DSD1_SCHPO
ID DSD1_SCHPO Reviewed; 415 AA.
AC Q9US35;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=D-serine dehydratase;
DE EC=4.3.1.18;
DE AltName: Full=D-serine deaminase;
DE Short=DSD;
GN ORFNames=SPAC1039.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Converts specifically D-serine to pyruvate and ammonia. May
CC play a role in D-serine detoxification (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DSD1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB63542.1; -; Genomic_DNA.
DR PIR; T50056; T50056.
DR RefSeq; NP_594997.1; NM_001020428.2.
DR AlphaFoldDB; Q9US35; -.
DR SMR; Q9US35; -.
DR BioGRID; 279434; 3.
DR STRING; 4896.SPAC1039.06.1; -.
DR MaxQB; Q9US35; -.
DR PaxDb; Q9US35; -.
DR EnsemblFungi; SPAC1039.06.1; SPAC1039.06.1:pep; SPAC1039.06.
DR GeneID; 2542996; -.
DR KEGG; spo:SPAC1039.06; -.
DR PomBase; SPAC1039.06; -.
DR VEuPathDB; FungiDB:SPAC1039.06; -.
DR eggNOG; ENOG502QRZ0; Eukaryota.
DR HOGENOM; CLU_031639_0_0_1; -.
DR InParanoid; Q9US35; -.
DR OMA; WPRFYGW; -.
DR PhylomeDB; Q9US35; -.
DR PRO; PR:Q9US35; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; ISM:PomBase.
DR GO; GO:0036088; P:D-serine catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Lyase; Nucleus; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..415
FT /note="D-serine dehydratase"
FT /id="PRO_0000317093"
SQ SEQUENCE 415 AA; 45647 MW; 31234FC8BFDFBAC3 CRC64;
MASNVDKFSS RFYLNVNKEE LKKEYVGKTI QQVPTPGFVI DEAIFEKNCN RMLDRASDIG
VTFRAHVKTH KTIEGTLLQL GDGRTKAVVV STLMEGFSLI PLILEGKIDD LLYGLPVAKS
RLPELYELSK IVPHLRLMID NPKQLDILRE FTSTLPDDAK PWSIFVKIDM GTHRAGVTND
SQVVKDLIST ILSDKSLFDL FGFYCHAGHS YASRSIDAAS EFLCAEIDAA NTAAKFATSI
DPSLKLTLSV GATPTAHSVS PKVKELLPTL SGKLEVHAGN YPMNDVQQMI TKCISQADVA
DYVFAEVISN YPGRNGEPGE VLVNAGVIAM SRETSPEGDF GIVITPGFES FYVDRLSQEH
GILKSKDPKA TLPDASQVLC IIPNHSCITA AAFPWYYITK GSDVITDIWV PWKGW
