BBE27_ARATH
ID BBE27_ARATH Reviewed; 535 AA.
AC Q9FI25; Q0WTH3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Berberine bridge enzyme-like 27 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 27 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN OrderedLocusNames=At5g44410 {ECO:0000312|Araport:AT5G44410};
GN ORFNames=MFC16.3 {ECO:0000312|EMBL:BAB09147.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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] OF 23-535.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18796151; DOI=10.1186/1471-2229-8-94;
RA Irshad M., Canut H., Borderies G., Pont-Lezica R., Jamet E.;
RT "A new picture of cell wall protein dynamics in elongating cells of
RT Arabidopsis thaliana: confirmed actors and newcomers.";
RL BMC Plant Biol. 8:94-94(2008).
RN [5]
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:18796151}.
CC -!- TISSUE SPECIFICITY: Accumulates in cell walls of etiolated hypocotyls.
CC {ECO:0000269|PubMed:18796151}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB017065; BAB09147.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95106.1; -; Genomic_DNA.
DR EMBL; AK227582; BAE99575.1; -; mRNA.
DR RefSeq; NP_199254.1; NM_123808.4.
DR AlphaFoldDB; Q9FI25; -.
DR SMR; Q9FI25; -.
DR STRING; 3702.AT5G44410.1; -.
DR iPTMnet; Q9FI25; -.
DR PaxDb; Q9FI25; -.
DR PRIDE; Q9FI25; -.
DR ProteomicsDB; 240639; -.
DR EnsemblPlants; AT5G44410.1; AT5G44410.1; AT5G44410.
DR GeneID; 834467; -.
DR Gramene; AT5G44410.1; AT5G44410.1; AT5G44410.
DR KEGG; ath:AT5G44410; -.
DR Araport; AT5G44410; -.
DR TAIR; locus:2163411; AT5G44410.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FI25; -.
DR OMA; ADKVPND; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FI25; -.
DR BioCyc; ARA:AT5G44410-MON; -.
DR PRO; PR:Q9FI25; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI25; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; IDA: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 InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..535
FT /note="Berberine bridge enzyme-like 27"
FT /id="PRO_5008179930"
FT DOMAIN 78..253
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 115
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9FI21"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 215
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 40..100
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 535 AA; 61274 MW; 2AC664B3A03EADE3 CRC64;
MEILRFLLSL FIYFLLLNLS LSHFPSISAQ RTNHENFLKC LSHRINEDDS RIIHTSKDPS
YFSILNSSIQ NPRFFVLETP KPVSIITPVQ ATDVQSTIKC ARLHGIHIRT RSGGHDYEGL
SYMAKSRPFV VIDLRNLRSI TLDVDNRTGW VQSGATIGEL YYEIGKLSKS LAFPAGLYPT
VGIGGQFGGG GYGTLMRKYG LSADNVIDAH IVDANGSFLD RQGMGEDFFW AIRGGGGSSF
SVVLSWKIRL LDVPSVVTVF KVVKTSEKEA VSIINKWQYI ADKVPNDLFI RAMLQKETEV
YASFPGLYLG PVSDLLALMK DKFPELGLEI GNCREMSWIE SVLWFIKGES MEILAKRKRT
SRSFKGKDDF IEEPIPKTAI QYLWRRFEAP EARLAKIILT PFGGKMSEIA DNEIPFPHRE
GNLYEIQYLA YWSEEEDKNK TNTEKYLRWV ESVYEFMTPY VSKSPRRAYV NFRDIDLGMY
LGLNMKTKYE EAKVWGVKYF KNNFDRLVRV KTNVDPMDFF CDEQSIPIMK YVNDI
