ID A0A371EXK8_MUCPR Unreviewed; 694 AA.
AC A0A371EXK8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
DE Flags: Fragment;
GN ORFNames=CR513_49975 {ECO:0000313|EMBL:RDX70751.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX70751.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDX70751.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDX70751.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDX70751.1}.
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; QJKJ01011585; RDX70751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371EXK8; -.
DR STRING; 157652.A0A371EXK8; -.
DR Proteomes; UP000257109; 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 GO; GO:0042221; P:response to chemical; IEA:UniProt.
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:SF68; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 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}; Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..694
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016721183"
FT DOMAIN 48..131
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 140..237
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 264..674
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 427
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 427
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDX70751.1"
SQ SEQUENCE 694 AA; 78641 MW; 5506B817671A713F CRC64;
MIVIPSTTEQ VSSTACTMKL FHLFSLLTLL FWFQVEAGVS VDPLQLSHPL DPLTKQEITR
IQVLVLKKYP TSQNRVSFHY VGLDDPEKAT VLKWVSSGAR TGPRKAFVIA IINSQIHELT
INLGSSNVVS DKVQHRNGFP TLTLEEQNEA IALPLTYGPF VESMKKRGLN LSEVVCSFFT
VGWYGETEIS RRTLRIECYL KEGTANIYMR PIGGISILVD INQMKIIEYH DNAILPVPKA
ENTEYRASNM KPPLAPTFHS YGSHQPQGPG FTIKGHTLSW ANWKFHIGYD MRAGVMISTA
SIYDSEVHKY RQVLYRGYIS ELFVPYQDPS EEWYCRTYFD AGEFGFGQSM VALEPLHDCP
PQAQFLDVYF AGRDGSPQHL ENAICVFEQY GGISWRHTES AIPNEKIREV RSDVTLIVRS
VITIGNYDNI IDWEFKPSGS IKPAISLSGM LEIKAVNITH KEEIKNDQHG TLISEHSIGV
YHDHYYIYHL DFDIDGVDNS FVKTNLKTVQ VTDHSSKRKS YWTTSSEIAK TESDAKTKLG
FSPSVLAMVN PNKKTSTGNE VGYRLVPSAA VHSLLTEDDY PQIRGAFTNY NVWVTPYNRS
EKWAGGLYVD QSRGEDTLPV WTKQNRDIEN KDIVLWYVVG IHHVPCQEDF PIMPLLSTGF
ELRPTNFFER NPVLKTLSPD MVKWPSCGKS FISF
//
