FOX2_ARATH
ID FOX2_ARATH Reviewed; 530 AA.
AC Q9FZC5; Q949N1;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Berberine bridge enzyme-like 4 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 4 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE AltName: Full=Flavin-dependent oxidoreductase FOX2 {ECO:0000303|PubMed:26352477};
DE EC=1.-.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=FOX2 {ECO:0000303|PubMed:26352477};
GN OrderedLocusNames=At1g26390 {ECO:0000312|Araport:AT1G26390};
GN ORFNames=T1K7.23 {ECO:0000312|EMBL:AAF98577.1};
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 NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=26352477; DOI=10.1038/nature14907;
RA Rajniak J., Barco B., Clay N.K., Sattely E.S.;
RT "A new cyanogenic metabolite in Arabidopsis required for inducible pathogen
RT defence.";
RL Nature 525:376-379(2015).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=26037923; DOI=10.1074/jbc.m115.659631;
RA Daniel B., Pavkov-Keller T., Steiner B., Dordic A., Gutmann A.,
RA Nidetzky B., Sensen C.W., van der Graaff E., Wallner S., Gruber K.,
RA Macheroux P.;
RT "Oxidation of monolignols by members of the berberine bridge enzyme family
RT suggests a role in plant cell wall metabolism.";
RL J. Biol. Chem. 290:18770-18781(2015).
CC -!- FUNCTION: Probable flavin-dependent oxidoreductase. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O64743};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000250|UniProtKB:O64743};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:O64743}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:O64743}.
CC -!- DISRUPTION PHENOTYPE: No effect on the levels of ICN metabolites.
CC {ECO:0000269|PubMed:26352477}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC013427; AAF98577.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30685.1; -; Genomic_DNA.
DR EMBL; AY051000; AAK93677.1; -; mRNA.
DR EMBL; BT015919; AAU95455.1; -; mRNA.
DR PIR; F86390; F86390.
DR RefSeq; NP_564245.1; NM_102403.3.
DR AlphaFoldDB; Q9FZC5; -.
DR SMR; Q9FZC5; -.
DR STRING; 3702.AT1G26390.1; -.
DR PaxDb; Q9FZC5; -.
DR PRIDE; Q9FZC5; -.
DR ProteomicsDB; 230526; -.
DR EnsemblPlants; AT1G26390.1; AT1G26390.1; AT1G26390.
DR GeneID; 839181; -.
DR Gramene; AT1G26390.1; AT1G26390.1; AT1G26390.
DR KEGG; ath:AT1G26390; -.
DR Araport; AT1G26390; -.
DR TAIR; locus:2197935; AT1G26390.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FZC5; -.
DR OMA; TWFYAKS; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FZC5; -.
DR BioCyc; ARA:AT1G26390-MON; -.
DR PRO; PR:Q9FZC5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZC5; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
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; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..530
FT /note="Berberine bridge enzyme-like 4"
FT /id="PRO_5004325706"
FT DOMAIN 73..247
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 32..95
FT /evidence="ECO:0000250|UniProtKB:P30986"
FT CROSSLNK 110..172
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CONFLICT 40
FT /note="E -> K (in Ref. 3; AAK93677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 58948 MW; 116C6CA06BE4C322 CRC64;
MKGTLSVLCL VLLVSVLEAA VTKPKFGDFI GCLRYRTSPE NPITDAISFA DNTTTFLSSY
VSYTKNKRFS TPNYRKLLAI VAAKHVSHVQ ATVVCAKSNG IQLRIRSGGH DYEGLSYMSS
VPFVILDMYN LRSITVDVSS KKAWIQAGAT LGELYTNVND VSQTLAFPAG VCATVGAGGH
ISGGGYGNLM RKYGITVDHV IDAQIIDVNG KLLNRATMGE DLFWAIRGGG GGSFGVILSW
KINLVDVPKI VTVFKVNKTL EQGGTDVLYK WQLVASKFPE SLFVRAMPQV ANGTKRGERT
ITVVFYAQFL GRTDALMAIM NQNWPELGLK HEDCQEMSWL NSTLFWADYP AGTPTSILLD
RPSSPGDFFK SKSDYVKKPI PKEGLEKLWK TMLKFNNNIV WMQFNPYGGV MDRIPATATA
FPHRKGNLFK IQYFTTWFNA NATMSSLSQM KELYEVAEPY VSSNPREAFF NYRDIDVGSN
PSGETNVDEA KIYGSKYFLG NLKRLMDVKA KYDPDNFFKN EQSIPPVRVM
