ID   LCB2_KLULA              Reviewed;         562 AA.
AC   P48241; Q6CSC6;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   25-MAY-2022, entry version 123.
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; OrderedLocusNames=KLLA0D02134g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96263 / JA6;
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=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U15646; AAC49535.1; -; Genomic_DNA.
DR   EMBL; CR382124; CAH00259.1; -; Genomic_DNA.
DR   PIR; JC5182; JC5182.
DR   RefSeq; XP_453163.1; XM_453163.1.
DR   AlphaFoldDB; P48241; -.
DR   SMR; P48241; -.
DR   STRING; 28985.XP_453163.1; -.
DR   EnsemblFungi; CAH00259; CAH00259; KLLA0_D02134g.
DR   GeneID; 2892894; -.
DR   KEGG; kla:KLLA0_D02134g; -.
DR   eggNOG; KOG1357; Eukaryota.
DR   HOGENOM; CLU_015846_7_2_1; -.
DR   InParanoid; P48241; -.
DR   OMA; IEDEPPY; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035339; C:SPOTS complex; IEA:EnsemblFungi.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004758; F:serine C-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:EnsemblFungi.
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; Lipid metabolism; Membrane; Pyridoxal phosphate;
KW   Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..562
FT                   /note="Serine palmitoyltransferase 2"
FT                   /id="PRO_0000163860"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         365
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        191
FT                   /note="G -> V (in Ref. 1; AAC49535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        492
FT                   /note="S -> L (in Ref. 1; AAC49535)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   562 AA;  62937 MW;  A23388A0BB681B1D CRC64;
     MISISSTRVP LIPPEDIPLE DKKENEFGQL TSEEYLYQSK SRDGKALQDP ILDAPAYHVS
     LITYLNYLIL IILGHIHDFL GLTFQKEKHK DIMEQDGLAP WFSTFESFYV RRLKQRIDDC
     FSRPTTGVPG RFIRCLDRVS HNLNDYFTYP GTTSMCLNLS SYNYLGFAQS EGQCTTAALE
     ATDKYGVYSG GPRTRIGTTD LHVMTEKYVA QFVGKEDAIL FSMGYGTNAN FFNSFLDSKC
     LVISDSLNHT SIRTGVRLSG AAVKTFKHND MRALEKLIRE QIVQGQSKTH RPWKKIIICV
     EGLYSMEGTM ANLPKLVELK KKYKCYLFVD EAHSIGAMGP SGRGVCDFFG IPCSDIDIMM
     GTLTKSFGAA GGYIAADKWI IDRFRLDLTT PHYGEPTPAP VLAQIASSLK TITGDINPGE
     GQERLQRIAF NARYLRLALQ RLGFIVYGIA DSPVIPMLLY APSKMPAFSR MMLQRKIAVV
     VVAYPATPLI ESRVRFCVSA ALTKEDIDYL LQHINEVGDK LFLKVSSGKA GGSLDGKPPR
     WNIDEVIKRT PTDCKDDSFF RI