ID   C5WYV3_SORBI            Unreviewed;       564 AA.
AC   C5WYV3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
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=SORBI_3001G508800 {ECO:0000313|EMBL:EER95531.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EER95531.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EER95531.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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; CM000760; EER95531.1; -; Genomic_DNA.
DR   RefSeq; XP_002468533.1; XM_002468488.1.
DR   AlphaFoldDB; C5WYV3; -.
DR   STRING; 4558.C5WYV3; -.
DR   EnsemblPlants; EER95531; EER95531; SORBI_3001G508800.
DR   GeneID; 8080586; -.
DR   Gramene; EER95531; EER95531; SORBI_3001G508800.
DR   KEGG; sbi:8080586; -.
DR   eggNOG; ENOG502QTBX; Eukaryota.
DR   HOGENOM; CLU_016754_5_1_1; -.
DR   InParanoid; C5WYV3; -.
DR   OMA; ARENMYA; -.
DR   OrthoDB; 46229at2759; -.
DR   Proteomes; UP000000768; Chromosome 1.
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:SF54; BETA-AMYLASE 2, 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:UP000000768}.
FT   ACT_SITE        274
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        472
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         434
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         473..474
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;  60984 MW;  8368513009B5ECD1 CRC64;
     MMALNLAHQT GAAVTAAPTA PRSAVVAAAA TVSAPSASAS AAPAPALQMQ TMTVDAAPAQ
     APDAVKPDLA MACQALVEGS TPDEAQHADV AAELKTKAGV PVFVMMPLDT VRKDGNSLNR
     RKAVEASLAA LKSAGVEGIM VDVWWGIAEA DGPGQYNFNG YMELMEMARK TGLKVQAVMS
     FHQCGGNVGD SVTIPLPRWV VEEMDKDQDL AYTDRSGRRN YEYVSLGCDT LPVLKGRTPI
     QCYADFMRAF RDHFATFMGN TIVEIQVGMG PAGELRYPSY PESDGTWSFP GIGEFQCYDR
     YMLSSLKAAA ESVGKPEWGN GGPGDAGGYK NWPEDTGFFR REGGWSNEYG QFFMSWYSQM
     LLEHGERILS AATGVYTGSP GVKISVKVAG IHWHYGTRSH AAELTAGYYN TRHHDGYAPI
     ARMLARHGAV LNFTCVEMRD HEQPQDAQCR PEALVQQVAA AAREAGVGLA GENALPRYDE
     TAHDQVVATA ADRAAEDRMV AFTYLRMGPD LFQPDNWRRF AAFVKRMSQP GARDACREQV
     EREADGVAHA TQPLVHEAAV ALTN
//