GLOX1_ARATH
ID GLOX1_ARATH Reviewed; 615 AA.
AC Q9FYG4;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Aldehyde oxidase GLOX1 {ECO:0000305};
DE EC=1.2.3.1 {ECO:0000305};
DE AltName: Full=Glyoxal oxidase 1 {ECO:0000305|PubMed:21673079};
DE Flags: Precursor;
GN Name=GLOX1 {ECO:0000303|PubMed:21673079};
GN OrderedLocusNames=At1g67290 {ECO:0000312|Araport:AT1G67290};
GN ORFNames=F1N21.11 {ECO:0000312|EMBL:AAG00252.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21673079; DOI=10.1105/tpc.110.082651;
RA Phan H.A., Iacuone S., Li S.F., Parish R.W.;
RT "The MYB80 transcription factor is required for pollen development and the
RT regulation of tapetal programmed cell death in Arabidopsis thaliana.";
RL Plant Cell 23:2209-2224(2011).
CC -!- FUNCTION: Catalyzes the oxidation of aldehydes to the corresponding
CC carboxylate by coupling the reaction to the reduction of dioxygen to
CC hydrogen peroxide. Substrates include glyoxal and other aldehydes (By
CC similarity). May be regulated by the transcription factor MYB80 during
CC anther development and play a role in tapetum and pollen development
CC (PubMed:21673079). {ECO:0000250|UniProtKB:Q01772,
CC ECO:0000269|PubMed:21673079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01772}.
CC -!- DEVELOPMENTAL STAGE: During anther development, expressed from stage 10
CC to the latest stage 14 in tapetal cells, developing microspores and
CC mature pollen grains and released pollen grains.
CC {ECO:0000269|PubMed:21673079}.
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DR EMBL; AC002130; AAG00252.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34623.1; -; Genomic_DNA.
DR EMBL; BT002818; AAO22637.1; -; mRNA.
DR EMBL; BT004443; AAO42437.1; -; mRNA.
DR RefSeq; NP_176897.1; NM_105397.3.
DR AlphaFoldDB; Q9FYG4; -.
DR SMR; Q9FYG4; -.
DR STRING; 3702.AT1G67290.1; -.
DR iPTMnet; Q9FYG4; -.
DR PaxDb; Q9FYG4; -.
DR PRIDE; Q9FYG4; -.
DR ProteomicsDB; 248586; -.
DR EnsemblPlants; AT1G67290.1; AT1G67290.1; AT1G67290.
DR GeneID; 843049; -.
DR Gramene; AT1G67290.1; AT1G67290.1; AT1G67290.
DR KEGG; ath:AT1G67290; -.
DR Araport; AT1G67290; -.
DR TAIR; locus:2019564; AT1G67290.
DR eggNOG; ENOG502QPS4; Eukaryota.
DR HOGENOM; CLU_009630_0_0_1; -.
DR InParanoid; Q9FYG4; -.
DR OMA; NKPNPGQ; -.
DR OrthoDB; 382481at2759; -.
DR PhylomeDB; Q9FYG4; -.
DR PRO; PR:Q9FYG4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FYG4; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC.
DR CDD; cd02851; E_set_GO_C; 1.
DR Gene3D; 2.130.10.80; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR009880; Glyoxal_oxidase_N.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF09118; DUF1929; 1.
DR Pfam; PF07250; Glyoxal_oxid_N; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..615
FT /note="Aldehyde oxidase GLOX1"
FT /id="PRO_5006751792"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 615 AA; 67775 MW; 6AA93F8866699FAD CRC64;
MKKSTRLLWL LSIIVLVAAV SKAVAEVDND DDDDNTSLEG MTTAKRETLE VEDHTSLEGM
VKREALEVKP PKAGKGKGKG KGRGTVAAGP EMNWPGQWEL FMKNSGVSAM HAILMPLINK
VQFYDATIWR ISQIKLPPGV PCHVFDAKKN KVDCWAHSVL VDINTGDIKP LALTTDTWCS
SGGLTVNGTL VSTGGFQGGA NTARYLSTCE NCVWIEYPKA LAARRWYSTQ ATLPDGTFIV
VGGRDALNYE YILPEGQNNK KLYDSQLLRQ TDDPEENNLY PFVWLNTDGN LFIFANNRSI
LLSPKTNKVL KEFPQLPGGA RNYPGSASSA LLPIRLYVQN PAIIPADVLV CGGAKQDAYF
RAERLKIYDW ALKDCARLNI NSAKPVWKTE TMPTSRVMSD TVILPNGEIL IINGAKRGSS
GWHLAKEPNF APLLYKPNKP LGQRFKELAP STIPRVYHSI AIALPDGKVL VGGSNTNNGY
QFNVEYPTEL RIEKFSPPYL DPALANMRPR IVNTATPKQI KYGQMFDVKI ELKQQNVAKE
NVMVTMLAPS FTTHSVSMNM RLLMLGINNV KNVGGDNHQI QAVAPPSGKL APPGYYLLFA
VYNGVPSVGE WIQIV
