ID I1QF45_ORYGL Unreviewed; 589 AA.
AC I1QF45;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=L-gulonolactone oxidase {ECO:0000256|ARBA:ARBA00013121};
DE EC=1.1.3.8 {ECO:0000256|ARBA:ARBA00013121};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA08G0004600.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA08G0004600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) 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 -!- 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 AlphaFoldDB; I1QF45; -.
DR STRING; 4538.I1QF45; -.
DR EnsemblPlants; ORGLA08G0004600.1; ORGLA08G0004600.1; ORGLA08G0004600.
DR Gramene; ORGLA08G0004600.1; ORGLA08G0004600.1; ORGLA08G0004600.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR OMA; VSWLPRQ; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
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; 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:SF90; L-GULONOLACTONE OXIDASE; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..589
FT /note="L-gulonolactone oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003650079"
FT DOMAIN 49..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 589 AA; 63649 MW; 48B4C1DEA966DBA0 CRC64;
MRTMLPLLVI LVVGLRLAGA SPPPQPVACT KGTTDCTVTN VYGSFPDRTI CRAADASFPR
TEAELVAAVA AAAAAGRKAK AATRHSHSFP KLACPGGRDG TIISTRFLNR TVAFDAAARR
ITVESGVVLR DLIRAAAAAG LALPHSPYWY GLTVGGLLAT GAHGSSLWGK GSAVHEYVVG
LRIVTPAPAS QGFAVVRELV AGDPDLDAAK VSLGVLGVIS QVTFELQPQF KRSVRFVTRD
DSDFAEKVAV WGGAHEFGDM AWLPRQGKVI YREDDRVDVA TPGNGLNDYL GFRAQPTLGL
ITARAAEERL ERNGTDIARC LAARLPPSLF ELQAYGFTND GVFFTGWPVV GFQHRIQASG
TCISSPEDGL LSSCTWDPRI RGPFLYNSGF SIALPRAAAF VADMMRLRDL NPRAFCDIDA
KLGILMRYVK ASSAYLGKPE DCVDFDVTYY RSYDDGEPRP HSDVFDELEQ MALRKYGAVP
HWGKNRNFAF DGAAAKYPNS GEFIKVKERY DPDGIFSSEW SDQVLGISGS PNIVDKRCAI
EGLCVCSDDS HCAPELGYFC RPGKLFKEAR VCSKDKSAAA GDDDLLDEL
//