ID J3L967_ORYBR Unreviewed; 601 AA.
AC J3L967;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=L-gulonolactone oxidase {ECO:0000256|ARBA:ARBA00013121};
DE EC=1.1.3.8 {ECO:0000256|ARBA:ARBA00013121};
GN Name=102714071 {ECO:0000313|EnsemblPlants:OB02G11840.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB02G11840.1};
RN [1] {ECO:0000313|EnsemblPlants:OB02G11840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB02G11840.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB02G11840.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) 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 RefSeq; XP_015689165.1; XM_015833679.1.
DR AlphaFoldDB; J3L967; -.
DR STRING; 4533.J3L967; -.
DR EnsemblPlants; OB02G11840.1; OB02G11840.1; OB02G11840.
DR GeneID; 102714071; -.
DR Gramene; OB02G11840.1; OB02G11840.1; OB02G11840.
DR KEGG; obr:102714071; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR OMA; PEDHIKC; -.
DR OrthoDB; 885025at2759; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000006038; Chromosome 2.
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: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 InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR010030; GULO_Plant.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR NCBIfam; TIGR01677; pln_FAD_oxido; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF117; OS08G0519100 PROTEIN; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..601
FT /note="L-gulonolactone oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003772392"
FT DOMAIN 60..242
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 601 AA; 63590 MW; 51E4A398E1218CD4 CRC64;
MHGVPLLLRL LAAVQLVALC VDSVRFAGAS PPAGPVRCAP ASGTANCTLT NAYGAFPDRS
TCRAAAVAYP ASEQELLRVV AGAVESRTRM KVATRYGHSV PKLACPGDGG GAGLLISTDA
LNRVVSVDAG RMEITVESGV LLSELIDAAA EARLALPNSP YWLGLTVGGL LSTGAHGSSL
WGKGSAAHEN VVAMRIVTPA PASEGYAKVR VLGAGDPELD AAKVSLGVLG VISQITLALQ
PMFMRSVAFR QRDDGDLAER VVAFAGEHEF ADILWLLSQR KTVYRVDDRV PNSTTDDGAV
YDLVTFRATP TPTIQASRLG EDALEATGNA AGKCLAGSAT TANLVAGNYG VTKRGMLAPF
PGTPVVGYQN RIQSSRGSCL TSADDGLLTA CTWDPRVEHH AFFFQSGLSV PLSKAAAFIR
DVQRLRDLSD PDALCGLDIY YGVLLRFVGA STAHLGKPED SVEFDITYYR SRDDPAAPRL
HEDVLEEIEQ MALRKYGGVP HWGKNRNVAF DGAIARYPNA GEFLKVKGTY DPDGLFSSEW
SDQVLGVAGA GGVSVVRNGC ALEGLCVCSE DAHCSPEKGY LCRSGRVYEE ARVCRRVTGD
L
//
