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Berberine bridge enzyme-like 28 (AtBBE-like 28) (EC 1.1.1.-)

 BBE28_ARATH             Reviewed;         533 AA.
Q9FI21; Q84WI1;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 108.
RecName: Full=Berberine bridge enzyme-like 28 {ECO:0000303|PubMed:26037923};
Short=AtBBE-like 28 {ECO:0000303|PubMed:26037923};
EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
Flags: Precursor;
OrderedLocusNames=At5g44440 {ECO:0000312|Araport:AT5G44440};
ORFNames=MFC16.10 {ECO:0000312|EMBL:BAB09151.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX.
Sequence features of the regions of 1,011,550 bp covered by seventeen
P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[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] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
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).
[5]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), FUNCTION, DISRUPTION
PHENOTYPE, DISULFIDE BONDS, AND INDUCTION BY SALT STRESS.
STRAIN=cv. Columbia;
PubMed=27276217; DOI=10.1371/journal.pone.0156892;
Daniel B., Wallner S., Steiner B., Oberdorfer G., Kumar P.,
van der Graaff E., Roitsch T., Sensen C.W., Gruber K., Macheroux P.;
"Structure of a berberine bridge enzyme-like enzyme with an active
site specific to the plant family brassicaceae.";
PLoS ONE 11:E0156892-E0156892(2016).
-!- FUNCTION: Involved in adaptation to salt stress.
{ECO:0000269|PubMed:27276217}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:O64743};
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000250|UniProtKB:O64743}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9FI21-1; Sequence=Displayed;
Note=Constructed according to the conserved gene model. No
experimental confirmation available.
{ECO:0000312|EMBL:AED95109.1};
Name=2;
IsoId=Q9FI21-2; Sequence=VSP_058627;
Note=No experimental confirmation available.
{ECO:0000312|EMBL:AAO29955.1, ECO:0000312|EMBL:AAP68305.1};
-!- INDUCTION: By salt stress, specifically in the root.
{ECO:0000269|PubMed:27276217}.
-!- DISRUPTION PHENOTYPE: No obvious developmental defects but reduced
biomass and reduced leaves number. Increased sensitivity to salt
stress. {ECO:0000269|PubMed:27276217}.
-!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB017065; BAB09151.1; -; Genomic_DNA.
EMBL; CP002688; AED95109.1; -; Genomic_DNA.
EMBL; BT003336; AAO29955.1; -; mRNA.
EMBL; BT008866; AAP68305.1; -; mRNA.
RefSeq; NP_199257.1; NM_123811.3. [Q9FI21-1]
UniGene; At.43771; -.
PDB; 5D79; X-ray; 1.85 A; A/B=1-533.
PDBsum; 5D79; -.
ProteinModelPortal; Q9FI21; -.
SMR; Q9FI21; -.
STRING; 3702.AT5G44440.1; -.
PaxDb; Q9FI21; -.
PRIDE; Q9FI21; -.
EnsemblPlants; AT5G44440.1; AT5G44440.1; AT5G44440. [Q9FI21-1]
EnsemblPlants; AT5G44440.2; AT5G44440.2; AT5G44440.
GeneID; 834471; -.
Gramene; AT5G44440.1; AT5G44440.1; AT5G44440. [Q9FI21-1]
Gramene; AT5G44440.2; AT5G44440.2; AT5G44440.
KEGG; ath:AT5G44440; -.
Araport; AT5G44440; -.
TAIR; locus:2163441; AT5G44440.
eggNOG; ENOG410IKHK; Eukaryota.
eggNOG; COG0277; LUCA.
HOGENOM; HOG000238933; -.
OMA; RSAGHCY; -.
OrthoDB; EOG09360CSE; -.
PhylomeDB; Q9FI21; -.
PRO; PR:Q9FI21; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FI21; baseline and differential.
GO; GO:0005618; C:cell wall; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
Gene3D; 3.30.43.10; -; 1.
InterPro; IPR012951; BBE.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell wall; Complete proteome;
Disulfide bond; FAD; Flavoprotein; Glycoprotein; Nucleotide-binding;
Oxidoreductase; Reference proteome; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 533 Berberine bridge enzyme-like 28.
/FTId=PRO_5008179916.
