BBE28_ARATH
ID BBE28_ARATH Reviewed; 533 AA.
AC Q9FI21; Q84WI1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Berberine bridge enzyme-like 28 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 28 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN OrderedLocusNames=At5g44440 {ECO:0000312|Araport:AT5G44440};
GN ORFNames=MFC16.10 {ECO:0000312|EMBL:BAB09151.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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] (ISOFORM 2).
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 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH FAD, FUNCTION,
RP DISRUPTION PHENOTYPE, DISULFIDE BONDS, AND INDUCTION BY SALT STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=27276217; DOI=10.1371/journal.pone.0156892;
RA Daniel B., Wallner S., Steiner B., Oberdorfer G., Kumar P.,
RA van der Graaff E., Roitsch T., Sensen C.W., Gruber K., Macheroux P.;
RT "Structure of a berberine bridge enzyme-like enzyme with an active site
RT specific to the plant family brassicaceae.";
RL PLoS ONE 11:E0156892-E0156892(2016).
CC -!- FUNCTION: Involved in adaptation to salt stress.
CC {ECO:0000269|PubMed:27276217}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:27276217};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:O64743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FI21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FI21-2; Sequence=VSP_058627;
CC -!- INDUCTION: By salt stress, specifically in the root.
CC {ECO:0000269|PubMed:27276217}.
CC -!- DISRUPTION PHENOTYPE: No obvious developmental defects but reduced
CC biomass and reduced leaves number. Increased sensitivity to salt
CC stress. {ECO:0000269|PubMed:27276217}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB017065; BAB09151.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95109.1; -; Genomic_DNA.
DR EMBL; BT003336; AAO29955.1; -; mRNA.
DR EMBL; BT008866; AAP68305.1; -; mRNA.
DR RefSeq; NP_199257.1; NM_123811.3. [Q9FI21-1]
DR PDB; 5D79; X-ray; 1.85 A; A/B=1-533.
DR PDBsum; 5D79; -.
DR AlphaFoldDB; Q9FI21; -.
DR SMR; Q9FI21; -.
DR STRING; 3702.AT5G44440.1; -.
DR PaxDb; Q9FI21; -.
DR PRIDE; Q9FI21; -.
DR EnsemblPlants; AT5G44440.1; AT5G44440.1; AT5G44440. [Q9FI21-1]
DR GeneID; 834471; -.
DR Gramene; AT5G44440.1; AT5G44440.1; AT5G44440. [Q9FI21-1]
DR KEGG; ath:AT5G44440; -.
DR Araport; AT5G44440; -.
DR TAIR; locus:2163441; AT5G44440.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FI21; -.
DR OMA; ATIRCSK; -.
DR PhylomeDB; Q9FI21; -.
DR BRENDA; 1.21.3.3; 399.
DR PRO; PR:Q9FI21; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI21; 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 GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
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; Alternative splicing; Cell wall; Disulfide bond; FAD;
KW Flavoprotein; Glycoprotein; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..533
FT /note="Berberine bridge enzyme-like 28"
FT /id="PRO_5008179916"
FT DOMAIN 74..249
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 111
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000269|PubMed:27276217"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 34..96
FT /evidence="ECO:0000269|PubMed:27276217,
FT ECO:0007744|PDB:5D79"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /id="VSP_058627"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:5D79"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:5D79"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:5D79"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:5D79"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 296..308
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 363..374
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 425..434
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 441..458
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:5D79"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 488..500
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:5D79"
FT HELIX 504..514
FT /evidence="ECO:0007829|PDB:5D79"
SQ SEQUENCE 533 AA; 60137 MW; 7EA3620D941F858E CRC64;
MEFSSFLFTI LLFSLNISPL VSAHGSNHED FLKCLSYRMN DNTVEPKVIH TSKDSSFFSI
LDSSIQNPRF SVSETPKPVS IITPVKASDV QTVIRCAQLH GIHVRTRSAG HCYEGLSYIA
YNKPFAVIDL RNLRSISLDV DNRTGWVQTG ATAGELYYEI GKTTKSLAFP AGIHPTVGVG
GQFSGGGYGT LLRKYGLAAD NIIDALVVDA SGRILDRQAM GEDYFWAIRG GGGSSFGVIL
SWKVKLVDVP STITVFKVQK TSKKEAVRII KKWQYAADKV PDDLFIRTTL ERSNKNAVHA
LFTGLYIGPV NNLLALMEEK FPELGLEKEG CEEMSWIESV LWFADFPKGE SLGVLTNRER
TSLSFKGKDD FVQEPIPEAA IQEIWRRLEA PEARLGKIIL TPFGGKMSEM AEYETPFPHR
GGNLYEIQYV AYWREEEDKN KTETDKYLKW VDSVYEFMTP YVSKSPRGAY VNFKDMDLGM
YLGKKKTKYE EGKSWGVKYF KNNFERLVRV KTRVDPTDFF CDEQSIPLVN KVT
