UniProt/TrEMBL: A0A078I6T1

Database: UniProt/TrEMBL
Entry: A0A078I6T1_BRANA

LinkDB:  A0A078I6T1_BRANA 
Original site:  A0A078I6T1_BRANA

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   A0A078I6T1_BRANA        Unreviewed;       564 AA.
AC   A0A078I6T1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Beta-amylase {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
DE            EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
GN   Name=BnaC09g21440D {ECO:0000313|EMBL:CDY45566.1};
GN   ORFNames=DARMORV10_C07P12240.1 {ECO:0000313|EMBL:CAF1963361.1},
GN   GSBRNA2T00082283001 {ECO:0000313|EMBL:CDY45566.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY45566.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY45566.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
RN   [2] {ECO:0000313|EMBL:CDY45566.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF1963361.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides so as to remove successive maltose units from the
CC         non-reducing ends of the chains.; EC=3.2.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000546,
CC         ECO:0000256|RuleBase:RU000509};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family.
CC       {ECO:0000256|ARBA:ARBA00005652, ECO:0000256|RuleBase:RU000509}.
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DR   EMBL; HG994371; CAF1963361.1; -; Genomic_DNA.
DR   EMBL; LK032628; CDY45566.1; -; Genomic_DNA.
DR   RefSeq; XP_013750064.1; XM_013894610.1.
DR   SMR; A0A078I6T1; -.
DR   STRING; 3708.A0A078I6T1; -.
DR   PaxDb; 3708-A0A078I6T1; -.
DR   EnsemblPlants; CDY45566; CDY45566; GSBRNA2T00082283001.
DR   GeneID; 106452475; -.
DR   Gramene; CDY45566; CDY45566; GSBRNA2T00082283001.
DR   KEGG; bna:106452475; -.
DR   OMA; AREMCAF; -.
DR   OrthoDB; 46229at2759; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR018238; Glyco_hydro_14_CS.
DR   InterPro; IPR001371; Glyco_hydro_14B_pln.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31352:SF31; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   PRINTS; PR00842; GLHYDLASE14B.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR   PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000509};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000509};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000509};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU000509};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028999}.
FT   REGION          15..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        268
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        466
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         386
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         467..468
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         506
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ   SEQUENCE   564 AA;  62617 MW;  4C3358F31E3BBC5A CRC64;
     MAFNLTHQLG ALAGTPIKSG EMTTPSAESS LSVSPPSARM PISMNRNVSP PMSPVLGSRR
     ADLSVACKAF AVETVEEQRT YKEGGIGGEK GKGGVPVFVM MPLDSVTMGN TVNRRKAMRA
     SLQALKSAGV EGIMIDVWWG LVEREAPGAY NWGGYNELLE MAKKVGLKVQ AVMSFHQCGG
     NVGDSVTIPL PQWVVEEVDK DPDLAYTDQW GRRNHEYISL GADTLPVLKG RTPVQCYSDF
     MRAFRDNFKH LLGDTIVEIQ VGMGPAGELR YPSYPEQDGT WRFPGIGAFQ CYDKYSLSSL
     KAAAEAYGKP EWGGTGPTDA GHYNNWPEDT QFFKKEDGGW NTEYGEFFLT WYSQMLLDHG
     ERILSSAKSI FQDTSVKISV KIAGIHWHYG TRSHAPELTA GYYNTRFRDG YLPIAQMLAR
     HNAIFNFTCI EMRDHEQPQD ALCAPEKLVN QVALATLAAE VPLAGENALP RYDDHAHEQI
     LKASALSFDQ NSEGENREMC AFTYLRMNPE LFKADNWGKF VGFVKKMGEG RDSDRCQEEV
     EREAEHFVHV TQPLVQEAAV ALTH
//

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