BBE13_ARATH
ID BBE13_ARATH Reviewed; 534 AA.
AC Q93ZA3; Q9SA92; Q9SY15;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Berberine bridge enzyme-like 13 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 13 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.194 {ECO:0000269|PubMed:26037923};
DE EC=1.1.1.195 {ECO:0000269|PubMed:26037923};
DE Flags: Precursor;
GN OrderedLocusNames=At1g30760 {ECO:0000312|Araport:AT1G30760};
GN ORFNames=T17H7.1 {ECO:0000312|EMBL:AAD32926.1},
GN T5I8.22 {ECO:0000312|EMBL:AAD25763.1};
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;
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 FUNCTION, CATALYTIC ACTIVITY, 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 -!- FUNCTION: Mediates oxidation of cinnamyl alcohol and of p-hydroxylated
CC derivatives of cinnamyl alcohol (i.e. the monolignols p-coumaryl-,
CC coniferyl-, and sinapyl alcohol) to their corresponding aldehydes. Can
CC use cinnamyl alcohol and derivatives, as well as beta-O-glycosylated
CC form of coniferyl alcohol (coniferin) as substrate.
CC {ECO:0000269|PubMed:26037923}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000269|PubMed:26037923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.194; Evidence={ECO:0000269|PubMed:26037923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000269|PubMed:26037923};
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 -!- PATHWAY: Phenylpropanoid metabolism.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:O64743}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25763.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD32926.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004135; AAD32926.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007060; AAD25763.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31270.1; -; Genomic_DNA.
DR EMBL; AY057687; AAL15318.1; -; mRNA.
DR EMBL; BT004513; AAO42759.1; -; mRNA.
DR PIR; D86433; D86433.
DR RefSeq; NP_001319117.1; NM_001332928.1.
DR AlphaFoldDB; Q93ZA3; -.
DR SMR; Q93ZA3; -.
DR STRING; 3702.AT1G30760.1; -.
DR PaxDb; Q93ZA3; -.
DR PRIDE; Q93ZA3; -.
DR ProteomicsDB; 241125; -.
DR EnsemblPlants; AT1G30760.1; AT1G30760.1; AT1G30760.
DR GeneID; 839958; -.
DR Gramene; AT1G30760.1; AT1G30760.1; AT1G30760.
DR KEGG; ath:AT1G30760; -.
DR Araport; AT1G30760; -.
DR TAIR; locus:2204579; AT1G30760.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q93ZA3; -.
DR PhylomeDB; Q93ZA3; -.
DR BRENDA; 1.21.3.3; 399.
DR PRO; PR:Q93ZA3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93ZA3; 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:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:TAIR.
DR GO; GO:0050268; F:coniferyl-alcohol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
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 Cell wall; Disulfide bond; FAD; Flavoprotein; Glycoprotein; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..534
FT /note="Berberine bridge enzyme-like 13"
FT /id="PRO_5008179559"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 38..102
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CROSSLNK 117..181
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 534 AA; 60192 MW; 99B05752E01E3D8F CRC64;
MAFVLMNNTN AFLVTLLLLS LSYIPLSFST IQQDFVMCLV DNSDASFPMD SSFFTHDLNA
SSFKLALETS AQNLRYLMPS NPKPEFIFEP LYETHVQAAV LCAKKLKLHL RLRSGGHDYE
GLSYVSEMET AFVIVDLSKL RQISVDIESN SAWVHAGASI GEVYYRIQEK SKIHGFPAGL
CTSLGIGGHI IGGAYGSMMR KFGLGADNVL DARIVDADGK ILNRAAMGED VFWAIRGGGG
GSFGVILAWK IKLVPVPEIV TVFTVTRTLE QDGTKLLYKW QQVADKLDED LFIRVIIQPT
SKTPKSKERT ISTSYQGQFL GDANRLLQVM QRSFPQLGLT KKDCLETSWI KSVMYIAGFP
STAPSEALLD GKSLFKNYFK AKSDYVEEPI PVEGLEGLWE KLLEEDSPLT IWNPYGGMMA
KIPETETPFP HRSGTLFKIQ WLTLWQDGKT SEAKHMGWMR EMYSYMEQYV SKSPRSAYVN
YRDLDLGMNG KGSDAREWGN RYFKGNFERL VEIKAKFDPE NFFRHEQSIP TELE
