CAO2_SCHPO
ID CAO2_SCHPO Reviewed; 794 AA.
AC O42890;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Copper amine oxidase-like protein cao2;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P46883};
GN Name=cao2; Synonyms=spao2; ORFNames=SPBC1289.16c, SPBC8E4.06;
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 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 [3]
RP FUNCTION.
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-like protein that does not show any
CC copper amine oxidase activity. May be the appropriate amine substrate
CC for cao2 has not been identified yet. {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:0000250|UniProtKB:P46883};
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 -!- 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; CU329671; CAB38696.1; -; Genomic_DNA.
DR PIR; T39367; T39367.
DR PIR; T50376; T39171.
DR RefSeq; NP_596841.2; NM_001023862.3.
DR AlphaFoldDB; O42890; -.
DR SMR; O42890; -.
DR BioGRID; 276181; 10.
DR STRING; 4896.SPBC1289.16c.1; -.
DR iPTMnet; O42890; -.
DR MaxQB; O42890; -.
DR PaxDb; O42890; -.
DR PRIDE; O42890; -.
DR EnsemblFungi; SPBC1289.16c.1; SPBC1289.16c.1:pep; SPBC1289.16c.
DR GeneID; 2539624; -.
DR KEGG; spo:SPBC1289.16c; -.
DR PomBase; SPBC1289.16c; cao2.
DR VEuPathDB; FungiDB:SPBC1289.16c; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_2_1; -.
DR InParanoid; O42890; -.
DR OMA; NTHHENL; -.
DR PhylomeDB; O42890; -.
DR PRO; PR:O42890; -.
DR Proteomes; UP000002485; Chromosome II.
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:0048038; F:quinone binding; ISM:PomBase.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR GO; GO:0071941; P:nitrogen cycle metabolic process; IC: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 3: Inferred from homology;
KW Copper; Cytoplasm; Manganese; Metal-binding; Oxidoreductase;
KW Reference proteome; TPQ.
FT CHAIN 1..794
FT /note="Copper amine oxidase-like protein cao2"
FT /id="PRO_0000064107"
FT REGION 563..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 394
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 307..318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 391..396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 445
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 447
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 593
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 594
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 604
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 394
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
SQ SEQUENCE 794 AA; 90127 MW; 81E0E1CAD73F54F9 CRC64;
MAEESKAAEY FDPLDPLSFN ELRYVVNLVR KSYPEKQISF DVVTLSEPHK EEYVHWRYSS
AHEGIPDRRA YVIVLEKEVP GVFEGIVNLT TGKIEKWEHS VDTCPIITAD LLAITDEIVR
NDANVIEQCK ICGVPESGLS NVYCDPWTIG YDERYGSGRR LQQALMYYKP GDSGHLRSIP
LDFCPIIDVD QKKVIAIDIP KVRRPIPQDV NSDNNLKKLE QEMEAMKMLK PLRITQPEGV
NFRIKGRYIE WQNFCFHIGF NYREGIVLSD VVFNEDGHLR PLFYRISLTE MAVPFGAKGH
SHHRKHAYDL GEYGVGYRTN PLSFTCGCEG VIHYMDADFV NYRGEITTIK NAISIHEEDD
GVLFKYSDLR DRNANISARS IKLVVSQVFT AANYEYLVYW IFRMDGVIEC EIRLTGILNT
NAINEDEDLK GHGTQVYPKI SAENHEHLFC LRINPMLDGL RNSVATVDAL RDKNGTLVSK
YIIPETVTEA ISNYDSSTGR TWDICNLNKL HPYSGKPVSY KLISRDTSPV LSQPGTTNSD
CSGFAENNIY VTPYMDDQIF PTGDYAPQAS DDTPKGLSKW ISDDPNAQIK NTDIVVWHTF
GMIHFPAPED FPIMPAESIH LFLQPRNFFK HNPALDTSSS VNSTSEATSP NTHHENLRDT
SQKRESHSTP HDYEPHVSDK NDKSVEDKLH FVQKDESRPK EPVVDAAQKH EGRSETLAQP
GQQNANQSEE KQGGQNGSNG GHHHHHHHHY ITGHVYGGYH KHSGSGGHLV DMMKNISDVT
HDFAMGNFRY HKYD
