ID V4MPU5_EUTSA Unreviewed; 679 AA.
AC V4MPU5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=EUTSA_v10006982mg {ECO:0000313|EMBL:ESQ33666.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ33666.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ33666.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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 ---------------------------------------------------------------------------
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; KI517683; ESQ33666.1; -; Genomic_DNA.
DR RefSeq; XP_006415313.1; XM_006415250.1.
DR AlphaFoldDB; V4MPU5; -.
DR STRING; 72664.V4MPU5; -.
DR EnsemblPlants; ESQ33666; ESQ33666; EUTSA_v10006982mg.
DR GeneID; 18991912; -.
DR Gramene; ESQ33666; ESQ33666; EUTSA_v10006982mg.
DR KEGG; eus:EUTSA_v10006982mg; -.
DR eggNOG; KOG1186; Eukaryota.
DR OMA; MYIVATD; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000030689; 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:0009753; P:response to jasmonic acid; 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:SF84; 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; PS01165; COPPER_AMINE_OXID_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030689};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..679
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004722520"
FT DOMAIN 28..115
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 124..218
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 248..662
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 413
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 413
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 679 AA; 76528 MW; B97017D872FE850F CRC64;
MTPLHFTIFI FVSFIFASSS SRSAPPGHPF DPLTETELKL VRTIINKSYP IGPNHKFTFQ
YVGLNEPDKS LVLSWHSSVN HTVKPPPRQA FVIARDNGKS REIVVDFSSR AIVSDKIHVG
NGYPMLSSYE QEAAIELVFK FKPFHDAVTK RGLNVSEIVF TTSTIGWYGE SEAETERVVR
MLPFYLDGSV NMYLRPIEGM TILVNLDVMK VTEFKDRLTV TMPKANGKEY RLSKLKPPFG
PTLQNAVVLQ PDGPGFNVDG HIVRWANWEF HLSFDVRAGI IISLASIFDM DVNKYRQVLY
KGHLSEIFIP YMDPSDDWYF ATYFDCGDFG CGKCAVSLKP YTDCPAGAVF MDGIFAGQYG
TPTKIPNVMC IFEKYAGDIM WRHTEAEIPN LEITEVRPDV SLIARIVTTV GNYDYIVDYE
FKPSGSIKIG VGLTGVLEVK PVEYIHKSEI GEEDIQGTIV TDNTVGVNHD HFVTFRLDLD
IDGTQNSFVR NELVTKRTAK SVNTPRKSYW TTRPKTAKTE AEARVKLGLK AEELVVVNPN
RKTKHGNEAG YRILSGAATG PLLAQDDYPQ IRAAFTNYNV WITLYNRSEV WAGGLYADQS
HGDDTLAVWS QRNREIENKD IVMWYTVGFH HVPSQEDFPT MPTLSGGFEL RPTNFFEQNP
VLKSKPIKLT NAEKCIPKN
//
