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Protein

Copper amine oxidase 1

Gene

cao1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Copper amine oxidase involved in the metabolism of xenobiotic and biogenic amines. Capable of catalyzing the oxidative deamination of primary amines such as ethylamine as alternate sources of nitrogen to support growth.1 Publication

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarity, Zn2+By similarityNote: Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity).By similarity
  • L-topaquinoneBy similarityNote: Contains 1 topaquinone per subunit.By similarity
  • Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei321Proton acceptorBy similarity1
Active sitei407Schiff-base intermediate with substrate; via topaquinoneBy similarity1
Metal bindingi458Copper; via tele nitrogenBy similarity1
Metal bindingi460Copper; via tele nitrogenBy similarity1
Metal bindingi616ManganeseBy similarity1
Metal bindingi617Manganese; via carbonyl oxygenBy similarity1
Metal bindingi627Copper; via pros nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • amine catabolic process Source: PomBase
  • cellular copper ion homeostasis Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-SPO-211945. Phase 1 - Functionalization of compounds.
R-SPO-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper amine oxidase 1 (EC:1.4.3.211 Publication)
Gene namesi
Name:cao1
Synonyms:spao1
ORF Names:SPAC2E1P3.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC2E1P3.04.
PomBaseiSPAC2E1P3.04. cao1.

Subcellular locationi

GO - Cellular componenti

  • ascospore-type prospore Source: PomBase
  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi456H → A: Decreases copper amine oxidase activity. 1 Publication1
Mutagenesisi458H → A: Impairs copper amine oxidase activity. 1 Publication1
Mutagenesisi460H → A: Impairs copper amine oxidase activity. 1 Publication1
Mutagenesisi627H → A: Impairs copper amine oxidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003160361 – 712Copper amine oxidase 1Add BLAST712

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi340 ↔ 366By similarity
Modified residuei4072',4',5'-topaquinoneBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, TPQ

Proteomic databases

MaxQBiQ9P7F2.
PRIDEiQ9P7F2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi278248. 6 interactors.
MINTiMINT-4705319.

Structurei

3D structure databases

ProteinModelPortaliQ9P7F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni319 – 330Substrate bindingBy similarityAdd BLAST12
Regioni404 – 409Substrate bindingBy similarity6

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Phylogenomic databases

HOGENOMiHOG000250947.
InParanoidiQ9P7F2.
KOiK00276.
OMAiDGVLFKH.
OrthoDBiEOG092C1J1W.
PhylomeDBiQ9P7F2.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P7F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYYPHLPYH HHHHTSVPGE RLSDPLDPLS ADELKLAVEI IRHEYPSKHF
60 70 80 90 100
AFNVVTLEEP PKAKYLHWKY SKEDAHKPER IALAVLLEKG VPGILEARVN
110 120 130 140 150
LTKAEVIQIE HITGVCPILT ADMLVNTEQI VRKDPAVIEQ CILSGVPPDQ
160 170 180 190 200
MDHVYCDPWT IGYDERYGNT RRMQQAMMYY RSNEDDSQYS HPLDFCPIID
210 220 230 240 250
TEDQKVVAID IPPVRRPLSK HKHSNFNKKD IEAELGKMRE VKPISVTQPE
260 270 280 290 300
GVNFRMKGRY IEWQNFRMHI GFNYREGIVL SDISYNDNGH IRPLFYRMSI
310 320 330 340 350
AEMVVPYGNP EHPHQRKHAF DLGEYGAGYL TNPLALGCDC KGVIHYLDAH
360 370 380 390 400
FVNNTGEVET VKNAICIHEE DDGVLFKHSD FRDKFRTTIS ARGIRLVISQ
410 420 430 440 450
IFTAANYEYM VYWIFHMDGV IECELKLTGI LNTYAMNEGE DLKGWGTQVY
460 470 480 490 500
PQVNAHNHQH LFCLRLNPML DGYSNSVAVV DGVSGPGEPG SKENYYGNAF
510 520 530 540 550
TTERTVPKTV KEAICDYNSD TSRTWDICNP NKLHPYSGKP VSYKLVSRET
560 570 580 590 600
PRLMARPGSL VSNRAGFARH HIHVTPYKDG QIYPAGDYVP QTSGEPTKGL
610 620 630 640 650
PEWIAEEPDA SVDNTDIVVW HTFGITHFPA PEDFPLMPAE PIRLLLRPRN
660 670 680 690 700
FFLRNPALDV PPSKNVTTSE VKQAHHHGNL HMMDMMKSLT DATSEFAFGE
710
KFCEKHKGDH FF
Length:712
Mass (Da):81,241
Last modified:October 1, 2000 - v1
Checksum:iE48DE1CBA0D1C084
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB83008.1.
RefSeqiNP_593985.1. NM_001019411.2.

Genome annotation databases

EnsemblFungiiSPAC2E1P3.04.1; SPAC2E1P3.04.1:pep; SPAC2E1P3.04.
GeneIDi2541754.
KEGGispo:SPAC2E1P3.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB83008.1.
RefSeqiNP_593985.1. NM_001019411.2.

3D structure databases

ProteinModelPortaliQ9P7F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278248. 6 interactors.
MINTiMINT-4705319.

Proteomic databases

MaxQBiQ9P7F2.
PRIDEiQ9P7F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC2E1P3.04.1; SPAC2E1P3.04.1:pep; SPAC2E1P3.04.
GeneIDi2541754.
KEGGispo:SPAC2E1P3.04.

Organism-specific databases

EuPathDBiFungiDB:SPAC2E1P3.04.
PomBaseiSPAC2E1P3.04. cao1.

Phylogenomic databases

HOGENOMiHOG000250947.
InParanoidiQ9P7F2.
KOiK00276.
OMAiDGVLFKH.
OrthoDBiEOG092C1J1W.
PhylomeDBiQ9P7F2.

Enzyme and pathway databases

ReactomeiR-SPO-211945. Phase 1 - Functionalization of compounds.
R-SPO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiQ9P7F2.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAO1_SCHPO
AccessioniPrimary (citable) accession number: Q9P7F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.