DOMAIN 74 249 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 106 112 FAD. {ECO:0000250|UniProtKB:O64743}.
NP_BIND 178 182 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 111 111 FAD (covalent; via 2 links, pros
nitrogen).
{ECO:0000250|UniProtKB:P30986}.
BINDING 117 117 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 188 188 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 239 239 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:O64743}.
BINDING 470 470 FAD. {ECO:0000250|UniProtKB:O64743}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 34 96 {ECO:0000244|PDB:5D79,
ECO:0000269|PubMed:27276217}.
VAR_SEQ 1 38 Missing (in isoform 2).
/FTId=VSP_058627.
HELIX 29 36 {ECO:0000244|PDB:5D79}.
HELIX 46 48 {ECO:0000244|PDB:5D79}.
STRAND 54 57 {ECO:0000244|PDB:5D79}.
HELIX 58 63 {ECO:0000244|PDB:5D79}.
HELIX 68 71 {ECO:0000244|PDB:5D79}.
STRAND 79 82 {ECO:0000244|PDB:5D79}.
HELIX 87 100 {ECO:0000244|PDB:5D79}.
STRAND 103 109 {ECO:0000244|PDB:5D79}.
TURN 116 118 {ECO:0000244|PDB:5D79}.
STRAND 121 123 {ECO:0000244|PDB:5D79}.
STRAND 125 129 {ECO:0000244|PDB:5D79}.
STRAND 136 139 {ECO:0000244|PDB:5D79}.
TURN 140 143 {ECO:0000244|PDB:5D79}.
STRAND 144 148 {ECO:0000244|PDB:5D79}.
HELIX 153 163 {ECO:0000244|PDB:5D79}.
STRAND 165 168 {ECO:0000244|PDB:5D79}.
HELIX 179 184 {ECO:0000244|PDB:5D79}.
HELIX 192 195 {ECO:0000244|PDB:5D79}.
HELIX 199 201 {ECO:0000244|PDB:5D79}.
STRAND 202 208 {ECO:0000244|PDB:5D79}.
HELIX 217 220 {ECO:0000244|PDB:5D79}.
HELIX 222 227 {ECO:0000244|PDB:5D79}.
TURN 228 230 {ECO:0000244|PDB:5D79}.
HELIX 233 235 {ECO:0000244|PDB:5D79}.
STRAND 238 245 {ECO:0000244|PDB:5D79}.
STRAND 253 260 {ECO:0000244|PDB:5D79}.
HELIX 263 276 {ECO:0000244|PDB:5D79}.
TURN 277 279 {ECO:0000244|PDB:5D79}.
STRAND 284 292 {ECO:0000244|PDB:5D79}.
STRAND 296 308 {ECO:0000244|PDB:5D79}.
HELIX 310 320 {ECO:0000244|PDB:5D79}.
HELIX 322 324 {ECO:0000244|PDB:5D79}.
HELIX 328 330 {ECO:0000244|PDB:5D79}.
STRAND 331 334 {ECO:0000244|PDB:5D79}.
HELIX 336 343 {ECO:0000244|PDB:5D79}.
HELIX 352 356 {ECO:0000244|PDB:5D79}.
STRAND 363 374 {ECO:0000244|PDB:5D79}.
HELIX 378 388 {ECO:0000244|PDB:5D79}.
HELIX 391 393 {ECO:0000244|PDB:5D79}.
STRAND 396 402 {ECO:0000244|PDB:5D79}.
HELIX 406 409 {ECO:0000244|PDB:5D79}.
HELIX 412 414 {ECO:0000244|PDB:5D79}.
STRAND 425 434 {ECO:0000244|PDB:5D79}.
HELIX 435 439 {ECO:0000244|PDB:5D79}.
HELIX 441 458 {ECO:0000244|PDB:5D79}.
HELIX 459 461 {ECO:0000244|PDB:5D79}.
HELIX 476 478 {ECO:0000244|PDB:5D79}.
STRAND 482 487 {ECO:0000244|PDB:5D79}.
HELIX 488 500 {ECO:0000244|PDB:5D79}.
HELIX 501 503 {ECO:0000244|PDB:5D79}.
HELIX 504 514 {ECO:0000244|PDB:5D79}.
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


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