ID G0RPS5_HYPJQ Unreviewed; 748 AA.
AC G0RPS5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=TRIREDRAFT_122963 {ECO:0000313|EMBL:EGR46907.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR46907.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR46907.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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}.
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DR EMBL; GL985071; EGR46907.1; -; Genomic_DNA.
DR RefSeq; XP_006967356.1; XM_006967294.1.
DR AlphaFoldDB; G0RPS5; -.
DR STRING; 431241.G0RPS5; -.
DR EnsemblFungi; EGR46907; EGR46907; TRIREDRAFT_122963.
DR GeneID; 18483525; -.
DR KEGG; tre:TRIREDRAFT_122963; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_122963; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_1_1; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
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 PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
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:UP000008984};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 256..673
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 414
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 414
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 748 AA; 83447 MW; B4FDA362C037C8A7 CRC64;
MAVTAAPRPH PLAPLSSAEH IKARDAVAKL HGPSESIFFR AIHVQEPKKA ELQPFLEAEH
TGKLTDETKR PDRVAIVEHD VIRADRSEYI NAFVNLNTGE VATVSAPVPH QPYVTPGEFD
LFNDACINSD LFKEAMSEFV LPEGFEICID PWPYGPPNAD EKDIPRYMQG LVFAKDTRKN
NEDSNHYGYP IPIVPVMDWH TKKLIRVERI ATGGIDDELE AKVRSDEPVK LFENHKGCEY
VPELLDVPLR TDLKPINIIQ PEGASFTIQE DGLIEWQKWR FRLGFTPREG AVLHDVHYDN
RSVMYRVSFS EMTVPYTDPR PPFHRKQAFD FGDGGMGRAA NNLELGCDCL GAIHYVDALT
TEPDGAPSPA KAVVCLHEQD NGILWKHTNF RTNRAVVTRN REFVVQFIAT LANYEYVLAY
KLDLAGSITL ETRATGIVSV TSIDEGKVSA YGNIMTPGVL AQNHQHIFAV RIDPAIDSYN
DAESQVVIEE SHGQKIDPKT NPYGNFYKVQ REKVEQATWI DAEPRLNRLL KLENANKKNL
ISGKNLAYKL VAPVTQMLLA DPEGLAAQRA QFAQHNAWVT GYRDGELWAA GEFTNQSTRE
VGGVADMVKR GDWFTDRETN GDAEGQGKRS SPVVWSVFGL THNPRVEDWP VMPVETFQIH
IRPTDFFNVN PAIDVPSTRN NASVLLGGSC CTTSSDKNTS AVQQHPVTHL QGSAPSIDPK
AVGAHVDEKL SKRLSKTFNG LFTKKESK
//
