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Database: UniProt
Entry: A0A0D2SAN7_GOSRA
LinkDB: A0A0D2SAN7_GOSRA
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ID   A0A0D2SAN7_GOSRA        Unreviewed;       397 AA.
AC   A0A0D2SAN7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ORFNames=B456_007G099100 {ECO:0000313|EMBL:KJB41329.1};
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:KJB41329.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB41329.1, 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|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; CM001746; KJB41329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2SAN7; -.
DR   EnsemblPlants; KJB41329; KJB41329; B456_007G099100.
DR   Gramene; KJB41329; KJB41329; B456_007G099100.
DR   Proteomes; UP000032304; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR018238; Glyco_hydro_14_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31352:SF62; BETA-AMYLASE 7; 1.
DR   Pfam; PF05687; BES1_N; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 1.
PE   3: Inferred from homology;
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU000509};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..207
FT                   /note="BES1/BZR1 plant transcription factor N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05687"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   397 AA;  43949 MW;  937F315A24CC4300 CRC64;
     MSADMQKLIG ANEEDDEEEI EMDVKEEDNE DHENGQKHIA AQMMLGADGV MPSTSHQFQI
     QQQLQEQVST PGGGARRSRP LEEKERTKLR ERHRRAITAR ILAGLRKHGN YNLRVRADIN
     DVIAALAREA GWVVLPDGTT FPSRSQGSRP AGDSSAGLTS SSSQMLSQQV PPTSLQGVSS
     GYCASVEYNA CHMKGVFMPT PAPYDLSSSG HSQSSGMVGN GGEQTESLPL IAGSMEVINE
     QLGVVNMKCE LVDPDGLLKQ LRVLKSINVD GVMIDCWWGI VEADAPQEYN WNGYRRLFQM
     VHELKLKLQV VMSFHECGGN VGDDVCIPLP HWVAEIGRSN PDIFFTDREG RRNTECLSWG
     IDKERVLRGR TAVEVLVFNI TVNIIVYIMQ TAFVLNH
//
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