(data stored in ACNUC8465 zone)

SWISSPROT: B6H1Y2_PENRW

ID   B6H1Y2_PENRW            Unreviewed;       676 AA.
AC   B6H1Y2;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=Pc13g03350 {ECO:0000313|EMBL:CAP91404.1}, PCH_Pc13g03350
GN   {ECO:0000313|EMBL:CAP91404.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 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:CAP91404.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91404.1, 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.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., 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=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
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   -!- COFACTOR:
CC       Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600269-51};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|PIRSR:PIRSR600269-51};
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent
CC       autoxidation of a specific tyrosyl residue.
CC       {ECO:0000256|PIRSR:PIRSR600269-51, ECO:0000256|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|RuleBase:RU000672}.
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DR   EMBL; AM920428; CAP91404.1; -; Genomic_DNA.
DR   RefSeq; XP_002558773.1; XM_002558727.1.
DR   STRING; 500485.XP_002558773.1; -.
DR   EnsemblFungi; CAP91404; CAP91404; PCH_Pc13g03350.
DR   GeneID; 8313435; -.
DR   KEGG; pcs:Pc13g03350; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   eggNOG; COG3733; LUCA.
DR   HOGENOM; HOG000250947; -.
DR   KO; K00276; -.
DR   OMA; APYPRKA; -.
DR   OrthoDB; EOG092C1J1W; -.
DR   BioCyc; PCHR:PC13G03350-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
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; 2.70.98.20; -; 1.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR   InterPro; IPR015800; Cu_amine_oxidase_N2.
DR   PANTHER; PTHR10638; PTHR10638; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   SUPFAM; SSF49998; SSF49998; 1.
DR   SUPFAM; SSF54416; SSF54416; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H1Y2.
DR   SWISS-2DPAGE; B6H1Y2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Copper {ECO:0000256|RuleBase:RU000672};
KW   Metal-binding {ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   TPQ {ECO:0000256|PIRSR:PIRSR600269-50, ECO:0000256|RuleBase:RU000672}.
FT   DOMAIN        2     94       Cu_amine_oxidN2. {ECO:0000259|Pfam:
FT                                PF02727}.
FT   DOMAIN      240    648       Cu_amine_oxid. {ECO:0000259|Pfam:
FT                                PF01179}.
FT   ACT_SITE    312    312       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR600269-50}.
FT   ACT_SITE    396    396       Schiff-base intermediate with substrate;
FT                                via topaquinone. {ECO:0000256|PIRSR:
FT                                PIRSR600269-50}.
FT   MOD_RES     396    396       2',4',5'-topaquinone. {ECO:0000256|PIRSR:
FT                                PIRSR600269-51}.
SQ   SEQUENCE   676 AA;  76534 MW;  2CC921C653676CF8 CRC64;
     MHPFDPLSPA EISEVTAIVR THFPGQLPVF RFITLKEPAK LEMLPFLENE HRGLPNITRP
     ARTSRVQVVM RSDKGENQLI ELLVDLDNKR VIKNEHLVGR HSYIDADYMR LVESACLADP
     KVQDEIKKLK LPANSTVIVE PWAYGTDGIN DMSERISMCW FYLRLLDNPD ANYYAYPLDL
     CAEVSEELKV TKIYYLPSSQ EERISDQARP FDINRIHSTV DSEYHPSLRP PPRNTTKPYQ
     VVQPEGPSFS TQGNRISWEK WTMRVGFNYR EGLTLHDIRY DGRSLFYRLS LAEMFVPYGD
     PRAPYPRKAA FDLGSDGAGV NANNLRLGCD CLGLIKYFDA WHNTSSGEPL KLPNVVCCHE
     QDDGILWKHT NFRTQNAVVA RARILVLQTI ITVSNYEYIF AFQFSQDASI HYEVRATGIL
     STCPINIGDK VPYGTIVAPG VLAPYHQHLF CLRMDPWVDG NVQNTLQVEE SHAMPISDTN
     PFGVGYTTSS NNITEETGLD LDISKNRTFK IINEHSINPI TGTPVGFKLL PSYSQMLLAH
     PDSYHAHRSE YAAHAVWVTR YDDEEMFPAG RHTMQSTGGE GIHSAITRRK NDGSKTSVRN
     EDIVLWHTFG STHNPRIEDW PVMPMDRMVV GIKPVNFFTG NPGLDVPPST QERNRSVLVN
     GDSDSLKSSS DTCCRL
//

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