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O59682 (LCB1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine palmitoyltransferase 1

Short name=SPT 1
Short name=SPT1
EC=2.3.1.50
Alternative name(s):
Long chain base biosynthesis protein 1
Gene names
Name:lcb1
ORF Names:SPBC18E5.02c, SPBC29A3.20c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine By similarity. UniProtKB P25045

Catalytic activity

Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2. UniProtKB P25045

Cofactor

Pyridoxal phosphate By similarity. UniProtKB P25045

Pathway

Lipid metabolism; sphingolipid metabolism. UniProtKB P25045

Subunit structure

Lcb1 and lcb2 encode essential subunits of the enzyme and form a heterodimer By similarity. UniProtKB P25045

Subcellular location

Cytoplasm By similarity. Endoplasmic reticulum. Membrane; Multi-pass membrane protein Potential Ref.2 UniProtKB P25045.

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509Serine palmitoyltransferase 1
PRO_0000309453

Regions

Transmembrane45 – 6521Helical; Potential
Transmembrane327 – 34721Helical; Potential
Transmembrane363 – 38321Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
O59682 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 26BC0BE6AA6D16A7

FASTA50957,469
        10         20         30         40         50         60 
MSYSYPFFDD VYAYYNQTVT FFGKALDVLP GSPIVKRYIK SSYQNDPLRT FIEFLLLVFA 

        70         80         90        100        110        120 
AYYVLRKPRT SPDNNYVEFT EKEINELVDD WKPEPLVAEL TDVEKLELKS IPVLESVHLH 

       130        140        150        160        170        180 
TKLIDGRPIT NFASFNFLDL AENKHITECA VATLRECGLG ACGPPGFYGT QDKHLRLEKD 

       190        200        210        220        230        240 
IASFIGVERA IVYAQSFQTI SSVIPAFSKR GDILVVDEAC NFAIQKGIQI SRTTIRYFKH 

       250        260        270        280        290        300 
NNMKDLERIL QELEDDFVKH NRPLTRRFII TEGISENYGD MVDLTKIVAL KKKYKYRLIL 

       310        320        330        340        350        360 
DETWSFGTCG RTGKGLTEHF GVPPTDVEII IGSLTTSLAG GGGFCAGSEL MVEHQRLSGM 

       370        380        390        400        410        420 
AYIYSAALPA SLAVAAYEAI SILSRDGGSM LNDLRSKSAL FHAKLSRNKF FETSSDIESP 

       430        440        450        460        470        480 
IIHLRFKDKD ISHDKQVFLL EEIVELCIAE GFLIARAKRV ESLERVKVQP SLRICISTGH 

       490        500 
SAEEIEKLAL LIKEKTEIVF DKHKVINQV 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA18397.1.
PIRT39753.
RefSeqNP_595848.1. NM_001021752.2.

3D structure databases

ProteinModelPortalO59682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277338. 4 interactions.
MINTMINT-4675422.
STRING4896.SPBC18E5.02c-1.

Proteomic databases

MaxQBO59682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC18E5.02c.1; SPBC18E5.02c.1:pep; SPBC18E5.02c.
GeneID2540820.
KEGGspo:SPBC18E5.02c.

Organism-specific databases

PomBaseSPBC18E5.02c.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000216602.
KOK00654.
OMAVNHQRIN.
OrthoDBEOG7XPZG0.
PhylomeDBO59682.

Enzyme and pathway databases

UniPathwayUPA00222.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

NextBio20801937.
PROO59682.

Entry information

Entry nameLCB1_SCHPO
AccessionPrimary (citable) accession number: O59682
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways