ID W9SDH2_9ROSA Unreviewed; 544 AA.
AC W9SDH2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=L484_023371 {ECO:0000313|EMBL:EXC26755.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC26755.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|EMBL:EXC26755.1}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schn.";
RL Submitted (JUN-2013) 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; KE346119; EXC26755.1; -; Genomic_DNA.
DR RefSeq; XP_010110537.1; XM_010112235.1.
DR AlphaFoldDB; W9SDH2; -.
DR STRING; 981085.W9SDH2; -.
DR GeneID; 21406136; -.
DR KEGG; mnt:21406136; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000030645; 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; 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 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:UP000030645}.
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 452
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 453..454
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 485
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 544 AA; 61241 MW; 7962842CC6EF8A8D CRC64;
MALTLRSSNY FLNLKDTKGL KTPDDLSGTV CFAQIKPSCR LRATKSSMKE AQISHEKNFT
PEGVRREKLH VLSSSHSPKN DSRVPVFVML PLDTLTLGGN LNKPRAMNAS LMALKAAGVE
GVMVDAWWGL VEKDGPLKYN WEGYAELVQM VEKHGLKLQF VMSFHQCGGN VGDSCSIPLP
PWVLEEISKN PDLVYTDRLG RRNPEYISLG CDSLPVLRGR TPIQVYTDYM RSFRERFRDF
LGDVIVEVQV GMGPCGELRY PAYPESNGTW KFPGIGEFQC YDKYMRASLE ASAEAIGKRD
WGQSGPHDAG QYRQFPEETG FFRNDGTWKT EYGQFFLEWY STKLSAHGDR ILAAAKGVFH
GTRAKLSGKI AGIHWHYRTR SHAAELTAGY YNTRNRNGYS ALAQIFAKHD VIFNFTCMEM
KDGEQPQHCS PEGLVQQVKM TTRSARIELA GENALERYDA SAYGRVLATS RSDSGNGLCA
FTYLRMNKRL FEGDNWRNLV EFVKSMSEGG RNRRLSECDS TGTDLYVGFI KEKNVKQTKE
AALV
//
