ID   LCB1_SCHPO              Reviewed;         509 AA.
AC   O59682;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Serine palmitoyltransferase 1;
DE            Short=SPT 1;
DE            Short=SPT1;
DE            EC=2.3.1.50;
DE   AltName: Full=Long chain base biosynthesis protein 1;
GN   Name=lcb1 {ECO:0000250|UniProtKB:P25045};
GN   ORFNames=SPBC18E5.02c, SPBC29A3.20c;
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] {ECO:0000312|EMBL:CAA18397.1}
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] {ECO:0000305}
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: Component of serine palmitoyltransferase (SPT), which
CC       catalyzes the committed step in the synthesis of sphingolipids, the
CC       condensation of serine with palmitoyl CoA to form the long chain base
CC       3-ketosphinganine. {ECO:0000250|UniProtKB:P25045}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC         CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:58299; EC=2.3.1.50;
CC         Evidence={ECO:0000250|UniProtKB:P25045};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P25045};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000250|UniProtKB:P25045}.
CC   -!- SUBUNIT: Lcb1 and lcb2 encode essential subunits of the enzyme and form
CC       a heterodimer. {ECO:0000250|UniProtKB:P25045}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25045,
CC       ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
CC       Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
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DR   EMBL; CU329671; CAA18397.1; -; Genomic_DNA.
DR   PIR; T39753; T39753.
DR   RefSeq; NP_595848.1; NM_001021752.2.
DR   AlphaFoldDB; O59682; -.
DR   SMR; O59682; -.
DR   BioGRID; 277338; 2.
DR   STRING; 284812.O59682; -.
DR   iPTMnet; O59682; -.
DR   MaxQB; O59682; -.
DR   PaxDb; 4896-SPBC18E5-02c-1; -.
DR   EnsemblFungi; SPBC18E5.02c.1; SPBC18E5.02c.1:pep; SPBC18E5.02c.
DR   GeneID; 2540820; -.
DR   KEGG; spo:SPBC18E5.02c; -.
DR   PomBase; SPBC18E5.02c; lcb1.
DR   VEuPathDB; FungiDB:SPBC18E5.02c; -.
DR   eggNOG; KOG1358; Eukaryota.
DR   HOGENOM; CLU_015846_0_2_1; -.
DR   InParanoid; O59682; -.
DR   OMA; LTKYGCG; -.
DR   PhylomeDB; O59682; -.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:O59682; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035339; C:SPOTS complex; ISO:PomBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004758; F:serine C-palmitoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   PANTHER; PTHR13693:SF2; SERINE PALMITOYLTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Endoplasmic reticulum; Lipid metabolism;
KW   Membrane; Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Serine palmitoyltransferase 1"
FT                   /id="PRO_0000309453"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   509 AA;  57469 MW;  26BC0BE6AA6D16A7 CRC64;
     MSYSYPFFDD VYAYYNQTVT FFGKALDVLP GSPIVKRYIK SSYQNDPLRT FIEFLLLVFA
     AYYVLRKPRT SPDNNYVEFT EKEINELVDD WKPEPLVAEL TDVEKLELKS IPVLESVHLH
     TKLIDGRPIT NFASFNFLDL AENKHITECA VATLRECGLG ACGPPGFYGT QDKHLRLEKD
     IASFIGVERA IVYAQSFQTI SSVIPAFSKR GDILVVDEAC NFAIQKGIQI SRTTIRYFKH
     NNMKDLERIL QELEDDFVKH NRPLTRRFII TEGISENYGD MVDLTKIVAL KKKYKYRLIL
     DETWSFGTCG RTGKGLTEHF GVPPTDVEII IGSLTTSLAG GGGFCAGSEL MVEHQRLSGM
     AYIYSAALPA SLAVAAYEAI SILSRDGGSM LNDLRSKSAL FHAKLSRNKF FETSSDIESP
     IIHLRFKDKD ISHDKQVFLL EEIVELCIAE GFLIARAKRV ESLERVKVQP SLRICISTGH
     SAEEIEKLAL LIKEKTEIVF DKHKVINQV
//