ID   A0A0A1U4X4_ENTIV        Unreviewed;       883 AA.
AC   A0A0A1U4X4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=serine C-palmitoyltransferase {ECO:0000256|ARBA:ARBA00013220};
DE            EC=2.3.1.50 {ECO:0000256|ARBA:ARBA00013220};
GN   ORFNames=EIN_486860 {ECO:0000313|EMBL:ELP89224.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP89224.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP89224.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP89224.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) 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   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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; KB206670; ELP89224.1; -; Genomic_DNA.
DR   RefSeq; XP_004255995.1; XM_004255947.1.
DR   AlphaFoldDB; A0A0A1U4X4; -.
DR   EnsemblProtists; ELP89224; ELP89224; EIN_486860.
DR   GeneID; 14888103; -.
DR   KEGG; eiv:EIN_486860; -.
DR   VEuPathDB; AmoebaDB:EIN_486860; -.
DR   OrthoDB; 9643at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
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   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); 2.
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; 2.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:ELP89224.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW   Transferase {ECO:0000313|EMBL:ELP89224.1}.
FT   DOMAIN          116..467
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   DOMAIN          534..879
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   883 AA;  98193 MW;  7B83E717366CE5D3 CRC64;
     MENNDSYQLS TWGGLWRYIG IERHAQYGYY YNLGYAKAQD YINWPMYYLG LKDQKPPLTG
     ESSEDFYIRS IYTSTYDCFN RPLCGPAAKD ISIGMRREVP IENVKHLVPI DEQREALNFG
     SYNYLGFGGV NPKVTPQIVE TLKQSGATLS GFASECGVSK EQEELELLMA DFLHKEASIV
     VPMGFATNST LIPILLGKGD VVFSDELNHS SIITGIKSSN AEVRVFKHND ILDLKSKLEE
     LKTKGMKGGK QPNKVMIIVE GLYSMEGEFC PLRELIALKK IYGFYLYIDE AHSIGALGAT
     GRGITEHLGC NFDDVDILMG TFSKSFASAG GYIASDKKTI ELLKSNCYSY VYGSAMSPIE
     AKQIIAALNL MKTDEGKQRI AQLRKNSINF RRKLIKAGCH VLGDLDSPVI PVMLYHVGKL
     KDVSRGCLKR GVAVVTVGYP ACSTIACRVR FCISAAHTDA DMEKAFNATI ECLKEVDCIF
     GDTPQPNVIY KAKKADLDEL EKEPKNPRKM NPLYENSDKR PILEAVKRPE PSDTNLSSYD
     IHGFGEDQER TQLIVKILEK YGCGSCGPRG FYGTTLEHLS IEDELMKFYG TNDALVYSYG
     NNTITSVVPV YGHAGDSILV DEMCNYEIQL GCRLSKKANI VKFKHNDVED VKAKIQEIKK
     TLVYPGRIAI VTEGVFRADL SLAPLAELSK LRKKNVLLIV DDSLGVGALG AHLKGSLEQA
     GITANDVDVY CGNMEMVCDT IGGFVVGKYS MIDKQRLFGA GYIFSASAPP FTCSAATFAF
     NKFEKNGIEM GVEMREKRKL FDQLFNEHVK NVKKIGDDNT PYVLLDAGDN QNMVKVLKEN
     GFFASQQVHL VEDWCQTKYV RACIGKNFTD EKIHKLVEIL AKL
//