ID B9S1Q4_RICCO Unreviewed; 668 AA.
AC B9S1Q4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN ORFNames=RCOM_0867240 {ECO:0000313|EMBL:EEF42523.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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|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; EQ973844; EEF42523.1; -; Genomic_DNA.
DR AlphaFoldDB; B9S1Q4; -.
DR STRING; 3988.B9S1Q4; -.
DR eggNOG; ENOG502QW2E; Eukaryota.
DR InParanoid; B9S1Q4; -.
DR Proteomes; UP000008311; 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; IPR008540; BES1_N.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31352:SF8; BETA-AMYLASE 8; 1.
DR Pfam; PF05687; BES1_N; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000509};
KW Glycosidase {ECO:0000256|RuleBase:RU000509, ECO:0000313|EMBL:EEF42523.1};
KW Hydrolase {ECO:0000256|RuleBase:RU000509, ECO:0000313|EMBL:EEF42523.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU000509};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT DOMAIN 70..213
FT /note="BES1/BZR1 plant transcription factor N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05687"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 75471 MW; DD0D600BF0D96073 CRC64;
MTSNSNQDVL LDPQIDHYSQ TQSQPQPHPV QSNSHHIQPQ PRRPRGFAAT AAAAAAATDP
TNTTAVNVSG RGKREREKEK ERTKLRERHR RAITSRMLAG LRQYGNFPLP ARADMNDVLA
ALAREAGWTV ESDGTTYRQS PAPSQLGSFG VRSVESPVST AKAAAALECH NHHQQSVLRI
DESLSPPSLD SVVMTEGDTR TDKFAPLTSV DSLDADQLIQ DVRSGEHEGD FTSTSYVPVY
VMLATGFINN FCQLVDPQGV RQELSHIKSL DVDGVVVECW WGIVEAWGPQ KYVWSGYREL
FNIIREFKLK LQVVMAFYEY QGSDSEEVLI SLPQWVLEIG KENQDIFFTD REGRRNTECL
SWGIDKERVL KGRTGIEVYF DFMRSFRVEF DDLFAEGIIS AVEIGLGASG ELKYPCFPER
MGWRYPGIGE FQCYDKYLQQ NLRSAAQSRG HPFWARGPDN AGQYNSRPHE TGFFCERGDY
DSYFGRFFLH WYARTLIDHA DNVLSLASLT FEDTRIIVKI PAVYWWYKTS SHAAELTAGY
HNPTNQDGYS PVFEALKKHS VTVKFVCSGL QVSAHENDEV LADPEGLSWQ VLNSAWDRGL
TVAGVNVLSC YDREGCMRVV EMAKPRCNPD HRQFAFFVYQ QPSPLVPGTL CFTELDYFIK
CMHGKNKP
//