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Database: UniProt
Entry: A0A091HK68_CALAN
LinkDB: A0A091HK68_CALAN
Original site: A0A091HK68_CALAN 
ID   A0A091HK68_CALAN        Unreviewed;       420 AA.
AC   A0A091HK68;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Serine palmitoyltransferase 1 {ECO:0000256|ARBA:ARBA00041066};
DE            EC=2.3.1.50 {ECO:0000256|ARBA:ARBA00013220};
DE   AltName: Full=Long chain base biosynthesis protein 1 {ECO:0000256|ARBA:ARBA00041765};
DE   AltName: Full=Serine-palmitoyl-CoA transferase 1 {ECO:0000256|ARBA:ARBA00042649};
DE   Flags: Fragment;
GN   ORFNames=N300_12354 {ECO:0000313|EMBL:KFO95482.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO95482.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFO95482.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO95482.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine +
CC         CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57394, ChEBI:CHEBI:65073;
CC         Evidence={ECO:0000256|ARBA:ARBA00036980};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684;
CC         Evidence={ECO:0000256|ARBA:ARBA00036980};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine
CC         + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57385, ChEBI:CHEBI:71007;
CC         Evidence={ECO:0000256|ARBA:ARBA00035775};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676;
CC         Evidence={ECO:0000256|ARBA:ARBA00035775};
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:ARBA00036326};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC         Evidence={ECO:0000256|ARBA:ARBA00036326};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine +
CC         CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57375, ChEBI:CHEBI:71008;
CC         Evidence={ECO:0000256|ARBA:ARBA00036641};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680;
CC         Evidence={ECO:0000256|ARBA:ARBA00036641};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR   EMBL; KL217467; KFO95482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091HK68; -.
DR   STRING; 9244.A0A091HK68; -.
DR   Proteomes; UP000054308; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
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; 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:SF2; SERINE PALMITOYLTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW   Transferase {ECO:0000313|EMBL:KFO95482.1}.
FT   DOMAIN          46..409
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO95482.1"
FT   NON_TER         420
FT                   /evidence="ECO:0000313|EMBL:KFO95482.1"
SQ   SEQUENCE   420 AA;  46827 MW;  E73A3EBECF9C4204 CRC64;
     VQEKEELIEE WQPEPLVPSV PKEHPALNYN IVSGPPTHII TVNGKKCVNF ASFNFLGLLD
     NEKVKNAAQA SLKKYGVGTC GPRGFYGTFD VHLELEERLA KFMRTEEAII YSYGFATIAS
     AIPAYSKRGD IVFVDEASCF AIQKGLQASR SNIKLFKHND MADLERLLKD QETEDQKNPR
     KARVTRRFIV VEGLYMNTGD ICPLPELIKL KYKYKVRIFL EESLSFGVLG EHGRGITEHF
     GINIDDIDLI SANMENSLAS IGGFCCGRSF IIDHQRLSGQ GYCFSASLPP LLAAAAIEAL
     NIMEDNPDIF QILRHKCERI HKALQGISGL KVVGESFSPT LHLQLEESCG SRENDVKLLK
     RVVDYCMNSG IALTQARYLD KEEKCLPAPS IRVVITVEQT EQELDKAASL LKEAAQSVLN
//
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