ID A0A0S3S8E0_PHAAN Unreviewed; 577 AA.
AC A0A0S3S8E0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=L-ascorbate oxidase {ECO:0000256|ARBA:ARBA00022095};
DE EC=1.10.3.3 {ECO:0000256|ARBA:ARBA00012301};
GN Name=Vigan.05G275800 {ECO:0000313|EMBL:BAT89075.1};
GN ORFNames=VIGAN_05275800 {ECO:0000313|EMBL:BAT89075.1};
OS Vigna angularis var. angularis.
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; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT89075.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT89075.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate
CC radical; Xref=Rhea:RHEA:30243, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=1.10.3.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000516};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SUBUNIT: Dimer. {ECO:0000256|ARBA:ARBA00011473}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; AP015038; BAT89075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3S8E0; -.
DR Proteomes; UP000291084; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008447; F:L-ascorbate oxidase activity; IEA:UniProtKB-EC.
DR CDD; cd13893; CuRO_3_AAO; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034267; CuRO_3_AAO.
DR InterPro; IPR017760; L-ascorbate_oxidase_pln.
DR NCBIfam; TIGR03388; ascorbase; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF394; PLASTOCYANIN-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..577
FT /note="L-ascorbate oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006617924"
FT DOMAIN 37..148
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 162..325
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 435..550
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 577 AA; 64564 MW; E7695E6750BE6084 CRC64;
MMRIMGLRAV IVWCIWLGLI EFSVGGRVRH YKFDVEYIIK KPDCLEHVVM GINGQFPGPT
IRAEVGDTLN IALTNKLFTE GTVIHWHGIR QVGTPWADGT AAISQCAINP GETFNYRFIV
DRPGTYFYHG HHGMQRAAGL YGSLIVDLPK GQNESFHYDG EFNLLLSDLW HISSHEQEVG
LSSKPLKWIG EPQTLLINGR GQFNCSLEAK FGNTTLPECQ FKGGEECAPQ ILHVEPNKTY
RIRVASTTSL TALNLAISDH KLVVVEADGN YVTPFVVDDM DIYSGETYSV LLRTDQDPNK
NYWLSIGVRG RKPNTTQGLT ILNYKTISAS VFPTSPPPVT PLWNDFERSK AFTKKIIAKM
GTPQPPQRSD RTIFLLNTQN RVHGFTKWSI NNVSLTLPAT PYLGSIKFKL NDAFDQTPPP
VTYPQEYDIF NPPVNPNSTV GNGVYKFNLG EVVDVILQNA NQLSGNGSEI HPWHLHGHDF
WVLGYGEGKF KQGDEKKFNL THAPLRNTAV IFPYGWTALR FKADNPGVWA FHCHIEPHLH
MGMGVIFAEG VHKVGKIPRE ALTCGLTGKK LVENGHY
//
