ID A0A0D9VBL4_9ORYZ Unreviewed; 613 AA.
AC A0A0D9VBL4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=L-gulonolactone oxidase {ECO:0000256|ARBA:ARBA00013121};
DE EC=1.1.3.8 {ECO:0000256|ARBA:ARBA00013121};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G01710.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR02G01710.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR02G01710.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR02G01710.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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}.
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 AlphaFoldDB; A0A0D9VBL4; -.
DR STRING; 77586.A0A0D9VBL4; -.
DR EnsemblPlants; LPERR02G01710.1; LPERR02G01710.1; LPERR02G01710.
DR Gramene; LPERR02G01710.1; LPERR02G01710.1; LPERR02G01710.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000032180; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..254
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 613 AA; 65614 MW; 48EA89238BD4735F CRC64;
MQLLHQTGHV NRQLITRRGG VLLLAAVHLM IVCVNYVHFA GANPPAGPVR CAPGTFTNCT
VSNAYGAFPD RSTCHVAAVA YPKSEHDLVA VVAAAARSKT KVKVTTRYGH SEPKLSCPGD
GGGGGIAIST DALSRVVGVD EARREITVEG GVLLSDLVDA AAGAGLALPH SPYWLGLTIG
GLLSTGAHGS SLWGKGSAVH EYVVGMRIVT PAPASEGYAK VRVLAAGDPE MDAAKVSLGV
LGVISQVTLA LQPMFKRSVA FQMLDDSDLA ERIVAFANEH EFGDILWLPG HHKAVYRIDD
RVPHDEHHND DAIYDLSAAR STPTRTIQSK RLEEETQEAT RNATGKCVSS SAFIAQLAAD
NYGVKIHNVL PPPQPGAALI GYQNKIQASG TCLDSPDDDG LATACPWDPR VERGAFYYND
AIGVPASRAA AFVRDAQRLR AVSPHAALCG VELYYSVLVR YVKASTAYLG KPEDSVEFDF
TFYRSRGVSP RLNEDVIDEI ELMAWRKYGA TPHWGKNRNI AFDGVAGKFP KIDEFLKVKD
AYDPEGLFSS EWSDQVLGVA GAGGVSVVRD GCALEGLCVC SEDAHCAPKK GYLCRPGRVY
HEARVCRLVA NNV
//
