ID   GGLO7_ARATH             Reviewed;         252 AA.
AC   Q9FM84;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable truncated L-gulonolactone oxidase 7, mitochondrial {ECO:0000303|PubMed:20622436};
DE            Short=AtGulLO7 {ECO:0000303|PubMed:20622436};
DE            EC=1.1.3.8 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=GULLO7 {ECO:0000303|PubMed:20622436};
GN   OrderedLocusNames=At5g56470 {ECO:0000312|Araport:AT5G56470};
GN   ORFNames=MCD7.24 {ECO:0000312|EMBL:BAB11275.1};
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   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   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC       {ECO:0000305|PubMed:20622436}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC   -!- DOMAIN: Lacks an FAD-binding domain present in all the other members of
CC       the family. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB009049; BAB11275.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96770.1; -; Genomic_DNA.
DR   RefSeq; NP_200458.1; NM_125030.1.
DR   AlphaFoldDB; Q9FM84; -.
DR   STRING; 3702.AT5G56470.1; -.
DR   PaxDb; Q9FM84; -.
DR   PRIDE; Q9FM84; -.
DR   EnsemblPlants; AT5G56470.1; AT5G56470.1; AT5G56470.
DR   GeneID; 835748; -.
DR   Gramene; AT5G56470.1; AT5G56470.1; AT5G56470.
DR   KEGG; ath:AT5G56470; -.
DR   Araport; AT5G56470; -.
DR   TAIR; locus:2161103; AT5G56470.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_019762_1_0_1; -.
DR   InParanoid; Q9FM84; -.
DR   OMA; INIGMSK; -.
DR   OrthoDB; 1134169at2759; -.
DR   PhylomeDB; Q9FM84; -.
DR   UniPathway; UPA00132; -.
DR   PRO; PR:Q9FM84; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FM84; differential.
DR   Genevisible; Q9FM84; AT.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; 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   InterPro; IPR007173; ALO_C.
DR   InterPro; IPR010030; GULO_Plant.
DR   Pfam; PF04030; ALO; 1.
DR   TIGRFAMs; TIGR01677; pln_FAD_oxido; 1.
PE   3: Inferred from homology;
KW   Ascorbate biosynthesis; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..102
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           103..252
FT                   /note="Probable truncated L-gulonolactone oxidase 7,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432508"
SQ   SEQUENCE   252 AA;  28680 MW;  5D0BFCE1F2213132 CRC64;
     MKRSMRSHLA KQTRSVIFTG YPVIGSQDRI MSSGACLDSH QNGLITSCPW DPRIKGEFFY
     QTALSVPLTH VKDFINDIKA LVKIEPKSLC GLELNYGVLV RYVTSSPAYL RKEEKALDFD
     LTYYRSKDDP WTPRLYEDYM EEIEQMAILK YNALPHWGKN RNLAFDGAIK KYKNANTFLK
     VKERLDPWGL FSTEWTDQIL GLKGNVTIVK QGCAPEGLCI CSDDSHCAPN KGYMCRPGKV
     YKEARVCTLV TA