ID BBE21_ARATH Reviewed; 539 AA. AC Q9SVG3; DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 26-FEB-2020, entry version 124. DE RecName: Full=Berberine bridge enzyme-like 21 {ECO:0000303|PubMed:26037923}; DE Short=AtBBE-like 21 {ECO:0000303|PubMed:26037923}; DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743}; DE Flags: Precursor; GN OrderedLocusNames=At4g20840 {ECO:0000312|Araport:AT4G20840}; GN ORFNames=F21C20.190 {ECO:0000312|EMBL:CAB45850.1}; 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=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). 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; TISSUE=Root; RX PubMed=19423640; DOI=10.1093/dnares/dsp009; RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., RA Shinozaki K.; RT "Analysis of multiple occurrences of alternative splicing events in RT Arabidopsis thaliana using novel sequenced full-length cDNAs."; RL DNA Res. 16:155-164(2009). 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 -!- 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 -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL080254; CAB45850.1; -; Genomic_DNA. DR EMBL; AL161553; CAB79084.1; -; Genomic_DNA. DR EMBL; CP002687; AEE84367.1; -; Genomic_DNA. DR EMBL; AK317639; BAH20300.1; -; mRNA. DR PIR; T10626; T10626. DR RefSeq; NP_193816.1; NM_118202.2. DR SMR; Q9SVG3; -. DR STRING; 3702.AT4G20840.1; -. DR PaxDb; Q9SVG3; -. DR PRIDE; Q9SVG3; -. DR EnsemblPlants; AT4G20840.1; AT4G20840.1; AT4G20840. DR GeneID; 827832; -. DR Gramene; AT4G20840.1; AT4G20840.1; AT4G20840. DR KEGG; ath:AT4G20840; -. DR Araport; AT4G20840; -. DR TAIR; locus:2121544; AT4G20840. DR eggNOG; ENOG410IKGW; Eukaryota. DR eggNOG; COG0277; LUCA. DR HOGENOM; CLU_018354_6_0_1; -. DR InParanoid; Q9SVG3; -. DR OMA; VNDHGTN; -. DR OrthoDB; 1049549at2759; -. DR PhylomeDB; Q9SVG3; -. DR BioCyc; ARA:AT4G20840-MONOMER; -. DR PRO; PR:Q9SVG3; -. DR Proteomes; UP000006548; Chromosome 4. DR Proteomes; UP000007605; Chromosome 4, ARATH_4. DR Proteomes; UP000007605; Chromosome 4, long arm. DR ExpressionAtlas; Q9SVG3; baseline and differential. DR GO; GO:0048046; C:apoplast; IDA:TAIR. DR GO; GO:0005618; C:cell wall; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IDA:TAIR. DR Gene3D; 3.30.43.10; -; 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; 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..26 FT /evidence="ECO:0000255" FT CHAIN 27..539 FT /note="Berberine bridge enzyme-like 21" FT /id="PRO_5008180483" FT DOMAIN 82..256 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 340 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 41..104 FT /evidence="ECO:0000250|UniProtKB:O64743" FT CROSSLNK 119..181 FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His- FT Cys)" FT /evidence="ECO:0000250|UniProtKB:O64743" SQ SEQUENCE 539 AA; 60144 MW; 6645E9376E216426 CRC64; MIATQTFVSV FFFVFFLVSL PFFSSAAPPS SDSIYESFVQ CFSDKTKSPQ AQITDNVFSR TNPSFSSVLR AYIRNGRFNT SSTPKPAIIV TPRSDIHVSA AVTCSKSLNF LLKIRSGGHD YEGLSYISDK PFFILDMSNL RDVSVDIADQ SAWISAGATL GEVYYRIWEK SKVHGFPAGV CPTVGVGGHI SGGGYGNMLR KFGLSVDNLI DAKIVDVNGQ ILDRKSMGED LFWAISGGGG ASFGVVLGYK VKLVPVPETV TVFRVEKYMD SGAVDMVHKW QSVGPKTDRN LFLRMLIQPV TRKKVKTVRA TVVALFLGRA EEVVALLGKE FPELSLKKEN CSEMTWFQSA LWWDNRVNPT QIDPKVFLDR NLDRANFGKR KSDYVASEIP RDGIESLFKK MTELGKIGLV FNPYGGKMAE VTVNATPFPH RSKLFKIQYS VTWQENSVEI EKGFLNQANV LYSFMTGFVS KNPRNAYLNY RDVDIGVNDH GTNSYEEGEV YGRKYFGDNF DRLVKVKTAA DPDNFFRNEQ SIPTVLSKA //