ID   GGLO4_ARATH             Reviewed;         577 AA.
AC   Q9FM82; Q84W90;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Probable L-gulonolactone oxidase 4 {ECO:0000303|PubMed:20622436};
DE            Short=AtGulLO4 {ECO:0000303|PubMed:20622436};
DE            EC=1.1.3.8 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=GULLO4 {ECO:0000303|PubMed:20622436};
GN   OrderedLocusNames=At5g56490 {ECO:0000312|Araport:AT5G56490};
GN   ORFNames=MCD7.26 {ECO:0000312|EMBL:BAB11277.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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   ---------------------------------------------------------------------------
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   EMBL; AB009049; BAB11277.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96772.1; -; Genomic_DNA.
DR   EMBL; BT004109; AAO42132.1; -; mRNA.
DR   RefSeq; NP_200460.1; NM_125032.4.
DR   AlphaFoldDB; Q9FM82; -.
DR   SMR; Q9FM82; -.
DR   STRING; 3702.AT5G56490.1; -.
DR   PaxDb; Q9FM82; -.
DR   PRIDE; Q9FM82; -.
DR   ProteomicsDB; 224780; -.
DR   EnsemblPlants; AT5G56490.1; AT5G56490.1; AT5G56490.
DR   GeneID; 835750; -.
DR   Gramene; AT5G56490.1; AT5G56490.1; AT5G56490.
DR   KEGG; ath:AT5G56490; -.
DR   Araport; AT5G56490; -.
DR   TAIR; locus:2161033; AT5G56490.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_019762_2_0_1; -.
DR   InParanoid; Q9FM82; -.
DR   OMA; SGRVMQE; -.
DR   OrthoDB; 1134169at2759; -.
DR   PhylomeDB; Q9FM82; -.
DR   UniPathway; UPA00132; -.
DR   PRO; PR:Q9FM82; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FM82; baseline and differential.
DR   Genevisible; Q9FM82; 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   2: Evidence at transcript level;
KW   Ascorbate biosynthesis; FAD; Flavoprotein; Oxidoreductase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..577
FT                   /note="Probable L-gulonolactone oxidase 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432505"
FT   DOMAIN          46..228
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   CONFLICT        186
FT                   /note="A -> V (in Ref. 3; AAO42132)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   577 AA;  64124 MW;  D7421BA2AF62D3B9 CRC64;
     MSFWLSLIFC FFTFASSSPP DDPVNCEFGN TMCTVTNSYG AFPDRSICKA AKVEYPRTEA
     ELVSIVAAAT RAGQKMRVVT RYSHSFPKLV CTDGKDGTLI STKFLNHVVT TNPEAKTLTV
     ESGVTLRQLI EEAAKFDLAL PYAPYWWGLT VGGMMGTGAH GSSLWGKGSA VHDYVTEIRL
     VSPGLASDGY VKVQVLSETI DPEEFRAAKV SLGVLGVISQ VTFELQPMFK RSLNYVMRND
     SDFGDQAVSF GERHEFADFL WLPSQGKVVY RMDGRVPLNT SGDGLFEFFP FRSQLSLVLA
     IDRSLEESEE SLEDANMKCV RAKLVSSSMF LMSYGVTNNG LIFTGYPVIG MQNHMMSSGS
     CLDSRQDGLI TACPWDPRIK GQFFHQTTFS VSLTNVKSFI NDIKALVKIE PKSLCVLEGS
     NGILIRYVTS SLAFLGKEEK ALDFDLTYYR SKNDPLAPRL YEDYIEEIEQ MAIFKYNALP
     HWGKNRNLAF DGAIRKYKNA NAFLKVKEKF DSLGLFSTEW TDQILGLKGN VTIVKQGCAL
     EGLCICSEDS HCAPTKGYLC RPGKVYREAR VCTRVSS