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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//