BBE23_ARATH
ID BBE23_ARATH Reviewed; 532 AA.
AC Q9FKV2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Berberine bridge enzyme-like 23 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 23 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN OrderedLocusNames=At5g44360 {ECO:0000312|Araport:AT5G44360};
GN ORFNames=K9L2.15 {ECO:0000312|EMBL:BAB10121.1};
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 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 [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:0000269|PubMed:18796151}.
CC -!- TISSUE SPECIFICITY: Accumulates in cell walls of etiolated hypocotyls.
CC {ECO:0000269|PubMed:18796151}.
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; BAB10121.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95101.1; -; Genomic_DNA.
DR RefSeq; NP_199249.1; NM_123803.2.
DR AlphaFoldDB; Q9FKV2; -.
DR SMR; Q9FKV2; -.
DR STRING; 3702.AT5G44360.1; -.
DR PaxDb; Q9FKV2; -.
DR PRIDE; Q9FKV2; -.
DR ProteomicsDB; 241201; -.
DR EnsemblPlants; AT5G44360.1; AT5G44360.1; AT5G44360.
DR GeneID; 834462; -.
DR Gramene; AT5G44360.1; AT5G44360.1; AT5G44360.
DR KEGG; ath:AT5G44360; -.
DR Araport; AT5G44360; -.
DR TAIR; locus:2158700; AT5G44360.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FKV2; -.
DR PhylomeDB; Q9FKV2; -.
DR PRO; PR:Q9FKV2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKV2; 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..532
FT /note="Berberine bridge enzyme-like 23"
FT /id="PRO_5008179960"
FT DOMAIN 80..256
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..102
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CROSSLNK 117..180
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 532 AA; 60499 MW; 84F15CB5F3D61D55 CRC64;
MRTLEAFALS LFLVFLVKWV NSDSSSSPSK DQFLSCMSTH SDSSFINPKS FIHKPDSRVY
TDFSQSLISQ NYRFLTLNFT SQKPILIVTP RTDTEIQRSL LCSRKLGVKV RTKSGGHDYE
GLSYLSLHSP FIILDLVNVR SIEINLADET AWVGAGATIG ELYYKIAKSS KIHGFPAGTC
PSVGVGGHFS GGGFGAMMRK HGLAADNVVD ARFVDANGRI YNSRREMGED LFWAIRGGGA
ASFGVVLSWK VKLVRVPEKV TCFRRNLPLT QNMTKIVHRW QQIAAELDDN LFIRVIVSIS
GGSVQTTFQA NYLGGIDKLI PLMNQKFPEL GLTFQDCSEM TWIDSIMYFN WKKGQPLETL
LDRGQRYNDL YFKAKSDFVK NPIPEIGLEG IWTRFHEVES PIMIMEPLGG KMYEIGETET
PFPHRRGNLY NIQYMVKWRL KDIGVMEKHV TWMRLLYRYM RVYVSASPRG AYLNYRDLDL
GMNRGVNTSF EDAKLWGFRY FGSNFKRLAI VKGKIDPTNF FRNEQSVPPL IV
