ID A0A409W6K5_9AGAR Unreviewed; 696 AA.
AC A0A409W6K5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=serine C-palmitoyltransferase {ECO:0000256|ARBA:ARBA00013220};
DE EC=2.3.1.50 {ECO:0000256|ARBA:ARBA00013220};
GN ORFNames=CVT26_006764 {ECO:0000313|EMBL:PPQ74160.1};
OS Gymnopilus dilepis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX NCBI_TaxID=231916 {ECO:0000313|EMBL:PPQ74160.1, ECO:0000313|Proteomes:UP000284706};
RN [1] {ECO:0000313|EMBL:PPQ74160.1, ECO:0000313|Proteomes:UP000284706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRW20 {ECO:0000313|EMBL:PPQ74160.1,
RC ECO:0000313|Proteomes:UP000284706};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
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:0000256|ARBA:ARBA00001016};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPQ74160.1}.
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DR EMBL; NHYE01005359; PPQ74160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409W6K5; -.
DR STRING; 231916.A0A409W6K5; -.
DR InParanoid; A0A409W6K5; -.
DR OrthoDB; 9643at2759; -.
DR Proteomes; UP000284706; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd06454; KBL_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
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.
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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000284706}.
FT DOMAIN 247..495
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT DOMAIN 557..658
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 696 AA; 75805 MW; 39688D917CF2B99A CRC64;
MPSKSPSPMA FTKPAQSPSI FKKRSASALS SLPASAASYL SALSQADARA RSANNNSPTS
TPALSLSSSI TSSSEDTILH EDDYMNDPVL GSNKDGLLLP SRPPTSEQVF STVHTEFGHC
ASEEYRMTSQ HPPGKPLAVH VPKDPPYYIL LSTYISYLIL IVLGHVRDFV GKRLNPGSYK
HLMPRDGYAP LNSDFDSFYT RRLKTRMDEC FSQPVTGVAG RTILLLDRIS PDYNHSYVFT
GSRTRALNIS SYNYLGFAQA RGGCADAVEE SIRRYGISTL GSRLEAGNSD LHVVSEALVA
KFVGMEDALI SSMGFATNST FIPALVSKGC LVISDEFNHA SIRFGVRISG ANVRMFKHND
MKSLESLLRE VISQGQPKTH RPWKKILVIV EGLYSMEGTL VNLPAIVELK KKYKFYLFVD
EAHSIGALGP HGRGVADYFG INPRAIDILM GTFTKSFGAA GGYIAGNKAL IDRLRVYGHS
GPYAEAMTPP VLTQVIASMA SIMGLKPSGA AGSGSTSEQL LVPRGSVPPA QALDDEYHHP
GPAPASSLPA WISLPAALSS GAEGRTRLRR LAFNARYLHH GLRKLGFITY GHPTSPIVPL
LIFNPGKMNM FHRLMKERQT PIIVVVVAYP ATPLVTSRVR FCVSAAHTKE DVDTVLRACD
EIGDVLDLKH GIPKRERWSI EEVVRRAVEL GTSEEE
//