BBE15_ARATH
ID BBE15_ARATH Reviewed; 532 AA.
AC O64743;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Berberine bridge enzyme-like 15 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 15 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.194 {ECO:0000269|PubMed:26037923};
DE EC=1.1.1.195 {ECO:0000269|PubMed:26037923};
DE AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 28 {ECO:0000303|PubMed:15634699};
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 23 {ECO:0000303|PubMed:15634699};
DE Flags: Precursor;
GN Name=MEE23 {ECO:0000303|PubMed:15634699};
GN Synonyms=EDA28 {ECO:0000303|PubMed:15634699};
GN OrderedLocusNames=At2g34790 {ECO:0000312|Araport:AT2G34790};
GN ORFNames=F19I3.2 {ECO:0000312|EMBL:AAC12819.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=19325888; DOI=10.1371/journal.pgen.1000440;
RA Cheng H., Song S., Xiao L., Soo H.M., Cheng Z., Xie D., Peng J.;
RT "Gibberellin acts through jasmonate to control the expression of MYB21,
RT MYB24, and MYB57 to promote stamen filament growth in Arabidopsis.";
RL PLoS Genet. 5:E1000440-E1000440(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH FAD, GLYCOSYLATION
RP AT ASN-57 AND ASN-431, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BONDS,
RP SUBCELLULAR LOCATION, COFACTOR, 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 -!- FUNCTION: Required for endosperm development and polar nuclei fusion
CC (PubMed:15634699). Mediates oxidation of cinnamyl alcohol and of p-
CC hydroxylated derivatives of cinnamyl alcohol (i.e. the monolignols p-
CC coumaryl-, coniferyl-, and sinapyl alcohol) to their corresponding
CC aldehydes. Can use cinnamyl alcohol and derivatives, as well as beta-O-
CC glycosylated form of coniferyl alcohol (coniferin) as substrate
CC (PubMed:26037923). {ECO:0000269|PubMed:15634699,
CC ECO:0000269|PubMed:26037923}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000269|PubMed:26037923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.194; Evidence={ECO:0000269|PubMed:26037923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000269|PubMed:26037923};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:26037923};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|PubMed:26037923};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000303|PubMed:26037923}.
CC -!- TISSUE SPECIFICITY: Expressed in sepals and stamen.
CC {ECO:0000269|PubMed:19325888}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000269|PubMed:26037923}.
CC -!- DISRUPTION PHENOTYPE: Endosperm development arrest and impaired polar
CC nuclei fusion. {ECO:0000269|PubMed:15634699}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC004238; AAC12819.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09022.1; -; Genomic_DNA.
DR EMBL; BT004022; AAO42058.1; -; mRNA.
DR EMBL; BT005187; AAO50720.1; -; mRNA.
DR PIR; T00461; T00461.
DR RefSeq; NP_181025.1; NM_129032.5.
DR PDB; 4UD8; X-ray; 2.09 A; A/B=1-532.
DR PDBsum; 4UD8; -.
DR AlphaFoldDB; O64743; -.
DR SMR; O64743; -.
DR STRING; 3702.AT2G34790.1; -.
DR iPTMnet; O64743; -.
DR PaxDb; O64743; -.
DR PRIDE; O64743; -.
DR ProteomicsDB; 240637; -.
DR EnsemblPlants; AT2G34790.1; AT2G34790.1; AT2G34790.
DR GeneID; 818044; -.
DR Gramene; AT2G34790.1; AT2G34790.1; AT2G34790.
DR KEGG; ath:AT2G34790; -.
DR Araport; AT2G34790; -.
DR TAIR; locus:2044692; AT2G34790.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; O64743; -.
DR OMA; LYEYMGT; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; O64743; -.
DR BioCyc; ARA:AT2G34790-MON; -.
DR BRENDA; 1.21.3.3; 399.
DR PRO; PR:O64743; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64743; 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:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:TAIR.
DR GO; GO:0050268; F:coniferyl-alcohol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0010197; P:polar nucleus fusion; IMP:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..532
FT /note="Berberine bridge enzyme-like 15"
FT /id="PRO_5008172792"
FT DOMAIN 76..254
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:26037923, ECO:0007744|PDB:4UD8"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:26037923, ECO:0007744|PDB:4UD8"
FT DISULFID 36..100
FT /evidence="ECO:0000269|PubMed:26037923,
FT ECO:0007744|PDB:4UD8"
FT CROSSLNK 115..179
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000269|PubMed:26037923"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4UD8"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:4UD8"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 289..299
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 307..319
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 375..386
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 435..445
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 450..464
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:4UD8"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:4UD8"
FT HELIX 505..515
FT /evidence="ECO:0007829|PDB:4UD8"
SQ SEQUENCE 532 AA; 59647 MW; 19F8149153818947 CRC64;
MAFAISKRNA TLFLVTLLLI SVPLSSSTLQ QDFVKCLVDN SDVSFPITAS FFSPDQNATL
FKEELESTAQ NLRYLTPSNP KPVFIFEPLY ETHVQAAVVC AKKLQLHLRL RSGGHDYEGL
SFVAEDETPF VIVDLSKLRQ VDVDLDSNSA WAHAGATIGE VYYRIQEKSQ THGFPAGLCS
SLGIGGHLVG GAYGSMMRKF GLGADNVLDA RIVDANGQIL DRAAMGEDVF WAIRGGGGGS
FGVILAWKIK LVPVPATVTV FTVTKTLEQD GTKVLYKWEQ IADKLDDDLF IRVIISPASK
TTKPGNRTIS MSYQAQFLGD SNRLLQVMQK SFPELGLTKK DCTEMSWIKS VMYIAGFPNS
AAPEALLAGK SLFKNHFKAK SDFVKEPIPV EGLEGLWERF LEEDSPLTIW NPYGGMMSRI
SESEIPFPHR NGTLFKIQWL STWQDGKVSE ERHMKWIREM YSYMEQYVSK NPRQAYVNYR
DLDLGTNEGE TDAREWGAKY YKGNFERLVK IKGEFDPDNF FRHEQSVPTK IG
