ID   SGPL_YEAST              Reviewed;         589 AA.
AC   Q05567;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Sphingosine-1-phosphate lyase;
DE            Short=SP-lyase;
DE            Short=ySPL;
DE            EC=4.1.2.27;
DE   AltName: Full=Sphingosine-1-phosphate aldolase;
DE   AltName: Full=Bestowed of sphingosine tolerance 1;
GN   Name=DPL1; Synonyms=BST1; OrderedLocusNames=YDR294C; ORFNames=D9819.5;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   FUNCTION.
RX   MEDLINE=97476195; PubMed=9334171; DOI=10.1074/jbc.272.42.26087;
RA   Saba J.D., Nara F., Bielawska A., Garrett S., Hannun Y.A.;
RT   "The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-
RT   phosphate lyase.";
RL   J. Biol. Chem. 272:26087-26090(1997).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as
CC       sphingosine-1-phosphate, into fatty aldehydes and
CC       phosphoethanolamine.
CC   -!- CATALYTIC ACTIVITY: Sphinganine 1-phosphate = phosphoethanolamine
CC       + palmitaldehyde.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- MISCELLANEOUS: Present with 13100 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       Sphingosine-1-phosphate lyase subfamily.
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DR   EMBL; U51031; AAB64470.1; -; Genomic_DNA.
DR   PIR; S70123; S70123.
DR   RefSeq; NP_010580.1; -.
DR   IntAct; Q05567; 2.
DR   PeptideAtlas; Q05567; -.
DR   Ensembl; YDR294C; Saccharomyces cerevisiae.
DR   GeneID; 851888; -.
DR   GenomeReviews; Z71256_GR; YDR294C.
DR   KEGG; sce:YDR294C; -.
DR   NMPDR; fig|4932.3.peg.1342; -.
DR   CYGD; YDR294c; -.
DR   SGD; S000002702; DPL1.
DR   HOGENOM; Q05567; -.
DR   OMA; Q05567; IIAACWA.
DR   BRENDA; 4.1.2.27; 250.
DR   NextBio; 969868; -.
DR   GermOnline; YDR294C; Saccharomyces cerevisiae.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IDA:SGD.
DR   GO; GO:0019722; P:calcium-mediated signaling; IMP:SGD.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:SGD.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IGI:SGD.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11999; Pyridoxal_deC; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Complete proteome; Lyase; Pyridoxal phosphate.
FT   CHAIN         1    589       Sphingosine-1-phosphate lyase.
FT                                /FTId=PRO_0000147018.
FT   MOD_RES     380    380       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   589 AA;  65566 MW;  75FAF8182AF72266 CRC64;
     MSGVSNKTVS INGWYGMPIH LLREEGDFAQ FMILTINELK IAIHGYLRNT PWYNMLKDYL
     FVIFCYKLIS NFFYLLKVYG PVRLAVRTYE HSSRRLFRWL LDSPFLRGTV EKEVTKVKQS
     IEDELIRSDS QLMNFPQLPS NGIPQDDVIE ELNKLNDLIP HTQWKEGKVS GAVYHGGDDL
     IHLQTIAYEK YCVANQLHPD VFPAVRKMES EVVSMVLRMF NAPSDTGCGT TTSGGTESLL
     LACLSAKMYA LHHRGITEPE IIAPVTAHAG FDKAAYYFGM KLRHVELDPT TYQVDLGKVK
     KFINKNTILL VGSAPNFPHG IADDIEGLGK IAQKYKLPLH VDSCLGSFIV SFMEKAGYKN
     LPLLDFRVPG VTSISCDTHK YGFAPKGSSV IMYRNSDLRM HQYYVNPAWT GGLYGSPTLA
     GSRPGAIVVG CWATMVNMGE NGYIESCQEI VGAAMKFKKY IQENIPDLNI MGNPRYSVIS
     FSSKTLNIHE LSDRLSKKGW HFNALQKPVA LHMAFTRLSA HVVDEICDIL RTTVQELKSE
     SNSKPSPDGT SALYGVAGSV KTAGVADKLI VGFLDALYKL GPGEDTATK
//