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Berberine bridge enzyme-like 24 (AtBBE-like 24) (EC 1.1.1.-)

 BBE24_ARATH             Reviewed;         541 AA.
Q9FKV0; Q570D1;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 108.
RecName: Full=Berberine bridge enzyme-like 24 {ECO:0000303|PubMed:26037923};
Short=AtBBE-like 24 {ECO:0000303|PubMed:26037923};
EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
Flags: Precursor;
OrderedLocusNames=At5g44380 {ECO:0000312|Araport:AT5G44380};
ORFNames=K9L2.18 {ECO:0000312|EMBL:BAB10123.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[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].
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[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:0000250|UniProtKB:O64743}.
-!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93999.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB011475; BAB10123.1; -; Genomic_DNA.
EMBL; CP002688; AED95103.1; -; Genomic_DNA.
EMBL; AY093127; AAM13126.1; -; mRNA.
EMBL; AK220778; BAD93999.1; ALT_INIT; mRNA.
EMBL; AK226516; BAE98656.1; -; mRNA.
RefSeq; NP_199251.1; NM_123805.5.
UniGene; At.19702; -.
UniGene; At.26608; -.
ProteinModelPortal; Q9FKV0; -.
SMR; Q9FKV0; -.
STRING; 3702.AT5G44380.1; -.
SwissPalm; Q9FKV0; -.
PaxDb; Q9FKV0; -.
PRIDE; Q9FKV0; -.
EnsemblPlants; AT5G44380.1; AT5G44380.1; AT5G44380.
EnsemblPlants; AT5G44380.2; AT5G44380.2; AT5G44380.
GeneID; 834464; -.
Gramene; AT5G44380.1; AT5G44380.1; AT5G44380.
Gramene; AT5G44380.2; AT5G44380.2; AT5G44380.
KEGG; ath:AT5G44380; -.
Araport; AT5G44380; -.
TAIR; locus:2158720; AT5G44380.
eggNOG; COG0277; LUCA.
HOGENOM; HOG000238933; -.
OMA; YANWLEN; -.
OrthoDB; EOG09360CSE; -.
PhylomeDB; Q9FKV0; -.
PRO; PR:Q9FKV0; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FKV0; baseline and differential.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
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.
2: Evidence at transcript level;
Cell wall; Complete proteome; Disulfide bond; FAD; Flavoprotein;
Glycoprotein; Nucleotide-binding; Oxidoreductase; Reference proteome;
Secreted; Signal.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 541 Berberine bridge enzyme-like 24.
/FTId=PRO_0000438217.
DOMAIN 83 259 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 115 121 FAD. {ECO:0000250|UniProtKB:O64743}.
NP_BIND 183 184 FAD. {ECO:0000250|UniProtKB:O64743}.
NP_BIND 188 192 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 120 120 FAD (covalent; via 2 links, pros
nitrogen).
{ECO:0000250|UniProtKB:P30986}.
BINDING 126 126 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 184 184 FAD (covalent; via 2 links).
{ECO:0000250|UniProtKB:P30986}.
BINDING 198 198 FAD. {ECO:0000250|UniProtKB:O64743}.
BINDING 480 480 FAD. {ECO:0000250|UniProtKB:O64743}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 41 105 {ECO:0000250|UniProtKB:O64743}.
SEQUENCE 541 AA; 60616 MW; A568A2414CCABD85 CRC64;
MGNSKPLPTI SCIIVSVLYF SFYCITPTSS SASIQDQFIN CVKRNTHVSF PLEKTLFTPA
KNVSLFNQVL ESTAQNLQFL AKSMPKPGFI FRPIHQSQVQ ASIICSKKLG IHFRVRSGGH
DFEALSYVSR IEKPFILLDL SKLKQINVDI ESNSAWVQPG ATLGELYYRI AEKSKIHGFP
AGLCTSVGIG GYMTGGGYGT LMRKYGLAGD NVLDVKMVDA NGKLLDRAAM GEDLFWAIRG
GGGASFGIVL AWKIKLVPVP KTVTVFTVTK TLEQDARLKT ISKWQQISSK IIEEIHIRVV
LRAAGNDGNK TVTMTYLGQF LGEKGTLLKV MEKAFPELGL TQKDCTEMSW IEAALFHGGF
PTGSPIEILL QLKSPLGKDY FKATSDFVKE PIPVIGLKGI FKRLIEGNTT FLNWTPYGGM
MSKIPESAIP FPHRNGTLFK ILYYANWLEN DKTSSRKINW IKEIYNYMAP YVSSNPRQAY
VNYRDLDFGQ NKNNAKVNFI EAKIWGPKYF KGNFDRLVKI KTKVDPENFF RHEQSIPPMP
Y


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