CAO1_SCHPO
ID CAO1_SCHPO Reviewed; 712 AA.
AC Q9P7F2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Copper amine oxidase 1;
DE EC=1.4.3.21 {ECO:0000269|PubMed:16946276};
GN Name=cao1; Synonyms=spao1; ORFNames=SPAC2E1P3.04;
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]
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]
RP CATALYTIC ACTIVITY.
RX PubMed=16946276; DOI=10.1099/mic.0.28998-0;
RA Laliberte J., Labbe S.;
RT "Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine
RT oxidase 1 expressed in Saccharomyces cerevisiae.";
RL Microbiology 152:2819-2830(2006).
RN [3]
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).
RN [4]
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF HIS-456; HIS-458;
RP HIS-460 AND HIS-627.
RX PubMed=18723604; DOI=10.1128/ec.00230-08;
RA Peter C., Laliberte J., Beaudoin J., Labbe S.;
RT "Copper distributed by Atx1 is available to copper amine oxidase 1 in
RT Schizosaccharomyces pombe.";
RL Eukaryot. Cell 7:1781-1794(2008).
CC -!- FUNCTION: Copper amine oxidase involved in the metabolism of xenobiotic
CC and biogenic amines. Capable of catalyzing the oxidative deamination of
CC primary amines such as ethylamine as alternate sources of nitrogen to
CC support growth. {ECO:0000269|PubMed:18723604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:16946276};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc
CC ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
CC ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:18723604}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB83008.1; -; Genomic_DNA.
DR RefSeq; NP_593985.1; NM_001019411.2.
DR AlphaFoldDB; Q9P7F2; -.
DR SMR; Q9P7F2; -.
DR BioGRID; 278248; 7.
DR STRING; 4896.SPAC2E1P3.04.1; -.
DR iPTMnet; Q9P7F2; -.
DR MaxQB; Q9P7F2; -.
DR PaxDb; Q9P7F2; -.
DR PRIDE; Q9P7F2; -.
DR EnsemblFungi; SPAC2E1P3.04.1; SPAC2E1P3.04.1:pep; SPAC2E1P3.04.
DR GeneID; 2541754; -.
DR KEGG; spo:SPAC2E1P3.04; -.
DR PomBase; SPAC2E1P3.04; cao1.
DR VEuPathDB; FungiDB:SPAC2E1P3.04; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_2_1; -.
DR InParanoid; Q9P7F2; -.
DR OMA; TNKLNPY; -.
DR PhylomeDB; Q9P7F2; -.
DR PRO; PR:Q9P7F2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0042764; C:ascospore-type prospore; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; ISS:PomBase.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:PomBase.
DR GO; GO:0048038; F:quinone binding; ISM:PomBase.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009310; P:amine catabolic process; IDA:PomBase.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:PomBase.
DR GO; GO:1990748; P:cellular detoxification; TAS:PomBase.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW Copper; Cytoplasm; Disulfide bond; Manganese; Metal-binding;
KW Oxidoreductase; Reference proteome; TPQ.
FT CHAIN 1..712
FT /note="Copper amine oxidase 1"
FT /id="PRO_0000316036"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 407
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 319..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 404..409
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 458
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 460
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 616
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 617
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 627
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 407
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT DISULFID 340..366
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MUTAGEN 456
FT /note="H->A: Decreases copper amine oxidase activity."
FT /evidence="ECO:0000269|PubMed:18723604"
FT MUTAGEN 458
FT /note="H->A: Impairs copper amine oxidase activity."
FT /evidence="ECO:0000269|PubMed:18723604"
FT MUTAGEN 460
FT /note="H->A: Impairs copper amine oxidase activity."
FT /evidence="ECO:0000269|PubMed:18723604"
FT MUTAGEN 627
FT /note="H->A: Impairs copper amine oxidase activity."
FT /evidence="ECO:0000269|PubMed:18723604"
SQ SEQUENCE 712 AA; 81241 MW; E48DE1CBA0D1C084 CRC64;
MAYYPHLPYH HHHHTSVPGE RLSDPLDPLS ADELKLAVEI IRHEYPSKHF AFNVVTLEEP
PKAKYLHWKY SKEDAHKPER IALAVLLEKG VPGILEARVN LTKAEVIQIE HITGVCPILT
ADMLVNTEQI VRKDPAVIEQ CILSGVPPDQ MDHVYCDPWT IGYDERYGNT RRMQQAMMYY
RSNEDDSQYS HPLDFCPIID TEDQKVVAID IPPVRRPLSK HKHSNFNKKD IEAELGKMRE
VKPISVTQPE GVNFRMKGRY IEWQNFRMHI GFNYREGIVL SDISYNDNGH IRPLFYRMSI
AEMVVPYGNP EHPHQRKHAF DLGEYGAGYL TNPLALGCDC KGVIHYLDAH FVNNTGEVET
VKNAICIHEE DDGVLFKHSD FRDKFRTTIS ARGIRLVISQ IFTAANYEYM VYWIFHMDGV
IECELKLTGI LNTYAMNEGE DLKGWGTQVY PQVNAHNHQH LFCLRLNPML DGYSNSVAVV
DGVSGPGEPG SKENYYGNAF TTERTVPKTV KEAICDYNSD TSRTWDICNP NKLHPYSGKP
VSYKLVSRET PRLMARPGSL VSNRAGFARH HIHVTPYKDG QIYPAGDYVP QTSGEPTKGL
PEWIAEEPDA SVDNTDIVVW HTFGITHFPA PEDFPLMPAE PIRLLLRPRN FFLRNPALDV
PPSKNVTTSE VKQAHHHGNL HMMDMMKSLT DATSEFAFGE KFCEKHKGDH FF
