SPTC2_DICDI
ID SPTC2_DICDI Reviewed; 490 AA.
AC Q54EX5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Serine palmitoyltransferase 2;
DE EC=2.3.1.50;
DE AltName: Full=Long chain base biosynthesis protein 2;
DE Short=LCB 2;
DE AltName: Full=Serine-palmitoyl-CoA transferase 2;
DE Short=SPT 2;
DE Short=SPT2;
GN Name=sptB; ORFNames=DDB_G0291283;
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).
RN [2]
RP PROTEIN SEQUENCE OF 160-167 AND 300-334, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Catalytic subunit 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 sptA. {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}.
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; AAFI02000177; EAL61625.1; -; Genomic_DNA.
DR RefSeq; XP_635115.1; XM_630023.1.
DR AlphaFoldDB; Q54EX5; -.
DR SMR; Q54EX5; -.
DR STRING; 44689.DDB0232041; -.
DR PaxDb; Q54EX5; -.
DR EnsemblProtists; EAL61625; EAL61625; DDB_G0291283.
DR GeneID; 8628062; -.
DR KEGG; ddi:DDB_G0291283; -.
DR dictyBase; DDB_G0291283; sptB.
DR eggNOG; KOG1357; Eukaryota.
DR HOGENOM; CLU_015846_7_0_1; -.
DR InParanoid; Q54EX5; -.
DR OMA; IEDEPPY; -.
DR PhylomeDB; Q54EX5; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q54EX5; -.
DR Proteomes; UP000002195; Chromosome 6.
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:0030148; P:sphingolipid biosynthetic process; ISS:dictyBase.
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; 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; Direct protein sequencing; Endoplasmic reticulum;
KW Lipid metabolism; Membrane; Pyridoxal phosphate; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..490
FT /note="Serine palmitoyltransferase 2"
FT /id="PRO_0000327871"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 321
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 490 AA; 54785 MW; 052F6E2457F163D8 CRC64;
MEDKEDVENV DDVGYLPILF LYIAYAFIIF NGKLAEFIGK LKGERYLHTP EGYAPLFVEF
EYFYQRRMYG RIKDAWDRPI NSIAGAWIDV MPRASKHYSQ RLELTGGKTI KCLNLGSYNY
LGFAQNEGPV ADKVIDSIYK YGVYTGSTSA EVGLSEPQRD LENLTARFVG KEDAIVFEMG
FATNSGTLPA LIGKGGLIIS DSLNHASLAT GCKNTGCKVK VFRHNDSKHL EEVIRESIIQ
GQPRTHRPWT MILIIIEGIY SMEGEVANLP EILAIKKKYK CYLYIDEAHS IGALGKTGRG
IVDYYGIDPK EIDILMGTYT KSFGAIGGYV ASDKSLIDHL RQSSFSQVYA NSMSPVCAVQ
ALEALRVIMG EDGTDTGAKK LKQLHDNSNY FREKIREMGF VILGNKDSPV IPLMLFNPAK
LSAFSRLCLE KHIAVVVVGY PATPLTEPRT RFCISASHTI EDLDWALRQI DEIGDLITLK
FHKGKYLKSK
