ID   SPT_BACTC               Reviewed;         420 AA.
AC   A7BFV8;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 46.
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   Bacteriovorax stolpii (Bdellovibrio stolpii).
OC   Bacteria; Proteobacteria; Oligoflexia; Bacteriovoracales;
OC   Bacteriovoracaceae; Bacteriovorax.
OX   NCBI_TaxID=960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 27052;
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   -!- ACTIVITY REGULATION: Significantly inhibited by palmitoyl-CoA
CC       concentrations greater than 100 uM. {ECO:0000269|PubMed:17557831}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.7 mM for L-serine {ECO:0000269|PubMed:17557831};
CC         Note=kcat is 0.03 sec(-1) (in the presence of 100 uM of palmitoyl-
CC         CoA). {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:0000269|PubMed:17557831}. Cell
CC       inner membrane {ECO:0000269|PubMed:17557831}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:17557831}. Note=Predominantly concentrated
CC       in a limited region near the inner membrane or organelle-like
CC       multilayered membrane structure. {ECO:0000269|PubMed:17557831}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AB259216; BAF73753.1; -; Genomic_DNA.
DR   BRENDA; 2.3.1.50; 800.
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; Cell inner membrane; Cell membrane; Cytoplasm;
KW   Lipid metabolism; Membrane; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..420
FT                   /note="Serine palmitoyltransferase"
FT                   /id="PRO_0000456077"
FT   BINDING         132..133
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   BINDING         233
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   BINDING         261
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   BINDING         263
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
SQ   SEQUENCE   420 AA;  46191 MW;  24BF917CB1E622C1 CRC64;
     MKHNLQDNLQ GEQMANTNSN GGKKPFSDAK IIERANLLRD NDLYFFFRAI EETEASTVTV
     KGKKQIMIGS NNYLGLTHHP AVKEAAIKAV EKYGTGCTGS RFLNGNLNIH EELDEKLAAY
     LGHEKAIVFS TGMQANLGAL SAICGPKDLM LFDSENHASI IDASRLSLGT TFKYKHNDMA
     SLEELLESNM SRFNRVIIVA DGVFSMTGDI LRLPEVVKLA KKYGAYVYVD DAHGLGVMGP
     QGRGTMAHFD VTKDVDFNMG TFSKSFASIG GVISGSKDAI DYVRHSARSF MFSASMPPAA
     VATVSACIDV VQNDETILNN LWSNVEFMRN GFKELGFFTY GSQTPIIPLF IGDDMKALKM
     TKWLESKGVF CTPVLPPAVP KGETLIRTSY MASHNREDLS TVLEVFAEAK KIFDIPNHLH