BBE11_ARATH
ID BBE11_ARATH Reviewed; 526 AA.
AC Q9SA88; Q6NNH8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Berberine bridge enzyme-like 11 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 11 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN OrderedLocusNames=At1g30730 {ECO:0000312|Araport:AT1G30730};
GN ORFNames=T5I8.18 {ECO:0000312|EMBL:AAD25760.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 355-526.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR24205.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007060; AAD25760.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31265.1; -; Genomic_DNA.
DR EMBL; BT010838; AAR24205.1; ALT_INIT; mRNA.
DR EMBL; BT011310; AAR92346.1; -; mRNA.
DR PIR; H86432; H86432.
DR RefSeq; NP_174360.1; NM_102809.3.
DR AlphaFoldDB; Q9SA88; -.
DR SMR; Q9SA88; -.
DR IntAct; Q9SA88; 1.
DR STRING; 3702.AT1G30730.1; -.
DR iPTMnet; Q9SA88; -.
DR PaxDb; Q9SA88; -.
DR PRIDE; Q9SA88; -.
DR ProteomicsDB; 240773; -.
DR EnsemblPlants; AT1G30730.1; AT1G30730.1; AT1G30730.
DR GeneID; 839953; -.
DR Gramene; AT1G30730.1; AT1G30730.1; AT1G30730.
DR KEGG; ath:AT1G30730; -.
DR Araport; AT1G30730; -.
DR TAIR; locus:2204634; AT1G30730.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9SA88; -.
DR OMA; PTTWSHI; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9SA88; -.
DR BioCyc; ARA:AT1G30730-MON; -.
DR PRO; PR:Q9SA88; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA88; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..526
FT /note="Berberine bridge enzyme-like 11"
FT /id="PRO_5008180376"
FT DOMAIN 72..247
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..94
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CROSSLNK 109..171
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 526 AA; 58913 MW; 9F6AFD5B13F6FA36 CRC64;
MEKLLIICML LISVLVATSQ SQTDPETFLR CLVREGSNPQ VFISDVTYIP SNSSFTTVLR
RRIPNLRFDK PTTPKPIAII TPTTWSHISP VLACARLFPV QVRIRSGGHD FEGLSYTSTA
PFFLIDLLNF KSVDVNLTEG TAWVDTGATL GELYYKIAEK SNVLGFPAGL CTTLGVGGHI
SGGGYGTMMR KYGLSVDNVV GSRIIDSNGN TYFDRMSMGE ELFWAVRGGG AASFGIVMGY
KIRLVPVPEK VTVFSVGKTV GEGAVDLIMK WQNFSHSTDR NLFVKLTLTL VNGAKPGEKK
VLATFIGMNL GGFDKTLNVM NRDFPELKLK KTDCTEMRWI DSVLFWAGYP VGTPTSVLLN
PTVTKKLFMK RKSDYVKRPV SRTGLGLILK KLVELEKVEM NWNPYGGRMG EIPSSRTPFP
HRGGNLFNIE YIIDWSEAGD NVEKKYLALA NEFYRFMTPY VSSNPREAFL NYRDIDIGSS
GNSTYEEGKI YGAKYFKDNF ERLVDIKTKF DEINFWRNEQ SIPVRK
