BAMY2_ORYSJ
ID BAMY2_ORYSJ Reviewed; 557 AA.
AC Q10RZ1; A3ADZ2;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-amylase 2, chloroplastic {ECO:0000305};
DE Short=OsBamy2 {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=BAMY2 {ECO:0000303|PubMed:21512221};
GN OrderedLocusNames=Os03g0141200 {ECO:0000312|EMBL:BAF10840.1},
GN LOC_Os03g04770 {ECO:0000312|EMBL:ABF93905.1};
GN ORFNames=OsJ_09355 {ECO:0000312|EMBL:EAZ25531.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAZ25531.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DP000009; ABF93905.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF10840.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82226.1; -; Genomic_DNA.
DR EMBL; CM000140; EAZ25531.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK068968; BAG91188.1; -; mRNA.
DR RefSeq; XP_015632708.1; XM_015777222.1.
DR AlphaFoldDB; Q10RZ1; -.
DR SMR; Q10RZ1; -.
DR STRING; 4530.OS03T0141200-01; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR PaxDb; Q10RZ1; -.
DR PRIDE; Q10RZ1; -.
DR EnsemblPlants; Os03t0141200-01; Os03t0141200-01; Os03g0141200.
DR GeneID; 4331577; -.
DR Gramene; Os03t0141200-01; Os03t0141200-01; Os03g0141200.
DR KEGG; osa:4331577; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_5_1_1; -.
DR InParanoid; Q10RZ1; -.
DR OMA; MHSFTFL; -.
DR OrthoDB; 533202at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
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..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..557
FT /note="Beta-amylase 2, chloroplastic"
FT /id="PRO_0000440335"
FT ACT_SITE 267
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P10538,
FT ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 466..467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 499
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
SQ SEQUENCE 557 AA; 60757 MW; 8DF437F3327B5C45 CRC64;
MMSLNLAHQT GAAAAVAPAA PRTAVVAAAA GTVSAPAVAP AAAPSLQLQT QTVDPAAPAQ
GPDLPMAFQA LVESLPEEQH PDVGGEERRK VGVPVYVMMP LDTVRKDGNG LNRRKAVEAS
LKALKSAGAE GIMVDVWWGI AECEGPGRYN FTGYMELMEM AKKNGLKVQA VMSFHQCGGN
VGDSVTIPLP KWVLEEMDKD QDLAYTDRSG RRNYEYLSLG ADAMPVLKGR TPVQCYGDFM
RAFRDHFAAF MGNTIVEIQV GMGPAGELRY PSYPESNGTW RFPGIGEFQC YDRYMLSSLK
AAAEAVGKPE WGNAGPGDSG GYNDWPEDSP FFRREGGWNT PYGEFFMSWY SQMLLEHGER
ILSAASGVYT GTPGVKISVK VAGIHWHYGT RSHAAELTAG YYNTRHHDGY QPIARMLARH
GAVLNFTCVE MRNHEQPQDA QCRPEELVQQ VAAAARESGV GLAGENALPR YDETAHDQIV
TTAAEKAEEE RMVAFTYLRM GPDLFQPDNW RRFAAFVKRM TESGVRDVCR EQVEREAQGV
AHATGSLVHE AAVALSN
