAMKSQ LEQQYEVEIQ GKLLLKKDSH LPISGSIKAR
     GGIYEVLTHA EQLAIKAEVL ELSDDYSKLF TEEFKSFFSQ YSIAVGSTGN LGMSIGIMSA
     KLGFSVSVHM SADARQWKKE KLRAHGVNVV EYNEDYSVAV EQGRQEAEND PKCFFIDDEN
     SQTLFLGYSV AGERLKQQFD AMHIVVDENN PLFVYLPCGV GGGPGGVAFG LKMAFGDNVH
     CIFAEPTHSP CMLLGILTGL HDGIAVQDIG IDNITAADGL AVGRASGFVG RAMERLLDGF
     YTISDQRMYD LLGLLNKVEG IQLEPSALAG MLGPIVVTNN DEYLKRINMS NEKLVNATHL
     IWATGGGMVP AIEMEKYLSK AGS
//