Skip Header

Contribute Send feedback
Read comments (?) or add your own

O43029 (FAP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
L-pipecolate oxidase

EC=1.5.3.7
Alternative name(s):
L-pipecolic acid oxidase
Gene names
Name:fap1
ORF Names:SPBC354.15
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidizes L-pipecolate and L-proline (6,7% of the activity for L-pipecolate). Ref.2

Catalytic activity

L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2. Ref.2

Cofactor

FAD. Ref.2

Subunit structure

Dimer. Ref.2

Subcellular location

Secreted Potential. Cytoplasm. Nucleus Ref.3.

Sequence similarities

Belongs to the MSOX/MTOX family.

Biophysicochemical properties

Kinetic parameters:

KM=4.07 mM for L-pipecolate Ref.2

KM=33.5 mM for L-proline Ref.2

Vmax=46.1 µmol/min/mg enzyme for L-pipecolate Ref.2

Vmax=9.45 µmol/min/mg enzyme for L-proline Ref.2

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Secreted
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processL-lysine catabolic process

Traceable author statement. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionL-pipecolate oxidase activity

Inferred from direct assay. Source: GeneDB_Spombe

flavin adenine dinucleotide binding

Inferred from direct assay. Source: GeneDB_Spombe

proline oxidase activity

Inferred from direct assay. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 412392L-pipecolate oxidase
PRO_0000347274

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O43029 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: BD36B86075D3F4EF

FASTA41246,320
        10         20         30         40         50         60 
MVKNTSVIIV GAGVFGLSAA LELTKRGGYT IKILDRAPPP VIDGSSVDAN RIIRSDYADA 

        70         80         90        100        110        120 
VYCSMGIDAL EEWRTNPLFK EQFYGSGLMF VGRDNVEYRD MSLENLTKMG VSAAKFQTTE 

       130        140        150        160        170        180 
ELRKLFPKWI GELNDGEAGY ANFSSGWANA EQSVKSVVNY LAHAGVSFIS GPEGTVEELI 

       190        200        210        220        230        240 
TEENVVKGVR TTTGAYMAEK LIFATGAWTA SLLPNDHTRF LATGQPVAYI KLTPEEYIRF 

       250        260        270        280        290        300 
LTNPVYLDFD TGFYIFPPTP DGYLKFARHG YGFTRMQNLK SGKVESVPPK KPLVSPILPK 

       310        320        330        340        350        360 
EAELDLRRNL QRTYGEEISQ RPFYKTRICY YTDTADAEFV FDYHPDYENL FVCTGGSGHG 

       370        380        390        400        410 
FKFFPILGKY SIGCMFRELE EPLLKKWRWK KENLEFAALD HSRAGPSRQE LS 

« Hide

References

« Hide 'large scale' 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe."
Yoshida N., Akazawa S., Katsuragi T., Tani Y.
J. Biosci. Bioeng. 97:278-280(2004) [PubMed: 16233628] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[3]"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: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA17815.1.
PIRT40295.
RefSeqNP_595239.1. NM_001021145.1.

3D structure databases

ProteinModelPortalO43029.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC354.15.1; SPBC354.15.1:pep; SPBC354.15.
GeneID2540916.
GenomeReviewsGene locus fap1 in contig CU329671_GR.
KEGGspo:SPBC354.15.
NMPDRfig|4896.1.peg.1105.

Organism-specific databases

GeneDB_SpombeSPBC354.15.

Phylogenomic databases

eggNOGfuNOG08637.
GeneTreeEFGT00050000004195.
HOGENOMHBG328502.
OMAFENCASS.
OrthoDBEOG4Q5CXW.

Gene expression databases

ArrayExpressO43029.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFAP1_SCHPO
AccessionPrimary (citable) accession number: O43029
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: June 1, 1998
Last modified: December 14, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families