ID A0A0D3DEJ8_BRAOL Unreviewed; 547 AA.
AC A0A0D3DEJ8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=106306418 {ECO:0000313|EnsemblPlants:Bo7g104960.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo7g104960.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo7g104960.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo7g104960.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013598485.1; XM_013743031.1.
DR AlphaFoldDB; A0A0D3DEJ8; -.
DR SMR; A0A0D3DEJ8; -.
DR STRING; 109376.A0A0D3DEJ8; -.
DR EnsemblPlants; Bo7g104960.1; Bo7g104960.1; Bo7g104960.
DR GeneID; 106306418; -.
DR Gramene; Bo7g104960.1; Bo7g104960.1; Bo7g104960.
DR KEGG; boe:106306418; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_1_1_1; -.
DR OMA; WNSEYGR; -.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000032141; Chromosome C7.
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:SF1; BETA-AMYLASE 3, 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.
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:UP000032141}.
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 258
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 455
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 456..457
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 547 AA; 61369 MW; D7DAA57E0F796117 CRC64;
MELTLNSSSS LIKRKDAKSS RIQENSSNMS FAKTKPPTYQ FQAKSSVKEM KFTHEKTYKP
ESETTERWEK LHVLSYPHPK NDSSVPVFVM LPLDTVTMSG HLNKPRAMNA SLMALKGAGV
EGVMVDAWWG LVEKDGPMKY NWEGYAELIQ MVQKHGLKLQ VVMSFHQCGG NVGDSCSIPL
PPWVLEEISK NPDLVYTDKS GRRNPEYISL GCDSVPVLRG RTPIQVYSDF MRSFRERFDN
YIGGVIAEIQ VGMGPCGELR YPSYPESNGT WRFPGIGEFQ CYDKYMKSSL QAYAELIGKT
NWGTSGPHDA GEYKNLPEDT EFFRRDGTWN SEYGKFFMEW YSGKLLEHGD KLLSSAKAIF
QGSGAKLSGK VAGIHWHYNT RSHAAELTAG YYNTRNHDGY LPIAKMFNKH GVVLNFTCME
MKDGEQPEHA NCSPEGLVKQ VQNATRQAGT ELAGENALER YDSSAFGQVV ATNRSDSGNG
LTAFTYLRMN KRLFEGQNWQ QLVEFVKNMK EGGHGRRLSE EDTTGSDLYV GFVGSKISET
VEEAALV
//
