ID   A7TED3_VANPO            Unreviewed;       562 AA.
AC   A7TED3;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   10-JUN-2026, entry version 78.
DE   RecName: Full=serine C-palmitoyltransferase {ECO:0000256|ARBA:ARBA00013220};
DE            EC=2.3.1.50 {ECO:0000256|ARBA:ARBA00013220};
GN   ORFNames=Kpol_1002p104 {ECO:0000313|EMBL:EDO19455.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|EMBL:EDO19455.1, ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO19455.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine + hexadecanoyl-CoA + H(+) = 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:0000256|ARBA:ARBA00048528};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008392,
CC       ECO:0000256|RuleBase:RU003693}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS480379; EDO19455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7TED3; -.
DR   FunCoup; A7TED3; 409.
DR   STRING; 436907.A7TED3; -.
DR   KEGG; vpo:Kpol_1002p104; -.
DR   eggNOG; KOG1357; Eukaryota.
DR   HOGENOM; CLU_015846_7_2_1; -.
DR   InParanoid; A7TED3; -.
DR   OMA; QPRANGC; -.
DR   OrthoDB; 65434at2759; -.
DR   PhylomeDB; A7TED3; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017059; C:serine palmitoyltransferase 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:0046513; P:ceramide biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd06454; KBL_like; 1.
DR   FunFam; 3.40.640.10:FF:000047; serine palmitoyltransferase 2 isoform X1; 1.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR050087; AON_synthase_class-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:SF3; LD36009P; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          156..513
FT                   /note="Aminotransferase class I/classII large"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   562 AA;  63273 MW;  E8C8F9D0CE0D4A23 CRC64;
     MSDFGSRQVP LIPPEILPIE VKRENEYGTL TSKRYLYNVK SLNGKSLKPP ILDTPPYHIS
     LITYLNYLIL IILGHIHDFL GLKFQRDKHL DIVEQNGYAP WFSKFESFYV RRLKKRIDDC
     FSRPTTGVPG RFIRCIDRVS HDFNEYFTYN GKTTMCLNLS SYNYLGFAQS EGQCTDAAID
     TVRKYGINVG GPRSQSGTTD LHIEAENLIA NFLGKEDAMV FSMGYGTNAN FFNSFLDSKC
     LVISDELNHT SIRTGVRSSG AAVRTFKHND MKALEKIIRE QIVIGQPKTN RPWKKIIICV
     EGLYSMEGTL CNLPDLIALK KKYKCYLYVD EAHSIGAMGP RGRGVCDVFG VDPNDVDILM
     GTLTKSFGAA GGYIACDKWI IDKFRLDLTT VNYGESIAAP VLAQIISSMK TITGDTNPGE
     GEERLQRIAF NSRYLRLGLQ RLGFIVYGAP DSPVIPMLLY CPSKMPAFSR MMLQRKIAVV
     VVAYPATPLI ESRVRFCMSS SLTKEDIDYL LRHVSEVGDK LFLKVSSGKA SVPEDGRPPR
     WDIEEVLRKT PEDCKDSKFF SI
//