ID   GGLO1_ARATH             Reviewed;         595 AA.
AC   Q9C614; Q9LQM9;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable L-gulonolactone oxidase 1 {ECO:0000303|PubMed:20622436};
DE            Short=AtGulLO1 {ECO:0000303|PubMed:20622436};
DE            EC=1.1.3.8 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=GULLO1 {ECO:0000303|PubMed:20622436};
GN   OrderedLocusNames=At1g32300 {ECO:0000312|Araport:AT1G32300};
GN   ORFNames=F27G20.8 {ECO:0000312|EMBL:AAG60168.1},
GN   F5D14.6 {ECO:0000312|EMBL:AAF81326.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=20622436; DOI=10.1271/bbb.100157;
RA   Maruta T., Ichikawa Y., Mieda T., Takeda T., Tamoi M., Yabuta Y.,
RA   Ishikawa T., Shigeoka S.;
RT   "The contribution of Arabidopsis homologs of L-gulono-1,4-lactone oxidase
RT   to the biosynthesis of ascorbic acid.";
RL   Biosci. Biotechnol. Biochem. 74:1494-1497(2010).
CC   -!- FUNCTION: May be involved in the biosynthesis of ascorbic acid.
CC       {ECO:0000305|PubMed:20622436}.
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:0000305};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P58710};
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC       {ECO:0000305|PubMed:20622436}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF81326.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007767; AAF81326.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC084110; AAG60168.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31461.1; -; Genomic_DNA.
DR   PIR; F86447; F86447.
DR   RefSeq; NP_564393.1; NM_102963.2.
DR   AlphaFoldDB; Q9C614; -.
DR   SMR; Q9C614; -.
DR   STRING; 3702.AT1G32300.1; -.
DR   PaxDb; Q9C614; -.
DR   PRIDE; Q9C614; -.
DR   ProteomicsDB; 221838; -.
DR   EnsemblPlants; AT1G32300.1; AT1G32300.1; AT1G32300.
DR   GeneID; 840122; -.
DR   Gramene; AT1G32300.1; AT1G32300.1; AT1G32300.
DR   KEGG; ath:AT1G32300; -.
DR   Araport; AT1G32300; -.
DR   TAIR; locus:2825463; AT1G32300.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_019762_2_0_1; -.
DR   InParanoid; Q9C614; -.
DR   OMA; NNYIAFR; -.
DR   OrthoDB; 1134169at2759; -.
DR   PhylomeDB; Q9C614; -.
DR   UniPathway; UPA00132; -.
DR   PRO; PR:Q9C614; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C614; baseline and differential.
DR   Genevisible; Q9C614; AT.
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; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 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   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   TIGRFAMs; TIGR01677; pln_FAD_oxido; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Ascorbate biosynthesis; FAD; Flavoprotein; Oxidoreductase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..595
FT                   /note="Probable L-gulonolactone oxidase 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432502"
FT   DOMAIN          47..229
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   595 AA;  65947 MW;  7FAA12855DABA380 CRC64;
     MAFWLSLIFF CFCTFASSTP PDDPVKCESG NNMCTVTNSY GAFPDRSICE AAKVEYPKTE
     AELVSIVAAA TRAGQKVRVV TRYVHSIPKL VCTDGKDGVL ISTKFLNNVV GTNPEAKTLT
     VESGVTLRQL IGEAAELELA LPHAPYWWGL TVGGLMGTGA HGSSLWGKGS AVHDYVSEIR
     MVSPGLASDG YVKVRVLSET IDPDEFRAAK VSLGVLGVIS QVTFQLQPMF KRSLTFVMQN
     DSDFGDQAVT FGEKHEFADF LWLPSQGKVV YRMDDRVPVN TSGNGLFDFF PFRPQLSVAL
     AIIRSLEESE ESSGDANDKC ARAEQITSFL FSISYGVTNN GMEFTGYPVI GKQNHMMSSG
     TCLDSHQDGL ITSCPWDPRI KGQFFHQTAF SIPLTRVKGF INDIKALVKI EPKSLCALER
     SNGILIRYVT SSPAFLGKEE KALDFDLTYY RSKDDPLAPR LYEDFIEEIE QMAIFKYNAL
     PHWGKNRNLA FDGVIRKYKN ANTFLKVKER FDPLGLFSTE WTNQILGLKG NVTIVKEGCA
     LEGLCVCSDD AHCAPKKGYL CRPGKVYTKA RVCTHVKSVN GYDDHTKFNL MFNRI