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 15-FEB-2017, entry version 105. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA 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., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Seki M., 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 RT family 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 -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000250|UniProtKB:O64743}. CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked CC oxidoreductase 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 UniGene; At.3570; -. DR UniGene; At.48889; -. DR ProteinModelPortal; Q9SVG3; -. DR SMR; Q9SVG3; -. DR STRING; 3702.AT4G20840.1; -. 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; HOG000238933; -. DR OMA; ERANLYM; -. DR OrthoDB; EOG09360CSE; -. DR PhylomeDB; Q9SVG3; -. DR BioCyc; ARA:AT4G20840-MONOMER; -. DR Proteomes; UP000006548; Chromosome 4. DR GO; GO:0048046; C:apoplast; IDA:TAIR. DR GO; GO:0005618; C:cell wall; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR012951; BBE. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_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; Complete proteome; Disulfide bond; FAD; Flavoprotein; KW Glycoprotein; Nucleotide-binding; Oxidoreductase; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 539 Berberine bridge enzyme-like 21. FT /FTId=PRO_5008180483. FT DOMAIN 82 256 FAD-binding PCMH-type. FT {ECO:0000255|PROSITE-ProRule:PRU00718}. FT NP_BIND 114 120 FAD. {ECO:0000250|UniProtKB:O64743}. FT NP_BIND 180 181 FAD. {ECO:0000250|UniProtKB:O64743}. FT NP_BIND 185 189 FAD. {ECO:0000250|UniProtKB:O64743}. FT BINDING 119 119 FAD (covalent; via 2 links, pros FT nitrogen). FT {ECO:0000250|UniProtKB:P30986}. FT BINDING 125 125 FAD. {ECO:0000250|UniProtKB:O64743}. FT BINDING 181 181 FAD (covalent; via 2 links). FT {ECO:0000250|UniProtKB:P30986}. FT BINDING 195 195 FAD. {ECO:0000250|UniProtKB:O64743}. FT BINDING 477 477 FAD. {ECO:0000250|UniProtKB:O64743}. FT CARBOHYD 79 79 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 340 340 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT DISULFID 41 104 {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 //