ID   Q652P5_ORYSJ            Unreviewed;       533 AA.
AC   Q652P5;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 135.
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   OrderedLocusNames=Os09g0569200 {ECO:0000313|EMBL:BAT09498.1};
GN   ORFNames=OSNPB_090569200 {ECO:0000313|EMBL:BAT09498.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:BAT09498.1, ECO:0000313|Proteomes:UP000059680};
RN   [1] {ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RA   Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA   Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA   Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA   Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA   Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA   Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA   Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA   Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA   Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA   Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA   Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA   Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA   Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA   Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA   Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA   Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA   Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA   Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA   Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA   Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA   Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA   Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA   Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA   Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA   Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA   Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA   Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA   Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA   Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA   Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA   Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA   Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA   Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA   Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA   Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA   Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA   Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA   Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA   Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA   Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2] {ECO:0000313|EMBL:BAT09498.1, ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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; AP014965; BAT09498.1; -; Genomic_DNA.
DR   RefSeq; XP_015611670.1; XM_015756184.1.
DR   AlphaFoldDB; Q652P5; -.
DR   SMR; Q652P5; -.
DR   STRING; 39947.Q652P5; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   PaxDb; 39947-Q652P5; -.
DR   EnsemblPlants; Os09t0569200-01; Os09t0569200-01; Os09g0569200.
DR   GeneID; 4347903; -.
DR   Gramene; Os09t0569200-01; Os09t0569200-01; Os09g0569200.
DR   KEGG; osa:4347903; -.
DR   eggNOG; ENOG502QTBX; Eukaryota.
DR   HOGENOM; CLU_016754_4_1_1; -.
DR   InParanoid; Q652P5; -.
DR   OMA; YKRLFHM; -.
DR   OrthoDB; 46229at2759; -.
DR   Proteomes; UP000059680; Chromosome 9.
DR   GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
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:SF62; BETA-AMYLASE 7; 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   1: Evidence at protein 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   Proteomics identification {ECO:0007829|ProteomicsDB:Q652P5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059680}.
FT   ACT_SITE        270
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        466
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         425
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         467..468
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         502
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ   SEQUENCE   533 AA;  59712 MW;  629B2E7577199DB5 CRC64;
     MISSPALFFL LQPGRPSIAA PPLPSSPAPP LRGISISPVA ARPISSLRSS SSIRIISPPH
     ALPDPLLSLP SMDPQEVPDL LPPRPPERDF AGTPYVPVYV MLPLGVVNGN GEVVDADVLV
     GQLRVLKAAG VDGVMVDCWW GNVEAHRPQE YNWTGYKRLF HMIRELKLKL QVVMSFHECG
     GNVGDDVSIP LPHWVTEIGR SNPDIYFTDR AGRRNTECLS WGIDKERVLQ GRTGVEVYFD
     YMRSFRVEFD EYFEDGIISE IEIGLGACGE LRYPSYPAKH GWKYPGIGEF QCYDRYLQKS
     LRRAAEARGH TIWARAPDSA GHYNSEPNLT GFFSDGGDYD SYYGRFFLNW YSQVLVDHAD
     RVLMLARLAF EGSDIAVKVS GVHWWYKTAS HAAELTAGFY NPCNRDGYAS IAAVLKKHGA
     ALNFTCVELR TMDQHEVFPE AFADPEGLVW QVLNAAWDAG IPVASENALP CYDRDGFNKI
     LENAKPLNDP DGRHLLGFTY LRLTKVLFER ANFLEFERFV KRMHGEAVLD LQV
//