ID   SPT_SPHSI               Reviewed;         399 AA.
AC   A7BFV7;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Serine palmitoyltransferase {ECO:0000303|PubMed:17557831};
DE            Short=SPT {ECO:0000303|PubMed:17557831};
DE            EC=2.3.1.50 {ECO:0000269|PubMed:17557831};
GN   Name=spt {ECO:0000303|PubMed:17557831};
OS   Sphingobacterium spiritivorum (Flavobacterium spiritivorum).
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=258;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=EY3101;
RX   PubMed=17557831; DOI=10.1128/jb.00194-07;
RA   Ikushiro H., Islam M.M., Tojo H., Hayashi H.;
RT   "Molecular characterization of membrane-associated soluble serine
RT   palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio
RT   stolpii.";
RL   J. Bacteriol. 189:5749-5761(2007).
CC   -!- FUNCTION: Catalyzes the condensation of L-serine with palmitoyl-CoA
CC       (hexadecanoyl-CoA) to produce 3-oxosphinganine.
CC       {ECO:0000269|PubMed:17557831}.
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:0000269|PubMed:17557831};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC         Evidence={ECO:0000269|PubMed:17557831};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:17557831};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.0 mM for L-serine {ECO:0000269|PubMed:17557831};
CC         KM=0.39 mM for palmitoyl-CoA {ECO:0000269|PubMed:17557831};
CC         Note=kcat is 0.15 sec(-1). {ECO:0000269|PubMed:17557831};
CC       pH dependence:
CC         Optimum pH is 7.0 to 8.0. {ECO:0000269|PubMed:17557831};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000305|PubMed:17557831}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17557831}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AB259215; BAF73752.1; -; Genomic_DNA.
DR   RefSeq; WP_003000371.1; NZ_UGYY01000002.1.
DR   BRENDA; 2.3.1.50; 10090.
DR   UniPathway; UPA00222; -.
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:0009058; P:biosynthetic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Lipid metabolism; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..399
FT                   /note="Serine palmitoyltransferase"
FT                   /id="PRO_0000456079"
FT   BINDING         113..114
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   BINDING         213
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   BINDING         241
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   BINDING         243
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   MOD_RES         244
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
SQ   SEQUENCE   399 AA;  43929 MW;  1C95E59948E20ADF CRC64;
     MSKGKLSERI SHFNIVEELK SKGLYAYFRP IQSKQDTEVM IDGKRVLMFG SNSYLGLTID
     PRIIEAAQDA LSKYGTGCAG SRFLNGTLDI HIELEHKLSQ LVGKEASILF STGFQSNLGP
     ISCLMGRNDY ILLDERDHAS IIDGSRLSFS KVIKYGHNDM DDLRAKLSRL PSESAKLIVT
     DGIFSMEGDI VNLPEMVKIA DEYDAALMVD DAHSLGVIGE HGAGTASHFG LTDKVDLIMG
     TFSKSLASLG GFVAGDADVI DYLKHNARSV MFSASMTPAS VASTLKALEI MISEPEHMEN
     LWKNTNYAKQ QLLESGFDLG ATESPILPIF IRNNEKTFWV TKMLQDDGVF VNPVVSPAVP
     SEESLIRFSL MATHTFDQID EAVEKMVRVF KQAEIESLI