SDHD_PEDPA
ID SDHD_PEDPA Reviewed; 432 AA.
AC Q03DF6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Probable 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}; OrderedLocusNames=PEPE_1745;
OS Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS 183-1w).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=278197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., 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:
CC Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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DR EMBL; CP000422; ABJ68766.1; -; Genomic_DNA.
DR RefSeq; WP_011673850.1; NC_008525.1.
DR AlphaFoldDB; Q03DF6; -.
DR SMR; Q03DF6; -.
DR STRING; 278197.PEPE_1745; -.
DR EnsemblBacteria; ABJ68766; ABJ68766; PEPE_1745.
DR GeneID; 33061818; -.
DR KEGG; ppe:PEPE_1745; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_9; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
DR Proteomes; UP000000773; Chromosome.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_01030; D_Ser_dehydrat; 1.
DR InterPro; IPR011780; D_Ser_am_lyase.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR48078:SF9; PTHR48078: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 Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..432
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000291735"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 432 AA; 47549 MW; 7A8FACDFC887413F CRC64;
MIDVDALSKK YPAIKQMQAY EPIFWKNLNY KKEAELPVGV EHIFDAEARF QRFAPYFEVA
FPETLPTHGI LESPLLKMDK MKAVLNAEAQ NQVKGDLYLK ADNYLPISGS IKSRGGIYEV
LKFAEKVAMK HGEIVYGDNY AKLNEPRFKD LFGQYGIVVG STGNLGLSIG IVACKLGFRT
SVHMSSDAAQ WKKDMLREKG VNVVEYNDNF THAITEARKS AEADPMAYFI DDEGSYDLFL
GYSVAAVRLQ AQLKAQNIKV DAEHPLFVYL PAGVGGSPSG VAFGLKKIIG ENVHPIFAEP
THIPSVSLGM MTGLNDQISV YDAGIDGVTK ADGLAVGRPS RIAGKMMDTL LYGIQTFDDQ
KMMKNVAELH DSENVDVEPS AASGFTILDD VQAQLEQDYP MENASHIVWA TGGSMVPKND
MDQYVAEGHQ VK