GGLO3_ARATH
ID GGLO3_ARATH Reviewed; 585 AA.
AC Q9LYD8;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=L-gulonolactone oxidase 3 {ECO:0000303|PubMed:20622436};
DE Short=AtGulLO3 {ECO:0000303|PubMed:20622436};
DE EC=1.1.3.8 {ECO:0000269|PubMed:20622436};
DE Flags: Precursor;
GN Name=GULLO3 {ECO:0000303|PubMed:20622436};
GN OrderedLocusNames=At5g11540 {ECO:0000312|Araport:AT5G11540};
GN ORFNames=F15N18.130 {ECO:0000312|EMBL:CAB87714.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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, 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).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=23738689; DOI=10.1111/tpj.12257;
RA Shen J., Suen P.K., Wang X., Lin Y., Lo S.W., Rojo E., Jiang L.;
RT "An in vivo expression system for the identification of cargo proteins of
RT vacuolar sorting receptors in Arabidopsis culture cells.";
RL Plant J. 75:1003-1017(2013).
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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305|PubMed:23738689}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AL163815; CAB87714.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91693.1; -; Genomic_DNA.
DR PIR; T48513; T48513.
DR RefSeq; NP_196715.1; NM_121192.2.
DR AlphaFoldDB; Q9LYD8; -.
DR SMR; Q9LYD8; -.
DR STRING; 3702.AT5G11540.1; -.
DR PaxDb; Q9LYD8; -.
DR PRIDE; Q9LYD8; -.
DR ProteomicsDB; 224779; -.
DR EnsemblPlants; AT5G11540.1; AT5G11540.1; AT5G11540.
DR GeneID; 831026; -.
DR Gramene; AT5G11540.1; AT5G11540.1; AT5G11540.
DR KEGG; ath:AT5G11540; -.
DR Araport; AT5G11540; -.
DR TAIR; locus:2144251; AT5G11540.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_019762_2_0_1; -.
DR InParanoid; Q9LYD8; -.
DR OMA; TANLWWW; -.
DR OrthoDB; 1134169at2759; -.
DR PhylomeDB; Q9LYD8; -.
DR BioCyc; ARA:AT5G11540-MON; -.
DR BioCyc; MetaCyc:GQT-4735-MON; -.
DR BRENDA; 1.1.3.37; 399.
DR BRENDA; 1.1.3.8; 399.
DR UniPathway; UPA00132; -.
DR PRO; PR:Q9LYD8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYD8; baseline and differential.
DR Genevisible; Q9LYD8; AT.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..585
FT /note="L-gulonolactone oxidase 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432504"
FT DOMAIN 51..233
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 585 AA; 64961 MW; A0578E45DD6AEDCF CRC64;
MRYSHTLQQF SILSFFVTIW TVQSVPPQPP IRCDQTGCTV SNAYGTWPDR KTCHAANVTY
PTTEEDLRKA VAYAAEHNLK VKTVTKFSHT IPKLACPSGS DALLISTSKY NSVIEIEPEL
LTVTADSGVS LRELIEKVEG AGFSIGTSPY WEGVSIGGLI STGSHGSSWS GRGGSVHDHV
VGISLVVPAN QSEGFAKVVR LEEGRDDTLL NAVKVSLGVL GVISKVKLSI EKAFKRSVTY
NFTSDVALED IFMEHGKKYE FGDITWYPSR KTAVYRYDIR APVNVSGNGV NDFLGFQSNP
ILISKGVRAL EKGFESSKNE NGKCTTADTT LAYKKLIGNG LKNSGLIFTG YPVIGRQGKI
QTSGSCLYSS SIRIDVACAW DPRYNGLFFY ETTAIFPVSR FRDFLLDVKK LRDMKPERLC
GIDIYNGIFI RFIKGSKAYL GQTEDSVVID FNYYRADDEL TPRLNQDVME EMEQMAFVKH
GAKPHWGKNR KVGFFGVKQK IGPNFDKFLE VKNKLDPKKM FSSEWSDEIL LGTEASKYDG
CALEGNCVCS EERHCNPSKG YFCKEGLVYT QARVCRFSPA QVIVM
