ID   A0A177EP19_9MICR        Unreviewed;       475 AA.
AC   A0A177EP19;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=serine C-palmitoyltransferase {ECO:0000256|ARBA:ARBA00013220};
DE            EC=2.3.1.50 {ECO:0000256|ARBA:ARBA00013220};
GN   ORFNames=NEIG_02429 {ECO:0000313|EMBL:OAG32852.1};
OS   Nematocida sp. ERTm5.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX   NCBI_TaxID=1805481 {ECO:0000313|EMBL:OAG32852.1, ECO:0000313|Proteomes:UP000077089};
RN   [1] {ECO:0000313|EMBL:OAG32852.1, ECO:0000313|Proteomes:UP000077089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERTm5 {ECO:0000313|EMBL:OAG32852.1,
RC   ECO:0000313|Proteomes:UP000077089};
RA   Reinke A.W., Balla K.M., Bennett E.J., Troemel E.R.;
RT   "Identification of microsporidia host-exposed proteins reveals a repertoire
RT   of large paralogous families and rapidly evolving proteins.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU003693};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008392,
CC       ECO:0000256|RuleBase:RU003693}.
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:OAG32852.1}.
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DR   EMBL; LTDK01000104; OAG32852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177EP19; -.
DR   VEuPathDB; MicrosporidiaDB:NEIG_02429; -.
DR   OrthoDB; 9643at2759; -.
DR   Proteomes; UP000077089; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:OAG32852.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          106..455
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   475 AA;  53907 MW;  1D99C0B737DF9EDD CRC64;
     MTNKIYIPFF TIVTTYLSYF IVIVLGHARD FIGQMLFPKL YKHMFPSNGR LPLFTTSGSF
     YTRRLYGRLN DCWNRPITGI PGRNVKVLLR TRDRDGEMKL TGESKMCLNL GSYNYLGYAG
     MYNEEAKKAL LKYPIAYCGP VKFLPPCPLV RQLEKEIATF LYKEDAIVFP MGFATNACTI
     PYLVNKGDLI IADSLNHSSI FFGTRISPCK VERFGHNDIN MLEKIIRKAI IEGQDRTHRP
     IGRILVIVEG IYSMEGECVK LKEILALKEK YPFYLFIDEA HSIGAMGKTG RGVCEYLDVD
     FNKIDLLMGT FTKSFGAAGG YIAANKNIIN LLRKRSELIN RGEQMPPVVA TQILECLKRM
     QTKEGKREIQ KLADKSRYFR KELHRMGFIV IGEKDCPVVP LMLYNPGKIA EFSRMCLKEN
     IAVVVVGYPA TPVISSRVRF CLSVAHTKED LNRALFVIDR IGDLLGLKMA RSKAS
//