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BBE17_ARATH
ID   BBE17_ARATH             Reviewed;         528 AA.
AC   Q9SVG7;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Berberine bridge enzyme-like 17 {ECO:0000303|PubMed:26037923};
DE            Short=AtBBE-like 17 {ECO:0000303|PubMed:26037923};
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g20800 {ECO:0000312|Araport:AT4G20800};
GN   ORFNames=F21C20.150 {ECO:0000312|EMBL:CAB45846.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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: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}.
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DR   EMBL; AL080254; CAB45846.1; -; Genomic_DNA.
DR   EMBL; AL161553; CAB79080.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84362.1; -; Genomic_DNA.
DR   EMBL; BT006176; AAP04159.1; -; mRNA.
DR   EMBL; BT008552; AAP40379.1; -; mRNA.
DR   EMBL; AK228650; BAF00557.1; -; mRNA.
DR   PIR; T10622; T10622.
DR   RefSeq; NP_193812.1; NM_118198.2.
DR   AlphaFoldDB; Q9SVG7; -.
DR   SMR; Q9SVG7; -.
DR   STRING; 3702.AT4G20800.1; -.
DR   PaxDb; Q9SVG7; -.
DR   PRIDE; Q9SVG7; -.
DR   ProteomicsDB; 241200; -.
DR   EnsemblPlants; AT4G20800.1; AT4G20800.1; AT4G20800.
DR   GeneID; 827828; -.
DR   Gramene; AT4G20800.1; AT4G20800.1; AT4G20800.
DR   KEGG; ath:AT4G20800; -.
DR   Araport; AT4G20800; -.
DR   TAIR; locus:2121509; AT4G20800.
DR   eggNOG; ENOG502QVGN; Eukaryota.
DR   HOGENOM; CLU_018354_6_0_1; -.
DR   InParanoid; Q9SVG7; -.
DR   OMA; MGELYTK; -.
DR   OrthoDB; 1049549at2759; -.
DR   PhylomeDB; Q9SVG7; -.
DR   BioCyc; ARA:AT4G20800-MON; -.
DR   PRO; PR:Q9SVG7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SVG7; 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   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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..528
FT                   /note="Berberine bridge enzyme-like 17"
FT                   /id="PRO_5008180492"
FT   DOMAIN          69..246
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        32..94
FT                   /evidence="ECO:0000250|UniProtKB:O64743"
FT   CROSSLNK        109..171
FT                   /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT                   Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:O64743"
SQ   SEQUENCE   528 AA;  58847 MW;  D70E7667AAAE3E7D CRC64;
     MKEVVYVLLL VLLVSVSDAN ETKPNIENFL RCLRNRTNPK NPIAEAIYTH ENSTFASSYV
     SYTNNKRCLN PNDTKLIAIV AAKHESHVQA TVVCAKSNGI QIRIRSGGHD YEGLSFTSSV
     PFVILDMHDL RSITIDVFRK QAWVDAGATM GELYTKIAAA SKTLAFAGGV CPTLGAGGHI
     SGGGYGNLIR KYGISVDHVV DARIVDVNGN ILTGATLGRD LLWAIRGGGG ASFGVILSWK
     INLVDVPKTV TVFKVNKTLE QGVTDVLYKW QLVSSKLPQD LFLRAMPKPV NGVVPSEKTI
     AVVFYAQFLG SARRLMAIMN KNLPELGLKR EDCYEMSWIN TTTFWQNYPV GTSTSVLLDR
     PSGPAGAFYK SKSDYVKKPI PKEEMEKIWK AMLKFNNMWM QWNPYGGVMD KIPADATAFP
     HRKGNLFKIQ YFALWTDANA TYANLGLMRD IYHEMEPYVS SNPREAFLNY RDIDVGSNPS
     GETNLEEAKI YGSKYFLGNF KRLMEVKAKY DPENFFRFEQ SIPPASAM
 
 
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