BBE25_ARATH
ID BBE25_ARATH Reviewed; 542 AA.
AC Q9FKU9; Q93Y11;
DT 02-NOV-2016, 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 25 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 25 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN OrderedLocusNames=At5g44390 {ECO:0000312|Araport:AT5G44390};
GN ORFNames=K9L2.19 {ECO:0000312|EMBL:BAB10124.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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).
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 oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB011475; BAB10124.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95104.1; -; Genomic_DNA.
DR EMBL; AY059832; AAL24314.1; -; mRNA.
DR EMBL; BT000369; AAN15688.1; -; mRNA.
DR RefSeq; NP_199252.1; NM_123806.3.
DR AlphaFoldDB; Q9FKU9; -.
DR SMR; Q9FKU9; -.
DR STRING; 3702.AT5G44390.1; -.
DR PaxDb; Q9FKU9; -.
DR PRIDE; Q9FKU9; -.
DR ProteomicsDB; 241203; -.
DR EnsemblPlants; AT5G44390.1; AT5G44390.1; AT5G44390.
DR GeneID; 834465; -.
DR Gramene; AT5G44390.1; AT5G44390.1; AT5G44390.
DR KEGG; ath:AT5G44390; -.
DR Araport; AT5G44390; -.
DR TAIR; locus:2158730; AT5G44390.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FKU9; -.
DR OMA; MAYIGQF; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FKU9; -.
DR BioCyc; ARA:AT5G44390-MON; -.
DR PRO; PR:Q9FKU9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKU9; 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 2: Evidence at transcript level;
KW Cell wall; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..542
FT /note="Berberine bridge enzyme-like 25"
FT /id="PRO_0000438218"
FT DOMAIN 82..258
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 119
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9FI21"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 40..104
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CONFLICT 327
FT /note="M -> I (in Ref. 3; AAL24314/AAN15688)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="I -> V (in Ref. 3; AAL24314/AAN15688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 61483 MW; 26CE60FDB664B293 CRC64;
MGNSKPLPTI SCISVFALYF SFYTITLTSS TSLQDDFIKC LYRNTNVRFT LDKTFFTPER
NASIFTEVLE STAQNQRYLT KTMPKPGFIF KPVHESHVQA SVICSKKLEI HFRVRSGGHD
YEGVSYVSQI EKPFVLIDLS KLRQINVDIK DTSAWVEAGA TVGELYYRIA EKSKFHGFPA
GVYPSLGIGG HITGGAYGSL MRKYGLAADN VLDAKIVDAN GKLLDRASMG EDLFWAIRGG
SGGSFGIILS WKIKLVPVPE TLTVFTVTKT FEQDRSFKIL SKWQEIADNL VDELFLRVFF
TVSGNKANKT VTMAYIGQFL GEKGTLMEVM KKDFPELGLT QKDCIEMSWI DSIIYNSGFP
TNPPPPIEIL LQAKSPIGKV YFKGKSDFAK KPIPVLGLEG MFKKLLEEDA ALVIWTPYGG
KMDKIPESEI PFPHRNGTNF MIQYYRSWSD SEKRPNRRTK WIRELYGYMT PYVSSNPRQA
YVNYRDLDLG QNKDNSKSNF IEAKIWGANY FKDNFNRLVR IKSKVDPDNF FRHEQSIPTL
PV
