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Database: UniProt
Entry: A0A0D2U7G9_GOSRA
LinkDB: A0A0D2U7G9_GOSRA
Original site: A0A0D2U7G9_GOSRA 
ID   A0A0D2U7G9_GOSRA        Unreviewed;       637 AA.
AC   A0A0D2U7G9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE            EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN   ORFNames=B456_008G218300 {ECO:0000313|EMBL:KJB51475.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB51475.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB51475.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
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|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; CM001747; KJB51475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2U7G9; -.
DR   EnsemblPlants; KJB51475; KJB51475; B456_008G218300.
DR   Gramene; KJB51475; KJB51475; B456_008G218300.
DR   OMA; NSAWDQG; -.
DR   Proteomes; UP000032304; Chromosome 8.
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; IPR008540; BES1_N.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31352:SF8; BETA-AMYLASE 8; 1.
DR   Pfam; PF05687; BES1_N; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000509};
KW   Glycosidase {ECO:0000256|RuleBase:RU000509};
KW   Hydrolase {ECO:0000256|RuleBase:RU000509};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU000509};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT   DOMAIN          46..174
FT                   /note="BES1/BZR1 plant transcription factor N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05687"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        570
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
SQ   SEQUENCE   637 AA;  72339 MW;  F267C1682CB7DE1F CRC64;
     MESQPQPQPQ PRRPRGFAAT AAAAAASVSP TGTPSGSAGA STASSGKGKR EREKEKERTK
     LRERHRRAIT SRMLAGLRQY GNFPLPARAD MNDVLAALAR EAGWTVEPDG TTYRHSPPPQ
     HQQHLNCSVK ATLDCQQPVV RIDDSLSPAS LDSVVIAERD TRSEKYPSTS PINSVECLEA
     DQLIQDVHST EHDNDFTGTQ YVPVYVKLST GVINNFCQLA DPDGVRQELS HMNSLNVDGV
     IVDCWWGIVE CWNPQKYVWS GYRELFNYIR EFKMKIQVVM AFHEYGRTDS ADVLISLPNW
     ILEIGKENQD IFFTDREGRR TTEFLSWGID KERVLNGRTG VEVYFDFMRS FRTEFDDLFA
     EGLISAVEIG LGPSGELRYP SFSERMGWRY PGIGEFQCYD KYLQQHLQRA AKLRGHSFWA
     RGPDNAGHYN SRPHETGFFC ERGDYDSYYG RFFLHWYAQA LMDHADNVLS LANLAFEETK
     IIVKIPAVYW WYKTSSHAAE LTAGYYNPTN QDGYSPVFEV LKKHSVTVKF VCYGLQICSY
     ENDEAFADPE GLSWQVLNSV WDRGLKVAGE NTLSCYDKEG CLRIIETAKP RNDPDRRHFS
     FFVYQQPSPL VQGVICLPDL DYFIKCMHGD ITGDLVP
//
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