ID A0A176VX22_MARPO Unreviewed; 526 AA.
AC A0A176VX22;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Amine oxidase domain-containing protein {ECO:0000259|Pfam:PF01593};
GN ORFNames=AXG93_1988s1270 {ECO:0000313|EMBL:OAE24822.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24822.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE24822.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24822.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000256|ARBA:ARBA00004723}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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:OAE24822.1}.
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DR EMBL; LVLJ01002473; OAE24822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VX22; -.
DR OrthoDB; 3032570at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0046592; F:polyamine oxidase activity; IEA:UniProt.
DR GO; GO:0006598; P:polyamine catabolic process; IEA:UniProt.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF313; POLYAMINE OXIDASE 2; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..526
FT /note="Amine oxidase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008052162"
FT DOMAIN 35..464
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 526 AA; 58131 MW; 406037867672DAD8 CRC64;
MVTAVYVVLF LSAVAFHALA AEDVNVDVII IGAGMAGIAA GRTLTEMGIT NFVILEATDR
VGGRIRNTDF AGMKVEMGAN WVEGVNGKEL NPVWDLAKQV NLRTILTDTS NLSSNVYDAS
GALPPQIQAQ AMATAQNEYV NSLSATLTAN NDDDVSVLTA QRLFGSVAST PVEMALDYQL
YDGEFAEPPR VTSLKNTQPL PTFENFGEDS YFAADPRGFA TIIQPVASYL KNTNGTIEDP
RLMLNKVVNK IAYGDWGVSV STEDGATYTA KAAIATVSLG VLQSKLINFE PDLPFWKLEA
IFEFNMAIYT KIFLKFPSKF WRTDPGTEFF LYADDSRGYY PVWQHLEREF PGSNIIFVTV
TDDESRRIEQ QSDNQTLSEI MDVLRKMYGP TIPMAEEILI PRWWSNRFFK GTFSNWPIGV
TSREFAELQA PIDRLYFAGE HTSADYNGYI HGAYFTGIDA AKSVATCLKQ GQCVSGSTKQ
KNKTKGKKLM EASVCAAPIK EELDAQRQHW VKKVKLVEEA LAAKCA
//
