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Berberine bridge enzyme-like 1 (AtBBE-like 1) (EC 1.1.1.-) (Protein SIMILAR TO ELECTRON CAREER 1A) (AtSEC1A)

 BBE1_ARATH              Reviewed;         541 AA.
Q9LPC3; Q56ZK2;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
10-OCT-2018, entry version 117.
RecName: Full=Berberine bridge enzyme-like 1 {ECO:0000303|PubMed:26037923};
Short=AtBBE-like 1 {ECO:0000303|PubMed:26037923};
EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
AltName: Full=Protein SIMILAR TO ELECTRON CAREER 1A {ECO:0000305};
Short=AtSEC1A {ECO:0000305};
Flags: Precursor;
Name=SEC1A {ECO:0000305};
OrderedLocusNames=At1g01980 {ECO:0000312|Araport:AT1G01980};
ORFNames=F22M8.11 {ECO:0000312|EMBL:AAF76476.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-541.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18796151; DOI=10.1186/1471-2229-8-94;
Irshad M., Canut H., Borderies G., Pont-Lezica R., Jamet E.;
"A new picture of cell wall protein dynamics in elongating cells of
Arabidopsis thaliana: confirmed actors and newcomers.";
BMC Plant Biol. 8:94-94(2008).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=26037923; DOI=10.1074/jbc.M115.659631;
Daniel B., Pavkov-Keller T., Steiner B., Dordic A., Gutmann A.,
Nidetzky B., Sensen C.W., van der Graaff E., Wallner S., Gruber K.,
Macheroux P.;
"Oxidation of monolignols by members of the berberine bridge enzyme
family suggests a role in plant cell wall metabolism.";
J. Biol. Chem. 290:18770-18781(2015).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:O64743};
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:18796151}.
-!- TISSUE SPECIFICITY: Accumulates in cell walls of etiolated
hypocotyls. {ECO:0000269|PubMed:18796151}.
-!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
oxidoreductase family. {ECO:0000305}.
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EMBL; AC020622; AAF76476.1; -; Genomic_DNA.
EMBL; CP002684; AEE27362.1; -; Genomic_DNA.
EMBL; AK220962; BAD94511.1; -; mRNA.
PIR; G86151; G86151.
RefSeq; NP_171700.1; NM_100078.3.
UniGene; At.51264; -.
ProteinModelPortal; Q9LPC3; -.
SMR; Q9LPC3; -.
STRING; 3702.AT1G01980.1; -.
PaxDb; Q9LPC3; -.
PRIDE; Q9LPC3; -.
EnsemblPlants; AT1G01980.1; AT1G01980.1; AT1G01980.
GeneID; 839296; -.
Gramene; AT1G01980.1; AT1G01980.1; AT1G01980.
KEGG; ath:AT1G01980; -.
Araport; AT1G01980; -.
TAIR; locus:2025452; AT1G01980.
eggNOG; ENOG410IKGW; Eukaryota.
eggNOG; COG0277; LUCA.
HOGENOM; HOG000238933; -.
InParanoid; Q9LPC3; -.
OMA; YDGVSYI; -.
OrthoDB; EOG093607EN; -.
PhylomeDB; Q9LPC3; -.
BioCyc; ARA:AT1G01980-MONOMER; -.
PRO; PR:Q9LPC3; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9LPC3; baseline and differential.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IDA:TAIR.
Gene3D; 3.30.43.10; -; 1.
InterPro; IPR012951; BBE.
InterPro; IPR016166; FAD-bd_PCMH.
InterPro; IPR036318; FAD-bd_PCMH-like_sf.
InterPro; IPR016167; FAD-bd_PCMH_sub1.
InterPro; IPR006094; Oxid_FAD_bind_N.
Pfam; PF08031; BBE; 1.
Pfam; PF01565; FAD_binding_4; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS51387; FAD_PCMH; 1.
2: Evidence at transcript level;
Cell wall; Complete proteome; Disulfide bond; FAD; Flavoprotein;
Glycoprotein; Nucleotide-binding; Oxidoreductase; Reference proteome;
Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 541 Berberine bridge enzyme-like 1.
/FTId=PRO_5008180149.
DOMAIN 76 255 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 108 114 FAD. {ECO:0000250|UniProtKB:O64743}.
NP_BIND 179 180 FAD. {ECO:0000250|UniProtKB:O64743}.
NP_BIND 184 188 FAD. {ECO:0000250|UniProtKB:O64743}.
COMPBIAS 145 243 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
BINDING 113 113 FAD (covalent; via 2 links, pros
nitrogen).
{ECO:0000250|UniProtKB:P30986}.
BINDING 119 119 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 180 180 FAD (covalent; via 2 links).
{ECO:0000250|UniProtKB:P30986}.
BINDING 194 194 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 245 245 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:O64743}.
BINDING 476 476 FAD. {ECO:0000250|UniProtKB:O64743}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 35 98 {ECO:0000250|UniProtKB:O64743}.
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


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