BAMY1_ORYSJ
ID BAMY1_ORYSJ Reviewed; 535 AA.
AC Q9AV88; I3QD77; Q7XDM6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Beta-amylase 1, chloroplastic {ECO:0000305};
DE Short=OsBamy1 {ECO:0000303|PubMed:21512221};
DE EC=3.2.1.2 {ECO:0000269|PubMed:21512221};
DE AltName: Full=4-alpha-D-glucan maltohydrolase {ECO:0000305};
DE Flags: Precursor;
GN Name=BAMY1 {ECO:0000303|PubMed:21512221};
GN OrderedLocusNames=Os10g0465700 {ECO:0000312|EMBL:BAF26712.1},
GN LOC_Os10g32810 {ECO:0000312|EMBL:AAP54185.1};
GN ORFNames=OSJNBa0006L06.1 {ECO:0000312|EMBL:AAK27799.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yoon U.H.;
RT "Structural and expression analysis of booting stage genes in Oryza sativa
RT L.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21512221; DOI=10.1271/bbb.100872;
RA Koide T., Ohnishi Y., Horinouchi S.;
RT "Characterization of recombinant beta-amylases from Oryza sativa.";
RL Biosci. Biotechnol. Biochem. 75:793-796(2011).
CC -!- FUNCTION: Possesses beta-amylase activity in vitro (PubMed:21512221).
CC May be involved in cold resistance by mediating the accumulation of
CC maltose upon freezing stress, thus contributing to the protection of
CC membranes (Probable). {ECO:0000269|PubMed:21512221, ECO:0000305}.
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:0000269|PubMed:21512221};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:21512221};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:21512221};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR EMBL; JF969232; AFI71858.1; -; mRNA.
DR EMBL; AC022457; AAK27799.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP54185.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26712.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11208.1; -; Genomic_DNA.
DR EMBL; AK067249; BAG90332.1; -; mRNA.
DR AlphaFoldDB; Q9AV88; -.
DR SMR; Q9AV88; -.
DR STRING; 4530.OS10T0465700-01; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR PaxDb; Q9AV88; -.
DR PRIDE; Q9AV88; -.
DR EnsemblPlants; Os10t0465700-01; Os10t0465700-01; Os10g0465700.
DR Gramene; Os10t0465700-01; Os10t0465700-01; Os10g0465700.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_5_1_1; -.
DR InParanoid; Q9AV88; -.
DR OMA; PGSYNWG; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 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; PTHR31352; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Glycosidase; Hydrolase; Plastid;
KW Polysaccharide degradation; Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..535
FT /note="Beta-amylase 1, chloroplastic"
FT /id="PRO_0000440334"
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P10538,
FT ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 446
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 447..448
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT CONFLICT 352
FT /note="D -> A (in Ref. 1; AFI71858)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="Y -> F (in Ref. 1; AFI71858)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="A -> V (in Ref. 1; AFI71858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 57952 MW; 05291BA2102E76E0 CRC64;
MALNLAQSAA AAACFATAGD ARRAASVVAM PSSSSSATTS LRMKRQAACE PVACRAVARH
VAAAAASSRR NGVPVFVMMP LDTVSKCGSA LNRRKAVAAS LAALKSAGVE GIMVDVWWGI
VESEGPGRYN FDGYVELMEM ARKTGLKVQA VMSFHQCGGN VGDSVNIPLP RWVVEEMEKD
NDLAYTDQWG RRNFEYISLG CDAMPVFKGR TPVECYTDFM RAFRDHFASF LGDTIVEIQV
GMGPAGELRY PSYPESNGTW RFPGIGAFQC NDRYMRSSLK AAAEARGKPE WGHGGPTDAG
GYNNWPEDTV FFRGDCGGWS TEYGEFFLSW YSQMLLEHGE RVLSGATSVF GDGAGAKISV
KVAGIHWHYG TRSHAPELTA GYYNTRHRDG YLPIARMLAR HGAVLNFTCV EMRDHEQPQE
AQCMPEALVR QVAAAARAAG VGLAGENALP RYDGTAHDQV VAAAADRAAE DRMVAFTYLR
MGPDLFHPDN WRRFVAFVRR MSESGSPREA AESAAHGVAQ ATGSLVHEAA VALRS
