ID   Q5F305_SOYBN            Unreviewed;       540 AA.
AC   Q5F305;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=bmy2 {ECO:0000313|EMBL:CAI39244.1};
GN   Synonyms=547683 {ECO:0000313|EnsemblPlants:KRH04262};
GN   ORFNames=GLYMA_17G150100 {ECO:0000313|EMBL:KRH04262.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:CAI39244.1};
RN   [1] {ECO:0000313|EMBL:CAI39244.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Katinakis P.;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRH04262.1, ECO:0000313|EnsemblPlants:KRH04262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH04262};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH04262.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [3] {ECO:0000313|EnsemblPlants:KRH04262}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH04262};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KRH04262.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH04262.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; AJ871579; CAI39244.1; -; mRNA.
DR   EMBL; CM000850; KRH04262.1; -; Genomic_DNA.
DR   RefSeq; NP_001236350.1; NM_001249421.1.
DR   AlphaFoldDB; Q5F305; -.
DR   SMR; Q5F305; -.
DR   STRING; 3847.Q5F305; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   PaxDb; 3847-GLYMA17G16020-1; -.
DR   EnsemblPlants; KRH04262; KRH04262; GLYMA_17G150100.
DR   GeneID; 547683; -.
DR   Gramene; KRH04262; KRH04262; GLYMA_17G150100.
DR   KEGG; gmx:547683; -.
DR   eggNOG; ENOG502QTBX; Eukaryota.
DR   HOGENOM; CLU_016754_5_1_1; -.
DR   InParanoid; Q5F305; -.
DR   OMA; THHQISH; -.
DR   OrthoDB; 46229at2759; -.
DR   Proteomes; UP000008827; Chromosome 17.
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:SF60; BETA-AMYLASE; 1.
DR   PANTHER; PTHR31352; 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.
PE   2: Evidence at transcript level;
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:UP000008827}.
FT   ACT_SITE        251
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        448
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         449..450
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ   SEQUENCE   540 AA;  60539 MW;  3748E17892DF09F2 CRC64;
     MALTLRSSTS FINQKETKVL KTSDNAPAIV SFSKFKPSSS LFRLRAKNSM QEAHHTREKW
     EKVLAPSVAH SHNDSKRVPV YVMLPLDTVT MGGSLNKPRA MNASLMALKS AGVEGVMVDA
     WWGLVEKEGP LKYNWEPYAE LVQMLQMHGL KLQVVMSFHQ CGGNVGDNCS IPLPPWVLEE
     ISKNPELVYT DRSGRRNPEY ISLGCDSVPV LNGRTPLQVY SDYMRSFRDK FRDYLGSVIV
     EIQLGMGPCG ELRYPSYPET NGTWRFPGIG EFQCYDKYMK ASLAAAAEDI GKKEWGGGGP
     HDSGQYNQFP EDTGFFKREG TWNTEYGQFF LEWYSGKLLE HGERILVSAK GIFETTGVKL
     SGKVAGIHWH YRARSHAAEL TAGYYNTRNN DGYLPIARML AKHGVVFNFT CMEMKDREQP
     DFANCSPEGL VHQVKMATTT ARAELAGENA LERYDADAYA QVLSTSKSES GSGLAAFTYL
     RMNKRLFEAD NWRHLVDFVR SMSEGGRRER LPAADSHGSD LYVGHIKATQ EKHTQEAALV
//