SPTC1_DICDI
ID SPTC1_DICDI Reviewed; 479 AA.
AC Q55FL5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Serine palmitoyltransferase 1;
DE EC=2.3.1.50;
DE AltName: Full=Long chain base biosynthesis protein 1;
DE Short=LCB 1;
DE AltName: Full=Serine-palmitoyl-CoA transferase 1;
DE Short=SPT 1;
DE Short=SPT1;
GN Name=sptA; ORFNames=DDB_G0268056;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of serine palmitoyltransferase (SPT), which
CC catalyzes the committed step in the synthesis of sphingolipids, the
CC condensation of serine with palmitoyl CoA to form the long chain base
CC 3-ketosphinganine. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Forms a heterodimer with sptB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73481.1; -; Genomic_DNA.
DR RefSeq; XP_647518.1; XM_642426.1.
DR AlphaFoldDB; Q55FL5; -.
DR SMR; Q55FL5; -.
DR STRING; 44689.DDB0232040; -.
DR PaxDb; Q55FL5; -.
DR EnsemblProtists; EAL73481; EAL73481; DDB_G0268056.
DR GeneID; 8616325; -.
DR KEGG; ddi:DDB_G0268056; -.
DR dictyBase; DDB_G0268056; sptA.
DR eggNOG; KOG1358; Eukaryota.
DR HOGENOM; CLU_015846_0_2_1; -.
DR InParanoid; Q55FL5; -.
DR OMA; RNTPTFA; -.
DR PhylomeDB; Q55FL5; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q55FL5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; ISS:dictyBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; ISS:dictyBase.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..479
FT /note="Serine palmitoyltransferase 1"
FT /id="PRO_0000327870"
FT TOPO_DOM 1..16
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 53519 MW; 10E6AFB435283F7D CRC64;
MFLFDIYNNI LYYTKEFIVT STSPNLFIHG LMAVFIIYLL TKRPFKPRQN DTLTKAEEDE
LIREWSPIPL TPKSNPLEVL NQTELIIQES EGTHVTINNK KYLNLARSNY LGLINNPEIN
KISENAIRKY GVGSCGPRGF YGTIDVHLDL EKKTASFMKT PEAVLYSSAY ATISSAIPSF
SKIGDIIIVD RGVSQPVQVG VSLSRSRIYY FNHNDMDDLQ RVLEQTQFKG SKAKIVRKFV
VIEGLYYNSG TIAPLPQILK FKEQYKFRLI MDESHSVGVL GSTGRGLTEH YNIDTNLVDI
LTGSYGNSFS SGGGFCCGSP EVVYHQRLNG VGYVFSASLP PFLACSSTKA IEMLEENPKM
LEMLHSNIGE LYQGLNKSGA LNGLLEITSL PISPVIHLSL LDSKSNKSNR INDELLLQKI
VDKAMDYGLL LTRAKYVSAE KFIPKPSIRI SVSSNLSSDQ IKQSIEIIKK CTSFVLESN
