BBE26_ARATH
ID BBE26_ARATH Reviewed; 537 AA.
AC Q9FKU8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Berberine bridge enzyme-like 26 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 26 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN OrderedLocusNames=At5g44400 {ECO:0000312|Araport:AT5G44400};
GN ORFNames=K9L2.20 {ECO:0000312|EMBL:BAB10125.1};
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 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 [3]
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 [4]
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 [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 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}.
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DR EMBL; AB011475; BAB10125.1; -; Genomic_DNA.
DR EMBL; AB017065; BAB10125.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED95105.1; -; Genomic_DNA.
DR EMBL; AY072198; AAL60019.1; -; mRNA.
DR RefSeq; NP_199253.1; NM_123807.4.
DR AlphaFoldDB; Q9FKU8; -.
DR SMR; Q9FKU8; -.
DR STRING; 3702.AT5G44400.1; -.
DR iPTMnet; Q9FKU8; -.
DR PaxDb; Q9FKU8; -.
DR PRIDE; Q9FKU8; -.
DR ProteomicsDB; 240714; -.
DR EnsemblPlants; AT5G44400.1; AT5G44400.1; AT5G44400.
DR GeneID; 834466; -.
DR Gramene; AT5G44400.1; AT5G44400.1; AT5G44400.
DR KEGG; ath:AT5G44400; -.
DR Araport; AT5G44400; -.
DR TAIR; locus:2158740; AT5G44400.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FKU8; -.
DR OMA; HESHVRI; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FKU8; -.
DR BioCyc; ARA:AT5G44400-MON; -.
DR PRO; PR:Q9FKU8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKU8; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..537
FT /note="Berberine bridge enzyme-like 26"
FT /id="PRO_5008179961"
FT DOMAIN 80..256
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 38..102
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CROSSLNK 117..181
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 537 AA; 60345 MW; 8951CDE0D30EFCF3 CRC64;
MGISKPLPLF SILVLYFSLY TITPTSSLAS LQDQFINCVQ RNTHVYFPLE KTFFAPTKNV
SMFSQVLEST AQNLRFLKKS MPKPGFIFSP IHESHVQASI ICSKKLRMHL RVRSGGHDYE
GLSYVSQIDK PFILMDLSKM RQVNINIQDN SAWVQSGATV GELYYRIAEK SKVHGFPAGL
CSSLGIGGHI TGGAYGSMMR KYGLGADNVL DAKIVDANGK LLDRAAMGED TFWAIRGGAG
GSFGIILAWK IKLVPVPKTV TVFTVTKTLQ QDVGNKIISK WQRVADKLVE ELFIRVLFNV
AGTGGNKTVT TSYNALFLGG KGTLMNVMKK SFPELGLTFK DCIEMSWLES IAYISGFPTH
TPTNVLLQGK SPFPKVSFKA KSDFVKTPIP ESGLQGIFKK LLKEDIPLMI WNPYGGMMAK
IPESQIPFPH RKGVLFKVQY VTSWLDSDKR PSRHINWIRD LYSYMTPYVS SNPREAYVNY
RDLDLGRNTK DVKTCIKQAQ VWGANYFKNN FNRLMMIKAK VDPENFFRHE QSIPPMM
