ID K3YR27_SETIT Unreviewed; 590 AA.
AC K3YR27;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=L-gulonolactone oxidase {ECO:0000256|ARBA:ARBA00013121};
DE EC=1.1.3.8 {ECO:0000256|ARBA:ARBA00013121};
GN Name=101776642 {ECO:0000313|EnsemblPlants:KQL29207};
GN ORFNames=SETIT_1G127500v2 {ECO:0000313|EMBL:RCV05993.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV05993.1};
RN [1] {ECO:0000313|EMBL:RCV05993.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL29207,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV05993.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV05993.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV05993.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL29207}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL29207};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate;
CC Xref=Rhea:RHEA:32363, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17587, ChEBI:CHEBI:38290; EC=1.1.3.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001630};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005147}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; AGNK02000185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003528; RCV05993.1; -; Genomic_DNA.
DR RefSeq; XP_004952251.1; XM_004952194.2.
DR AlphaFoldDB; K3YR27; -.
DR STRING; 4555.K3YR27; -.
DR EnsemblPlants; KQL29207; KQL29207; SETIT_016721mg.
DR GeneID; 101776642; -.
DR Gramene; KQL29207; KQL29207; SETIT_016721mg.
DR KEGG; sita:101776642; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR InParanoid; K3YR27; -.
DR OMA; KFGRPYF; -.
DR OrthoDB; 885025at2759; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000004995; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050105; F:L-gulonolactone oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010030; GULO_Plant.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR01677; pln_FAD_oxido; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..590
FT /note="L-gulonolactone oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010127066"
FT DOMAIN 54..237
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 590 AA; 62977 MW; 33E2FAA6164BBB1A CRC64;
MRATFLLLLL LLLSCHAPAP ALSLPPRPPV RCGSGDNAAC VLSNAYAAWS SDRADCPVSA
VAYPASEREV VAAVARASAD GARIKVVSGF AHTIPKLACP GGGGGNASTL LISTARLAAV
EVDAAARTVT ADAGAPLRAV IDAAEARGLS LTAAPYWEGV SIGGLVSTGS HGSSWWGRGG
AVHDHVVGLR LVAPAGEADG WARVLPLRRG DELFPAALVS LGLLGVITKI TLSLEPRFKR
SITYEYRDDS TFQDDFAAHA ARHEFADITW YPSQHTAVYR VDDRAPLNAS GDGVNDFIGF
QPTAIAVTAG LRALETSLER SRNVRGKCAM AAVEGAAKRL VGNGLKNNGL LFTGYPVVGY
QGKMQTSGSC ARSPASDLLR ACGWDPRFRG LFFYESTAIF SPPARFRDFV LDVKRLRDAA
GAESLCGVDV YNGLLVRFVR ASAAHLGQPE DSVVVDFNYY RASDPAAPRL SGDVWEEVEQ
LAFVKHGARP HWAKNRLVAF AGVRGKYPRW GQFAAAKRRL DPRGLFDSPW SDEVVGGVEV
EVDKGDGCAL DGRCVCLEDR HCSPGQGYYC RPGLVFTEAR VCRYSVSQNQ
//
