FOX5_ARATH
ID FOX5_ARATH Reviewed; 529 AA.
AC Q9FZC8;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Berberine bridge enzyme-like 7 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 7 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE AltName: Full=Flavin-dependent oxidoreductase FOX5 {ECO:0000303|PubMed:26352477};
DE EC=1.-.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=FOX5 {ECO:0000303|PubMed:26352477};
GN OrderedLocusNames=At1g26420 {ECO:0000312|Araport:AT1G26420};
GN ORFNames=T1K7.20 {ECO:0000312|EMBL:AAF98574.1};
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 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).
RN [4]
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).
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; AAF98574.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30688.1; -; Genomic_DNA.
DR PIR; A86391; A86391.
DR RefSeq; NP_173966.1; NM_102406.3.
DR AlphaFoldDB; Q9FZC8; -.
DR SMR; Q9FZC8; -.
DR STRING; 3702.AT1G26420.1; -.
DR PaxDb; Q9FZC8; -.
DR PRIDE; Q9FZC8; -.
DR ProteomicsDB; 228883; -.
DR EnsemblPlants; AT1G26420.1; AT1G26420.1; AT1G26420.
DR GeneID; 839184; -.
DR Gramene; AT1G26420.1; AT1G26420.1; AT1G26420.
DR KEGG; ath:AT1G26420; -.
DR Araport; AT1G26420; -.
DR TAIR; locus:2198000; AT1G26420.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FZC8; -.
DR OMA; QYSTTWL; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FZC8; -.
DR BioCyc; ARA:AT1G26420-MON; -.
DR PRO; PR:Q9FZC8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZC8; 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..529
FT /note="Berberine bridge enzyme-like 7"
FT /id="PRO_5004326165"
FT DOMAIN 69..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 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 439
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 529 AA; 59217 MW; 0DC786AA3CB0590D CRC64;
MKEALSILCL ALLVSVSEAE VTKPNSENFI ECLRYRTSSE NPITDSISIA DNTTTFLSSY
LSYTKNKRYS SPNFKKLLAI VAAKHVSHVQ ATVVCAKTNG IQLRIRSGGH DLEGLSYRSS
VPFVILDMFN LRSITVNVLS KKAWVQAGAT LGELYVKINE ASQTLAFPAG VCPTVGVGGH
ISGGGYGNLM RKFGITVDHV SDAQLIDVNG KLLNRASMGE DLFWAIRGGG GASFGVILSW
KINLVKVPKI LTVFKVNKTL EQGGTDVLYK WQLVATKFPE DLFMRAWPQI INGAERGDRT
IAVVFYAQFL GPADKLLAIM NQRLPELGLR REDCHEMSWF NTTLFWADYP AGTPKSVLLD
RPTNPGFFKS KSDYVKKPIP KEGLEKLWKT MFKFNNIVWM QFNPYGGVMD QIPSTATAFP
HRKGNMFKVQ YSTTWLAANA TEISLSMMKE LYKVAEPYVS SNPREAFFNY RDIDIGSNPS
DETNVDEAKI YGYKYFLGNL KRLMQVKAKY DPENFFKNEQ SIPPVRVIE
