ID   LCB2_SCHPO              Reviewed;         603 AA.
AC   Q09925;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 148.
DE   RecName: Full=Serine palmitoyltransferase 2;
DE            Short=SPT 2;
DE            EC=2.3.1.50;
DE   AltName: Full=Long chain base biosynthesis protein 2;
GN   Name=lcb2; ORFNames=SPAC21E11.08, SPAC2C4.02;
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 [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8921873; DOI=10.1016/0378-1119(96)00309-5;
RA   Nagiec M.M., Lester R.L., Dickson R.C.;
RT   "Sphingolipid synthesis: identification and characterization of mammalian
RT   cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase.";
RL   Gene 177:237-241(1996).
RN   [2]
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   [3]
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: Catalytic subunit 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}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- SUBUNIT: Lcb1 and lcb2 encode essential subunits of the enzyme and form
CC       a heterodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U15645; AAC49534.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA91967.2; -; Genomic_DNA.
DR   PIR; JC5183; JC5183.
DR   RefSeq; XP_001713103.1; XM_001713051.2.
DR   AlphaFoldDB; Q09925; -.
DR   SMR; Q09925; -.
DR   BioGRID; 280491; 4.
DR   STRING; 4896.SPAC21E11.08.1; -.
DR   iPTMnet; Q09925; -.
DR   MaxQB; Q09925; -.
DR   PaxDb; Q09925; -.
DR   EnsemblFungi; SPAC21E11.08.1; SPAC21E11.08.1:pep; SPAC21E11.08.
DR   PomBase; SPAC21E11.08; lcb2.
DR   VEuPathDB; FungiDB:SPAC21E11.08; -.
DR   eggNOG; KOG1357; Eukaryota.
DR   HOGENOM; CLU_015846_7_2_1; -.
DR   InParanoid; Q09925; -.
DR   OMA; IEDEPPY; -.
DR   PhylomeDB; Q09925; -.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:Q09925; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017059; C:serine C-palmitoyltransferase complex; ISO:PomBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004758; F:serine C-palmitoyltransferase activity; ISO:PomBase.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
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   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 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..603
FT                   /note="Serine palmitoyltransferase 2"
FT                   /id="PRO_0000163861"
FT   TRANSMEM        90..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         398
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   603 AA;  67519 MW;  251A2383CC9B8472 CRC64;
     MAQADFVSPT SIDVSEKKEV EFHKKVDHVE NPPLSTESAK LEAEEVAAEK LNSEHLLENE
     FAPITDPTHR RVSKNPDGAE LFQFEDEPSY YYVVATYLTY LVLIIIGHVR DFFGKRFHKD
     DYKYLKDNDG YAPLYNHFDN FYVRRLQHRI NDCFSRPTMG VPGRVIRLMN RYSTDSNSTF
     KLTGDTSLAL NVSSYNYLGF AQSHGPCATK VEEAMQKYGL STCSSNAICG TYGLHKEVEE
     LTANFVGKPA ALVFSQGFST NATVFSTLMC PGSLIISDEL NHTSIRFGAR LSGANIRVYK
     HNDMTDLERV LREVISQGQP RTHRPYSKIL VVIEGLYSME GNFCDLPKVV ELKNRYKFYL
     FIDEAHSIGA IGPRGGGICD YFGISTDHVD ILMGTFTKSF GAAGGYISAT PNIINKLRVT
     NPGYVYAESM SPAVLAQIKS SFLEIMDNSP TSAGLERIER LAFNSRYIRL GLKRLGFIIF
     GNDDSPVVPL LLYNPGKINA FSHEMLKRGI AVVVVGYPAC PLLTSRVRFC FSASHNKADM
     DYFLRACDEV GEKLQLKFST GAAGEDVGKT NVEKMKKNQG WFKPPRWKIE DVLKHGVHDA
     LTQ