GGLO5_ARATH
ID GGLO5_ARATH Reviewed; 590 AA.
AC O81030;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=L-gulonolactone oxidase 5 {ECO:0000303|PubMed:20622436};
DE Short=AtGulLO5 {ECO:0000303|PubMed:20622436};
DE EC=1.1.3.8 {ECO:0000269|PubMed:20622436};
DE Flags: Precursor;
GN Name=GULLO5 {ECO:0000303|PubMed:20622436};
GN OrderedLocusNames=At2g46740 {ECO:0000312|Araport:AT2G46740};
GN ORFNames=F19D11.2 {ECO:0000312|EMBL:AEC10747.1};
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, AND CATALYTIC ACTIVITY.
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: Catalyzes the oxidation of L-gulono-1,4-lactone to ascorbic
CC acid (PubMed:20622436). L-gulono-1,4-lactone is oxidized to hydrogen
CC peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to
CC L-ascorbate (By similarity). {ECO:0000250|UniProtKB:P58710,
CC ECO:0000269|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:0000269|PubMed:20622436};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P58710};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC {ECO:0000269|PubMed:20622436}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC005310; AAC33493.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10747.1; -; Genomic_DNA.
DR PIR; T02675; T02675.
DR RefSeq; NP_182197.1; NM_130240.3.
DR AlphaFoldDB; O81030; -.
DR SMR; O81030; -.
DR STRING; 3702.AT2G46740.1; -.
DR PaxDb; O81030; -.
DR PRIDE; O81030; -.
DR ProteomicsDB; 224781; -.
DR EnsemblPlants; AT2G46740.1; AT2G46740.1; AT2G46740.
DR GeneID; 819287; -.
DR Gramene; AT2G46740.1; AT2G46740.1; AT2G46740.
DR KEGG; ath:AT2G46740; -.
DR Araport; AT2G46740; -.
DR TAIR; locus:2044330; AT2G46740.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR InParanoid; O81030; -.
DR OMA; TFELQAY; -.
DR OrthoDB; 1134169at2759; -.
DR PhylomeDB; O81030; -.
DR BioCyc; ARA:AT2G46740-MON; -.
DR BioCyc; MetaCyc:GQT-4288-MON; -.
DR BRENDA; 1.1.3.37; 399.
DR BRENDA; 1.1.3.8; 399.
DR UniPathway; UPA00132; -.
DR PRO; PR:O81030; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81030; baseline and differential.
DR Genevisible; O81030; 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; IMP:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Ascorbate biosynthesis; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..590
FT /note="L-gulonolactone oxidase 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432506"
FT DOMAIN 60..242
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 590 AA; 64890 MW; DB98C44E57321533 CRC64;
MAFGYSPSYC SFWRTLLGLY CLFTLVHTVI STPPEDPVKC VSGNTNCIVT NSLGAFPDRS
TCRAANVAYP TTEAELVSIV AAATKAGRKM RVTTRYSHSI PKLTCTDGND GLFISTKFLN
HTVQADAKAM TLTVESGVTL RQLIAEAAKV GLALPYAPYW WGVTVGGMMG TGAHGSSLWG
KGSAVHDYVT EIRMVSPGSV NDGFAKIRVL SETTTPNEFN AAKVSLGVLG VISQVTFELQ
PMFKRSLKYV MRNDLDFNDE ALTFGKKHEF ADFVWLPSQG KVVYRMDDRV AVNTLGNGLY
DFFPFRSQLS AVLATTRSSE ETQETLRDAH GKCVTATTIS STLFSTSYGL TNNGITFTGY
PVIGSQNRMM SSGSCLDGLE DKLTSACAWD SRVKGVFYHQ TTFSIPLTQV KSFINDIKSL
LKIDSKSLCG LELYYGILMR YVTSSPAYLG KETEAIDFDI TYYRANDPLT PRLYEDFIEE
IEQIALLKYN ALPHWGKNRN LAFDGVIKKY KNAPAFLKVK ESYDPNGLFS SEWTDQILGI
KGNPTIVKDG CALEGLCICS DDAHCAPSKG YLCRPGKVYK EARVCTHVPK
