ID B6HSE8_PENRW Unreviewed; 698 AA.
AC B6HSE8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=Pc22g17240 {ECO:0000313|EMBL:CAP99012.1}, PCH_Pc22g17240
GN {ECO:0000313|EMBL:CAP99012.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP99012.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP99012.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000672};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000256|RuleBase:RU000672};
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC ECO:0000256|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM920437; CAP99012.1; -; Genomic_DNA.
DR RefSeq; XP_002565637.1; XM_002565591.1.
DR AlphaFoldDB; B6HSE8; -.
DR STRING; 500485.B6HSE8; -.
DR GeneID; 8312209; -.
DR KEGG; pcs:Pc22g17240; -.
DR VEuPathDB; FungiDB:PCH_Pc22g17240; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_2_1; -.
DR OMA; CMHPSET; -.
DR OrthoDB; 34972at2759; -.
DR BioCyc; PCHR:PC22G17240-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c22.
DR GO; GO:0052595; F:aliphatic amine oxidase activity; IEA:RHEA.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 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; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF86; COPPER AMINE OXIDASE 1-RELATED; 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; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000672};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 36..120
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 127..221
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 254..668
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 416
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 416
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 698 AA; 78646 MW; 296026078F187EFF CRC64;
MASAPDTESI PGYTIFREGD YESVAAAAML PQGTPHPLDQ LSIKEIPEAA KIIRDYANPK
SIKFNCLTLR EPRKAEYRAF RAGAVPAPAR RAFAIVIVRE TNKIAEVVAN LATGKVEEWK
DVHDVMPTLT LEDLDVMERV ARKDTRVIRA CKDLGIIDMN KVFFDAWAIG IDERWGYDHR
LQQGLAYYRS SDFDNQYAHP LDFSVVADTD TEEVLSVDIR YVNGERTATP LKEHNYLPEF
IGDKYKHDRL KPIDITQPEG VSFKVRGNEL TWANFKMHVG FNYREGIVLS DVRTHDMYED
RERTLFNRIS VVEMVVPYGC PEKPHHKKHA FDVGEYGTGL MTNSLKLGCD CKGAIHYMDG
VMSTSKGEAA VIKNAICIHE EDNGLLYKHT DFRDGTVISA RDRKLIISQI ITAANYEYGF
YHTFTLDGTY KLEVKLTGML NTYCMHPTET AAPFGTEVAP SITAHNHQHL FSLRIDPEID
GQNNSVVQSD AVSFEAPVGS PENPYGNGFY SKKTPLRTSL EGAADYCFET NRSWDIINPN
RMNTVAKKPV GYKILNNNCP PMLAKPGSTV WKRAAFARKP LWVTPYKDYE LFPAGDYVCQ
SDGSEGHPYN PTIADWAKRN ENIENTDIVC YMQFGLTHFP RTEDFPIMPA EPVSIMLRAS
NFFEKNPGLW VPPSAICVDT QSKNAFPSSC CATSKPRM
//
