ID D8T1Z4_SELML Unreviewed; 570 AA.
AC D8T1Z4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, 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 ORFNames=SELMODRAFT_235822 {ECO:0000313|EMBL:EFJ09316.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ09316.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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 EMBL; GL377664; EFJ09316.1; -; Genomic_DNA.
DR RefSeq; XP_002989646.1; XM_002989600.1.
DR AlphaFoldDB; D8T1Z4; -.
DR STRING; 88036.D8T1Z4; -.
DR EnsemblPlants; EFJ09316; EFJ09316; SELMODRAFT_235822.
DR GeneID; 9637144; -.
DR Gramene; EFJ09316; EFJ09316; SELMODRAFT_235822.
DR KEGG; smo:SELMODRAFT_235822; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR InParanoid; D8T1Z4; -.
DR OMA; MNASFVC; -.
DR OrthoDB; 313562at2759; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000001514; 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: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 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: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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..570
FT /note="L-gulonolactone oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003123229"
FT DOMAIN 38..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 268..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 62028 MW; BC9CE8E7CFAA6B5E CRC64;
MILLLCCSSA VAILPISCGS GSSACTLQNY QGIWYERALC GVANVAYPTT EAELVAAVAS
GVQQRQKIKV VSKLSHSLVR AACPGGSSGL LISTSRYDSR IVIDSNAMTV TADAGVQLQD
LLARLAAQNL ALPCTPYFNG LSIAGVISTG SHGSSLLGKG GAVHDYVSGI TIVVPASREQ
GYAKVIKLGK SSPDLNAAKL SIGVLGAIST VTLDVEPMFK RSITKQARDD STLENDVAGF
ASRYAFGDIN WYISQKKILL RVDNKVSAST PGEGRNAGND PAPETNVRQS RVREENFMSQ
MNASFVCQQS LNGVENRVSS GDGLVNDRSN TFRGYPVVGF NHQLQTAGGC QNTALNNTRS
ASGERLTCYW DPDVPGQFYF QTSLAIPLSR INEAIQDIKK IRDGMDPTKL CGANIYGGAQ
LRFIKGSTAY LAEPEDSVAF ELLYFRDRRQ NMPRLDQDAT DEIEQMLLKK YKGRPHWGKN
KNAMFEDMGS RVTNLAKFLE VRQRYDPDGY FSSEWSDAVL GIKQNASVYR DYCALEGLCL
CKEDRHCAPE RGFLCKPGLV FTDARVCRRA
//
