DSD1_YEAST
ID DSD1_YEAST Reviewed; 428 AA.
AC P53095; D6VTV7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=D-serine dehydratase;
DE EC=4.3.1.18;
DE AltName: Full=D-serine deaminase;
DE Short=DSD;
GN Name=DSD1; OrderedLocusNames=YGL196W; ORFNames=G1315;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-387.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION OF FRAMESHIFTS.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17869212; DOI=10.1016/j.ab.2007.07.030;
RA Ito T., Takahashi K., Naka T., Hemmi H., Yoshimura T.;
RT "Enzymatic assay of D-serine using D-serine dehydratase from Saccharomyces
RT cerevisiae.";
RL Anal. Biochem. 371:167-172(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, HOMODIMERIZATION, COFACTOR, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17937657; DOI=10.1042/bj20070642;
RA Ito T., Hemmi H., Kataoka K., Mukai Y., Yoshimura T.;
RT "A novel zinc-dependent D-serine dehydratase from Saccharomyces
RT cerevisiae.";
RL Biochem. J. 409:399-406(2008).
CC -!- FUNCTION: Converts specifically D-serine to pyruvate and ammonia. May
CC play a role in D-serine detoxification. {ECO:0000269|PubMed:17869212,
CC ECO:0000269|PubMed:17937657}.
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:0000269|PubMed:17869212, ECO:0000269|PubMed:17937657};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17937657};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17937657};
CC -!- ACTIVITY REGULATION: Sodium cyanoborohydride, N-ethylmaleimide,
CC hydroxylamine, phenyhydrazin and EDTA are inhibitors of the catalytic
CC activity. {ECO:0000269|PubMed:17937657}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.39 mM for D-serine {ECO:0000269|PubMed:17937657};
CC KM=0.13 mM for D-threonine {ECO:0000269|PubMed:17937657};
CC KM=1.45 mM for beta-Cl-D-alanine {ECO:0000269|PubMed:17937657};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17937657};
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the DSD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA62948.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA96908.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X91837; CAA62948.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z72718; CAA96908.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY558389; AAS56715.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07918.1; -; Genomic_DNA.
DR PIR; S64213; S64213.
DR RefSeq; NP_011319.2; NM_001181061.1.
DR AlphaFoldDB; P53095; -.
DR SMR; P53095; -.
DR BioGRID; 33061; 95.
DR STRING; 4932.YGL196W; -.
DR MaxQB; P53095; -.
DR PaxDb; P53095; -.
DR PRIDE; P53095; -.
DR EnsemblFungi; YGL196W_mRNA; YGL196W; YGL196W.
DR GeneID; 852679; -.
DR KEGG; sce:YGL196W; -.
DR SGD; S000003164; DSD1.
DR VEuPathDB; FungiDB:YGL196W; -.
DR eggNOG; ENOG502QRZ0; Eukaryota.
DR HOGENOM; CLU_031639_0_0_1; -.
DR InParanoid; P53095; -.
DR OMA; WPRFYGW; -.
DR BioCyc; YEAST:G3O-30677-MON; -.
DR BRENDA; 4.3.1.18; 984.
DR SABIO-RK; P53095; -.
DR PRO; PR:P53095; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53095; protein.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IDA:SGD.
DR GO; GO:0036088; P:D-serine catabolic process; IBA:GO_Central.
DR GO; GO:0070178; P:D-serine metabolic process; IMP:SGD.
DR Gene3D; 2.40.37.20; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR026956; D-ser_dehydrat-like_dom.
DR InterPro; IPR042208; D-ser_dehydrat-like_sf.
DR InterPro; IPR029066; PLP-binding_barrel.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR Pfam; PF14031; D-ser_dehydrat; 1.
DR SMART; SM01119; D-ser_dehydrat; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
PE 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..428
FT /note="D-serine dehydratase"
FT /id="PRO_0000202722"
FT CONFLICT 125
FT /note="S -> R (in Ref. 1; CAA62948 and 2; CAA96908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 47828 MW; 0A068BA701FDA879 CRC64;
MSDVLSQYKG CSVRDLPTPN FVINEEKFDK NCTTMLNNVE KLSQECGVPI KFRAHVKTHK
TAKGTLKQLG HGLPLAKRTT RAILVSTLKE AEELLNYQDR QCSDYIDDIT YSLPCCVPEF
IPLLSNLSRR VNNFQVFVDN IEHLENLKNF GRPASGKKWS VFIKVDMGTK RAGLAFDSPE
FLSLLKKLTS SEIKEVIEPY GFYAHAGHSY SSTSINDTQN LLMEEVKAVN SAAKVLCSVD
PQFDPSKLTL SVGATPTSNS LKLDNKSTLV KFITTQLVST LEIHCGNYCM YDLQQVATGC
VQDHELSGFV LGTVLSSYPS RGELLSNTGV MCLTREASSI KGFGICADLE HVLKSESFSR
EWYVARVSQE HGILRPIRNW NETTPLKLGS KIAVLPQHAC ITMGQFPYYF VVNSEGIVND
VWLPFQKW
