GGLO6_ARATH
ID GGLO6_ARATH Reviewed; 603 AA.
AC O81032;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable L-gulonolactone oxidase 6 {ECO:0000303|PubMed:20622436};
DE Short=AtGulLO6 {ECO:0000303|PubMed:20622436};
DE EC=1.1.3.8 {ECO:0000305};
DE Flags: Precursor;
GN Name=GULLO6 {ECO:0000303|PubMed:20622436};
GN OrderedLocusNames=At2g46760 {ECO:0000312|Araport:AT2G46760};
GN ORFNames=F19D11.4 {ECO:0000312|EMBL:AAC33495.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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}.
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DR EMBL; AC005310; AAC33495.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10749.1; -; Genomic_DNA.
DR PIR; T02677; T02677.
DR RefSeq; NP_182199.1; NM_130242.2.
DR AlphaFoldDB; O81032; -.
DR SMR; O81032; -.
DR STRING; 3702.AT2G46760.1; -.
DR PaxDb; O81032; -.
DR PRIDE; O81032; -.
DR ProteomicsDB; 224782; -.
DR EnsemblPlants; AT2G46760.1; AT2G46760.1; AT2G46760.
DR GeneID; 819289; -.
DR Gramene; AT2G46760.1; AT2G46760.1; AT2G46760.
DR KEGG; ath:AT2G46760; -.
DR Araport; AT2G46760; -.
DR TAIR; locus:2044350; AT2G46760.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR InParanoid; O81032; -.
DR OMA; KCAGATL; -.
DR OrthoDB; 1134169at2759; -.
DR PhylomeDB; O81032; -.
DR UniPathway; UPA00132; -.
DR PRO; PR:O81032; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81032; baseline and differential.
DR Genevisible; O81032; 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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..603
FT /note="Probable L-gulonolactone oxidase 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432507"
FT DOMAIN 64..246
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 603 AA; 66282 MW; BCB3ECE9EEC8C391 CRC64;
MAFTSSPSYG SLNAAFWRTI FVVHCISTLV FTTISTPPED PVKCVSGNTN CTVTNSYGAF
PDRSTCRAAN VAYPTTEAEL ISVVAAATKA GRKMRVTTRY SHSITKLACT DGTDGLLIST
KFLNHTVRTD ATAMTLTVES GVTLRQLIAE AAKVGLALPY APYWWGLTVG GMMGTGAHGS
SLWGKGSAVH DYVTEIRIVS PGSVNDGFAK VRVLRETTTP KEFNAAKVSL GVLGVISQVT
LKLQPMFKRS LRYVMRNDSD FGDQAVTFGM KHEFADFIWL PSQGKVVYRM DDRVAVNTSG
NGLLDFMPFR SQLSAALAII RSSEETQERF RDANGKCAGA TLITSTLFAT SYGLTNNGMI
FTGYPVIGSQ NRMMSSGSCL DSLHDGLITA CPWDSRIKSE FFHQTTFSIP LTQVKSFIND
IKSLVKIESK SLCVLELYDG ILMRYVTSSP AYLGKETEAL DFDLTYYRAK DPLSPRLYED
FIEEIEQIAL FKYNALPHWG KNRNLAFDGV IKKYKNVPAF LKVKESYDPM GLFSSEWTDQ
ILGIKGNVTI IKDGCALEGL CVCSEDAHCA PTKGYFCRPG KVYKEARVCT RADDISVIQS
LSY
