LCB1_SCHPO
ID LCB1_SCHPO Reviewed; 509 AA.
AC O59682;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine palmitoyltransferase 1;
DE Short=SPT 1;
DE Short=SPT1;
DE EC=2.3.1.50;
DE AltName: Full=Long chain base biosynthesis protein 1;
GN Name=lcb1 {ECO:0000250|UniProtKB:P25045};
GN ORFNames=SPBC18E5.02c, SPBC29A3.20c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA18397.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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|UniProtKB:P25045}.
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:0000250|UniProtKB:P25045};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P25045};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:P25045}.
CC -!- SUBUNIT: Lcb1 and lcb2 encode essential subunits of the enzyme and form
CC a heterodimer. {ECO:0000250|UniProtKB:P25045}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25045,
CC ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
CC Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
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DR EMBL; CU329671; CAA18397.1; -; Genomic_DNA.
DR PIR; T39753; T39753.
DR RefSeq; NP_595848.1; NM_001021752.2.
DR AlphaFoldDB; O59682; -.
DR SMR; O59682; -.
DR BioGRID; 277338; 1.
DR STRING; 4896.SPBC18E5.02c.1; -.
DR iPTMnet; O59682; -.
DR MaxQB; O59682; -.
DR PaxDb; O59682; -.
DR PRIDE; O59682; -.
DR EnsemblFungi; SPBC18E5.02c.1; SPBC18E5.02c.1:pep; SPBC18E5.02c.
DR GeneID; 2540820; -.
DR KEGG; spo:SPBC18E5.02c; -.
DR PomBase; SPBC18E5.02c; lcb1.
DR VEuPathDB; FungiDB:SPBC18E5.02c; -.
DR eggNOG; KOG1358; Eukaryota.
DR HOGENOM; CLU_015846_0_2_1; -.
DR InParanoid; O59682; -.
DR OMA; RNTPTFA; -.
DR PhylomeDB; O59682; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:O59682; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; ISO:PomBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IBA:GO_Central.
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; Cytoplasm; Endoplasmic reticulum; Lipid metabolism;
KW Membrane; Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Serine palmitoyltransferase 1"
FT /id="PRO_0000309453"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 509 AA; 57469 MW; 26BC0BE6AA6D16A7 CRC64;
MSYSYPFFDD VYAYYNQTVT FFGKALDVLP GSPIVKRYIK SSYQNDPLRT FIEFLLLVFA
AYYVLRKPRT SPDNNYVEFT EKEINELVDD WKPEPLVAEL TDVEKLELKS IPVLESVHLH
TKLIDGRPIT NFASFNFLDL AENKHITECA VATLRECGLG ACGPPGFYGT QDKHLRLEKD
IASFIGVERA IVYAQSFQTI SSVIPAFSKR GDILVVDEAC NFAIQKGIQI SRTTIRYFKH
NNMKDLERIL QELEDDFVKH NRPLTRRFII TEGISENYGD MVDLTKIVAL KKKYKYRLIL
DETWSFGTCG RTGKGLTEHF GVPPTDVEII IGSLTTSLAG GGGFCAGSEL MVEHQRLSGM
AYIYSAALPA SLAVAAYEAI SILSRDGGSM LNDLRSKSAL FHAKLSRNKF FETSSDIESP
IIHLRFKDKD ISHDKQVFLL EEIVELCIAE GFLIARAKRV ESLERVKVQP SLRICISTGH
SAEEIEKLAL LIKEKTEIVF DKHKVINQV
