FOX4_ARATH
ID FOX4_ARATH Reviewed; 552 AA.
AC Q9FZC7; Q8RWA4;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Berberine bridge enzyme-like 6 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 6 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE AltName: Full=Flavin-dependent oxidoreductase FOX4 {ECO:0000303|PubMed:26352477};
DE EC=1.-.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=FOX4 {ECO:0000303|PubMed:26352477};
GN OrderedLocusNames=At1g26410 {ECO:0000312|Araport:AT1G26410};
GN ORFNames=T1K7.21 {ECO:0000312|EMBL:AAF98575.1};
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 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 [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).
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; AAF98575.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30687.1; -; Genomic_DNA.
DR EMBL; AY093233; AAM13232.1; -; mRNA.
DR PIR; H86390; H86390.
DR RefSeq; NP_173965.1; NM_102405.3.
DR AlphaFoldDB; Q9FZC7; -.
DR SMR; Q9FZC7; -.
DR STRING; 3702.AT1G26410.1; -.
DR PaxDb; Q9FZC7; -.
DR PRIDE; Q9FZC7; -.
DR ProteomicsDB; 230038; -.
DR EnsemblPlants; AT1G26410.1; AT1G26410.1; AT1G26410.
DR GeneID; 839183; -.
DR Gramene; AT1G26410.1; AT1G26410.1; AT1G26410.
DR KEGG; ath:AT1G26410; -.
DR Araport; AT1G26410; -.
DR TAIR; locus:2197900; AT1G26410.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FZC7; -.
DR OMA; MWFDANA; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FZC7; -.
DR BioCyc; ARA:AT1G26410-MON; -.
DR PRO; PR:Q9FZC7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZC7; 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 GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..552
FT /note="Berberine bridge enzyme-like 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434891"
FT DOMAIN 93..270
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 56..119
FT /evidence="ECO:0000250|UniProtKB:P30986"
FT CROSSLNK 134..196
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CONFLICT 381
FT /note="L -> F (in Ref. 3; AAM13232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 61485 MW; AC432E47E3DB6044 CRC64;
MKEAFVFLLC LTNKFPKKFN SCSKKKETLY VLGLVLLVSF IEAPVTKPNF GKFIECLRDR
TTPENPITDV ISIADNSTTF LSSYVSYTKN KRFSSPNFKK LLAIIAAKHV SHVQATVVCA
KSNGIQLRIR SGGHDNEGFS YMSSVPFVIL DMHNLRSIDV NLSRKNAWVQ AGATLGELYV
KINEASQTLA FPAGVCPTVG AGGHISGGGF GNLMRKFGIT VDHVIDAQII DVNGKLLNRA
AMGEDLFWAI RGGGSSFGVI LSWKINLVEV PKILTVFKVN KTLEQGGTDI LYKWQLVANK
LPDSLFITAW PRTVNGPKPG ERTVAVVFYA QFLGPTDKLM EIMDQSFPEL GLGREDCHEM
SWLNTTLFWA NYPAGTPKSI LLDRPPTNSV SFKSKSDFVK KPIPKKGLEK LWKTMFKFNS
SVSLQFNPYG GVMDRIPATA TAFPHRKGNL FKVQYSTMWF DANATESSLA MMNELFEVAE
PYVSSNPREA FFNFRDIDIG SNPSGETNVD EAKIYGSKYF LGNLKRLMDV KAKYDPDNFF
KNEQSIPPVR VK
