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Reviewed, UniProtKB/Swiss-Prot Q9P7F2 (AMOH2_SCHPO)

Last modified June 16, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative primary amine oxidase 2
    EC=1.4.3.21
Alternative name(s):
    Copper amine oxidase 2
Gene names
ORF Names: SPAC2E1P3.04
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length712 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Contains 1 topaquinone per subunit By similarity.

Subcellular location

Cytoplasm. Ref.2

Post-translational modification

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue By similarity.

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMTPQ
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processamine catabolic process

Inferred from direct assay. Source: GeneDB_SPombe

copper ion homeostasis

Inferred from mutant phenotype. Source: GeneDB_SPombe

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionamine oxidase activity

Inferred from direct assay. Source: GeneDB_SPombe

copper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: GeneDB_SPombe

quinone binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 712712Putative primary amine oxidase 2
PRO_0000316036

Sites

Active site3211Proton acceptor By similarity
Active site4071Schiff-base intermediate with substrate; via topaquinone By similarity
Metal binding4581Copper By similarity
Metal binding4601Copper By similarity
Metal binding6271Copper By similarity

Amino acid modifications

Modified residue40712',4',5'-topaquinone By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P7F2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E48DE1CBA0D1C084

FASTA71281,241
        10         20         30         40         50         60 
MAYYPHLPYH HHHHTSVPGE RLSDPLDPLS ADELKLAVEI IRHEYPSKHF AFNVVTLEEP 

        70         80         90        100        110        120 
PKAKYLHWKY SKEDAHKPER IALAVLLEKG VPGILEARVN LTKAEVIQIE HITGVCPILT 

       130        140        150        160        170        180 
ADMLVNTEQI VRKDPAVIEQ CILSGVPPDQ MDHVYCDPWT IGYDERYGNT RRMQQAMMYY 

       190        200        210        220        230        240 
RSNEDDSQYS HPLDFCPIID TEDQKVVAID IPPVRRPLSK HKHSNFNKKD IEAELGKMRE 

       250        260        270        280        290        300 
VKPISVTQPE GVNFRMKGRY IEWQNFRMHI GFNYREGIVL SDISYNDNGH IRPLFYRMSI 

       310        320        330        340        350        360 
AEMVVPYGNP EHPHQRKHAF DLGEYGAGYL TNPLALGCDC KGVIHYLDAH FVNNTGEVET 

       370        380        390        400        410        420 
VKNAICIHEE DDGVLFKHSD FRDKFRTTIS ARGIRLVISQ IFTAANYEYM VYWIFHMDGV 

       430        440        450        460        470        480 
IECELKLTGI LNTYAMNEGE DLKGWGTQVY PQVNAHNHQH LFCLRLNPML DGYSNSVAVV 

       490        500        510        520        530        540 
DGVSGPGEPG SKENYYGNAF TTERTVPKTV KEAICDYNSD TSRTWDICNP NKLHPYSGKP 

       550        560        570        580        590        600 
VSYKLVSRET PRLMARPGSL VSNRAGFARH HIHVTPYKDG QIYPAGDYVP QTSGEPTKGL 

       610        620        630        640        650        660 
PEWIAEEPDA SVDNTDIVVW HTFGITHFPA PEDFPLMPAE PIRLLLRPRN FFLRNPALDV 

       670        680        690        700        710 
PPSKNVTTSE VKQAHHHGNL HMMDMMKSLT DATSEFAFGE KFCEKHKGDH FF 

« 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[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: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAB83008.1.
RefSeqNP_593985.1.

3D structure databases

HSSPHSSP built from PDB template 1EKM based on UniProtKB P12807.
ModBaseSearch...

Genome annotation databases

GeneID2541754.
KEGGspo:SPAC2E1P3.04.
NMPDRfig|4896.1.peg.3955.

Organism-specific databases

GeneDB_SpombeSPAC2E1P3.04.

Phylogenomic databases

OMAQ9P7F2. ITHFPAP.

Enzyme and pathway databases

BRENDA1.4.3.6. 653.

Gene expression databases

ArrayExpressQ9P7F2.

Family and domain databases

InterProIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
Gene3DG3DSA:3.10.450.40. CuNH_oxidase. 2 hits.
G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHERPTHR10638. CuNH_oxidase. 1 hit.
PfamPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMOH2_SCHPO
AccessionPrimary (citable) accession number: Q9P7F2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents