BBE1_ARATH
ID BBE1_ARATH Reviewed; 541 AA.
AC Q9LPC3; Q56ZK2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Berberine bridge enzyme-like 1 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 1 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE AltName: Full=Protein SIMILAR TO ELECTRON CAREER 1A {ECO:0000305};
DE Short=AtSEC1A {ECO:0000305};
DE Flags: Precursor;
GN Name=SEC1A {ECO:0000305};
GN OrderedLocusNames=At1g01980 {ECO:0000312|Araport:AT1G01980};
GN ORFNames=F22M8.11 {ECO:0000312|EMBL:AAF76476.1};
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 10-541.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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: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; AC020622; AAF76476.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27362.1; -; Genomic_DNA.
DR EMBL; AK220962; BAD94511.1; -; mRNA.
DR PIR; G86151; G86151.
DR RefSeq; NP_171700.1; NM_100078.3.
DR AlphaFoldDB; Q9LPC3; -.
DR SMR; Q9LPC3; -.
DR STRING; 3702.AT1G01980.1; -.
DR PaxDb; Q9LPC3; -.
DR PRIDE; Q9LPC3; -.
DR ProteomicsDB; 241126; -.
DR EnsemblPlants; AT1G01980.1; AT1G01980.1; AT1G01980.
DR GeneID; 839296; -.
DR Gramene; AT1G01980.1; AT1G01980.1; AT1G01980.
DR KEGG; ath:AT1G01980; -.
DR Araport; AT1G01980; -.
DR TAIR; locus:2025452; AT1G01980.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9LPC3; -.
DR OMA; MWMQSYA; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9LPC3; -.
DR BioCyc; ARA:AT1G01980-MON; -.
DR PRO; PR:Q9LPC3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPC3; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IDA: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 2: Evidence at transcript level;
KW Cell wall; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..541
FT /note="Berberine bridge enzyme-like 1"
FT /id="PRO_5008180149"
FT DOMAIN 76..255
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 73
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 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 35..98
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CROSSLNK 113..180
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 541 AA; 60103 MW; BA4F3100043A7037 CRC64;
MKLSCLVFLI VSSLVSSSLA TAPPNTSIYE SFLQCFSNQT GAPPEKLCDV VLPQSSASFT
PTLRAYIRNA RFNTSTSPKP LLVIAARSEC HVQATVLCTK SLNFQLKTRS GGHDYDGVSY
ISNRPFFVLD MSYLRNITVD MSDDGGSAWV GAGATLGEVY YNIWQSSKTH GTHGFPAGVC
PTVGAGGHIS GGGYGNMIRK YGLSVDYVTD AKIVDVNGRI LDRKSMGEDL FWAIGGGGGA
SFGVILSFKI KLVPVPPRVT VFRVEKTLVE NALDMVHKWQ FVAPKTSPDL FMRLMLQPVT
RNTTQTVRAS VVALFLGKQS DLMSLLTKEF PELGLKPENC TEMTWIQSVM WWANNDNATV
IKPEILLDRN PDSASFLKRK SDYVEKEISK DGLDFLCKKL MEAGKLGLVF NPYGGKMSEV
ATTATPFPHR KRLFKVQHSM NWKDPGTDVE SSFMEKTRSF YSYMAPFVTK NPRHTYLNYR
DLDIGINSHG PNSYREAEVY GRKYFGENFD RLVKVKTAVD PENFFRDEQS IPTLPTKPSS
S
