BBE9_ARATH
ID BBE9_ARATH Reviewed; 531 AA.
AC Q9SA86;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Berberine bridge enzyme-like 9 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 9 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN OrderedLocusNames=At1g30710 {ECO:0000312|Araport:AT1G30710};
GN ORFNames=T5I8.16 {ECO:0000312|EMBL:AAD25758.1};
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].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) 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; AC007060; AAD25758.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31263.1; -; Genomic_DNA.
DR EMBL; BT033024; ACE62892.1; -; mRNA.
DR PIR; F86432; F86432.
DR RefSeq; NP_174358.1; NM_102807.4.
DR AlphaFoldDB; Q9SA86; -.
DR SMR; Q9SA86; -.
DR STRING; 3702.AT1G30710.1; -.
DR PaxDb; Q9SA86; -.
DR PRIDE; Q9SA86; -.
DR ProteomicsDB; 241128; -.
DR EnsemblPlants; AT1G30710.1; AT1G30710.1; AT1G30710.
DR GeneID; 839951; -.
DR Gramene; AT1G30710.1; AT1G30710.1; AT1G30710.
DR KEGG; ath:AT1G30710; -.
DR Araport; AT1G30710; -.
DR TAIR; locus:2204614; AT1G30710.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9SA86; -.
DR OMA; CNGHSYA; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9SA86; -.
DR BioCyc; ARA:AT1G30710-MON; -.
DR PRO; PR:Q9SA86; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA86; 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 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..531
FT /note="Berberine bridge enzyme-like 9"
FT /id="PRO_5008180359"
FT DOMAIN 77..252
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 35..99
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CROSSLNK 114..177
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 531 AA; 59330 MW; BCF6FF7AFA920A2E CRC64;
MTSLTTQTLI ITIFLLTIPT SFASPPSLED VFAQCVTDFK PSNPKSPIQN YIYTQRSPNF
LTILNNYVRN LRYFNNMTRK PVAIVAAADV THIQATITCA KKLGLQLRIR SGGHDYDGMS
YLSTIDFVVL DMFNLRSINI DPKLDTAWVQ SGATLGEIYY GVANKSNDLR GFPAGICPGL
GAGGHFSGGG YGNMMRKYGL SIDNIIDAKI VDAKGRVLDR SSMGEDLFWA LRGGGAASFC
VVLAWKIKLV PVPAKVTVFN IETFGNTGSV NTTELVAKWQ EIADKIDNDL FIRLTLGSSN
KTVKASFMGM YLGNSSNLLE IMNAKFPELG LIKRECIEMK WIESVLFWLG IPPGTAPTTS
MLNRIPQKQI YLKRKSDYVQ KPISRTGLES IFKIMTENEN VTMAFNPYGG RMSEIPSTET
AFPHRAGNMF KIQYAANWFV PGEAVAKDCL SQTERLFEAM SPYVSKNPRE AFLNYRDVDI
GKSLNSTYEE GKVYGFKYFK DNFEKLVKIK SRVDPDNFFR YEQSIPVLSS H
