FOX3_ARATH
ID FOX3_ARATH Reviewed; 527 AA.
AC Q9FZC6;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Berberine bridge enzyme-like 5 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 5 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE AltName: Full=Flavin-dependent oxidoreductase FOX3 {ECO:0000303|PubMed:26352477};
DE EC=1.-.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=FOX3 {ECO:0000303|PubMed:26352477};
GN OrderedLocusNames=At1g26400 {ECO:0000312|Araport:AT1G26400};
GN ORFNames=T1K7.22 {ECO:0000312|EMBL:AAF98576.1};
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 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 [4]
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; AAF98576.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30686.1; -; Genomic_DNA.
DR PIR; G86390; G86390.
DR RefSeq; NP_173964.1; NM_102404.1.
DR AlphaFoldDB; Q9FZC6; -.
DR SMR; Q9FZC6; -.
DR STRING; 3702.AT1G26400.1; -.
DR PaxDb; Q9FZC6; -.
DR PRIDE; Q9FZC6; -.
DR ProteomicsDB; 230527; -.
DR EnsemblPlants; AT1G26400.1; AT1G26400.1; AT1G26400.
DR GeneID; 839182; -.
DR Gramene; AT1G26400.1; AT1G26400.1; AT1G26400.
DR KEGG; ath:AT1G26400; -.
DR Araport; AT1G26400; -.
DR TAIR; locus:2197920; AT1G26400.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FZC6; -.
DR OMA; TMMKELY; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FZC6; -.
DR BioCyc; ARA:AT1G26400-MON; -.
DR PRO; PR:Q9FZC6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZC6; 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 3: Inferred from homology;
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..527
FT /note="Berberine bridge enzyme-like 5"
FT /id="PRO_5004325687"
FT DOMAIN 73..247
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 52
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 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"
SQ SEQUENCE 527 AA; 58736 MW; 8DFBFCDE6D2CE6B1 CRC64;
MKALFSVLCL VLLVSILRAA VTKPDSGIFT GCLRNRTSLE NPITDAIFTS RNTTTFLSSY
VSYTKNKRYS SLNYQKLVAI VAAKHVSHVQ ATVVCAKANG IQLRIRSGGH DYEGLSYTSS
VPFVILDMYN LRSITVDVSS KKAWVQAGAT LGELYTKINE ASQTLAFPAG VCPTVGVGGH
ITGGGFGNLM RKFGITVDHV IDAQLIGVNG KLLDRATMGE DLFWAIRGGG GASFGVILSW
KINLVEVPKI LTVFKVSKTL EQGGTDVLYK WQLVATKVPE DLFIRAWPQI VKGTKLGERT
IGVVFFAQFL GPTDKLMEIM SQSLPELGLR REDCHEMSWF NTTLFWANYP VGTPTRVLLD
RPSTPGEFFK SKSDNIKKPI PKEGLEKIWK TMLKFNFVWI EFNPYGGVMD RIPATATAFP
HRKGNLFNLQ YSTIWLDAKE TENKLTMMKE LYEVAGPYVS SNPREALFNF RDFDIGINPS
GLNVDEAKIY GYKYFLGNLK RLMDVKAKCD PDNFFKNEQS ILPARVM
