ID I1PIV5_ORYGL Unreviewed; 743 AA.
AC I1PIV5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA04G0012400.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA04G0012400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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|RuleBase:RU000672}.
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DR STRING; 4538.I1PIV5; -.
DR EnsemblPlants; ORGLA04G0012400.1; ORGLA04G0012400.1; ORGLA04G0012400.
DR Gramene; ORGLA04G0012400.1; ORGLA04G0012400.1; ORGLA04G0012400.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_2_0_1; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR10638:SF18; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000672};
KW TPQ {ECO:0000256|PIRSR:PIRSR600269-51, ECO:0000256|RuleBase:RU000672}.
FT DOMAIN 404..686
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT MOD_RES 450
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 743 AA; 85314 MW; 1CDBCD3535C9C376 CRC64;
IHLLKLHLSL VYHRGEKQFQ ASRTSRGHRE ATPXTHYRLL KLLWLXQLSK LLQVLLRSEM
ACVLLKLRSW NQKRTLWHXL MHTFSLHSNH HCFLETEMLL SFQPSCHQGG PSLLSTTDRQ
MRLVFGLXNS LKCMLIVILG VDITEEASSY HQRLXFPMFN LRWMPWNLLS VKLLXKATPL
SLKPXEKEEL MTWILSQXIH GVQDITVMLM LPVEESPNLW CSVELKVITL SRMAMHDLLK
GFILSLICRT IRXXSSKIGS LSLFPHQIIX GTTLQGKHEV VLIEVMXSLX LSINLKAQVS
MSTVTLWNGR RLTGCLXCLL FXFNYWRSTX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXMXLLGFH KILXCTFSIL YGVETIENAV CLHEEDHGIL
WKHRDWRTGL AEVRRSRRLT VSFVCTIANY EYGFYWHFYQ DGKIEAEVKL TGILSVGALM
PEEQRKYGTT IAPSLYAPVH QHFFVTRMDM AVDCKPNEAY NQVVEVNVNA ECAGPNNMHN
NAFYAEEKLL KSELQAMRDC HPSSARHWIV RNTRTVNRTG QPTGYKLIPG SNCLPLPLPE
AKFLRRAGFL KHNLWVTSYK NDEMYPGGEF PNQNPRINEG LSTWVKQDRS LEETNIVLWY
VFGVTHVPRL EDWPVMPVEH IGFMLKIVFL SYIAPDNVTA LNIGTHIVFV LLQPDGFFDC
SPAIDVPLGS EVHTKKAERP RRF
//