GGLO2_ARATH
ID GGLO2_ARATH Reviewed; 591 AA.
AC Q6NQ66; O81031; Q0WNK2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=L-gulonolactone oxidase 2 {ECO:0000303|PubMed:20622436};
DE Short=AtGulLO2 {ECO:0000303|PubMed:20622436};
DE EC=1.1.3.8 {ECO:0000269|PubMed:20622436};
DE Flags: Precursor;
GN Name=GULLO2 {ECO:0000303|PubMed:20622436};
GN OrderedLocusNames=At2g46750 {ECO:0000312|Araport:AT2G46750};
GN ORFNames=F19D11.3 {ECO:0000312|EMBL:AAC33494.1};
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|EMBL:AAQ89618.1};
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-590.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY METHYL JASMONATE.
RX PubMed=16061506; DOI=10.1093/jxb/eri246;
RA Wolucka B.A., Goossens A., Inze D.;
RT "Methyl jasmonate stimulates the de novo biosynthesis of vitamin C in plant
RT cell suspensions.";
RL J. Exp. Bot. 56:2527-2538(2005).
RN [6]
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 -!- INDUCTION: Up-regulated by methyl jasmonate.
CC {ECO:0000269|PubMed:16061506}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33494.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005310; AAC33494.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC10748.1; -; Genomic_DNA.
DR EMBL; BT010596; AAQ89618.1; -; mRNA.
DR EMBL; AK229437; BAF01297.1; -; mRNA.
DR PIR; T02676; T02676.
DR RefSeq; NP_182198.2; NM_130241.3.
DR AlphaFoldDB; Q6NQ66; -.
DR SMR; Q6NQ66; -.
DR STRING; 3702.AT2G46750.1; -.
DR PaxDb; Q6NQ66; -.
DR PRIDE; Q6NQ66; -.
DR ProteomicsDB; 221839; -.
DR EnsemblPlants; AT2G46750.1; AT2G46750.1; AT2G46750.
DR GeneID; 819288; -.
DR Gramene; AT2G46750.1; AT2G46750.1; AT2G46750.
DR KEGG; ath:AT2G46750; -.
DR Araport; AT2G46750; -.
DR TAIR; locus:2044340; AT2G46750.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR InParanoid; Q6NQ66; -.
DR OMA; CHCAILS; -.
DR OrthoDB; 1134169at2759; -.
DR PhylomeDB; Q6NQ66; -.
DR BRENDA; 1.1.3.37; 399.
DR BRENDA; 1.1.3.8; 399.
DR UniPathway; UPA00132; -.
DR PRO; PR:Q6NQ66; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q6NQ66; baseline and differential.
DR Genevisible; Q6NQ66; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..591
FT /note="L-gulonolactone oxidase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432503"
FT DOMAIN 56..238
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 591 AA; 64970 MW; 00D3A3BF79EFB3CA CRC64;
MAFTFPPSYR TLVGLYYIFT LMHTAVSTPP DDPVKCVSGN TNCTVTNSYG AFPDRSTCRA
ANVAYPKTEA ELVSVVAAAT QAGRKMRVTT RYSHSITKLV CTDGTEGLFI STKFLNHTVQ
ADATAMTMTV ESGMTLRQLI VEAAKVGLAL PYAPYWWGLT VGGMMGTGAH GSSLWGKGSA
VHDYVTEIRM VSPGSVNEGF AKIRILSETT TPNEFNAAKV SLGVLGVISQ VTFELQPMFK
RSLTYTMRND SDFEDQAVTF GKKHEFADFI WLPSQGKVVY RRDDRVAVNT SGNGLFDFLP
FRSQLSAAIA IIRTSEETQE RFRDANGKCV GATIISSTLF APSYGLTNNG IIFTGYPVVG
SQNRMMSSGS CLDSLQDGLI TACAWDSRIK GEFFHQTTLS VPLTQVKSFI SDIKSLVKIE
QKSLCGLELH YGILMRYVTS SPAYLGKETE ALDFDITYYR AKDPLTPRLY EDFIEEIEQI
ALFKYNALPH WGKNRNLAFD GVIRKYNNAP AFLKVKDSYD PKGLFSSEWT DQILGIKGNA
SIVKDGCALE GLCICSKDAH CAPAKGYLCR PGKVYKEARV CTRVDGIISV I
