ID K4A838_SETIT Unreviewed; 543 AA. AC K4A838; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 24-JAN-2024, entry version 58. 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 Name=106804122 {ECO:0000313|EnsemblPlants:KQK88805}; GN ORFNames=SETIT_9G229700v2 {ECO:0000313|EMBL:RCV42618.1}; OS Setaria italica (Foxtail millet) (Panicum italicum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria. OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK88805, ECO:0000313|Proteomes:UP000004995}; RN [1] {ECO:0000313|EMBL:RCV42618.1, ECO:0000313|Proteomes:UP000004995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK88805, RC ECO:0000313|Proteomes:UP000004995}, and Yugu1 RC {ECO:0000313|EMBL:RCV42618.1}; RX PubMed=22580951; DOI=10.1038/nbt.2196; RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J., RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J., RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X., RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P., RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P., RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.; RT "Reference genome sequence of the model plant Setaria."; RL Nat. Biotechnol. 30:555-561(2012). RN [2] {ECO:0000313|EMBL:RCV42618.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV42618.1}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:KQK88805} RP IDENTIFICATION. RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK88805}; RG EnsemblPlants; RL Submitted (AUG-2018) to UniProtKB. 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}. 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; AGNK02005574; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CM003536; RCV42618.1; -; Genomic_DNA. DR RefSeq; XP_014660051.1; XM_014804565.1. DR AlphaFoldDB; K4A838; -. DR STRING; 4555.K4A838; -. DR EnsemblPlants; KQK88805; KQK88805; SETIT_035044mg. DR GeneID; 106804122; -. DR Gramene; KQK88805; KQK88805; SETIT_035044mg. DR KEGG; sita:106804122; -. DR eggNOG; ENOG502QTBX; Eukaryota. DR HOGENOM; CLU_016754_5_1_1; -. DR InParanoid; K4A838; -. DR OMA; WGRRNCE; -. DR OrthoDB; 46229at2759; -. DR Proteomes; UP000004995; Chromosome IX. 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; 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; BETA-AMYLASE 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31352:SF31; BETA-AMYLASE 1, CHLOROPLASTIC; 1. DR Pfam; PF01373; Glyco_hydro_14; 1. DR PRINTS; PR00750; BETAAMYLASE. DR PRINTS; PR00842; GLHYDLASE14B. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00506; BETA_AMYLASE_1; 1. DR PROSITE; PS00679; BETA_AMYLASE_2; 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 Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|RuleBase:RU000509}; KW Reference proteome {ECO:0000313|Proteomes:UP000004995}. FT REGION 11..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 256 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1" FT ACT_SITE 454 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" FT BINDING 369 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" FT BINDING 374 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" FT BINDING 416 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" FT BINDING 455..456 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" FT BINDING 488 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2" SQ SEQUENCE 543 AA; 58892 MW; 6DFD594A402FE230 CRC64; MAFNLAQSTA AAASVAPRTP RHAAAAPASV SVRKAGGAPP SSSGLRLQRQ ACCEPSVAPA RPVACRAAAA AAERASRRRA GVPVFVMMPL DTVKKCGTAL NRRKAVQASL AALKSAGVEG VMVDVWWGIA ESDGPGRYNF AGYAELMEMA RKTGLKVQAV MSFHQCGGNV GDSVNIPLPR WALEEMEKDQ DLCYTDQWGR RNFEYVSLGC DAMPVLKGRT PVECYTDFMR AFRDHFADYL GNTIVEIQVG MGPAGELRYP SYPESNGTWR FPGIGAFQCN DRYMLSSLKA AAEAAGKPEW GHGGPTDAGS YNNWPEDTIF FRRENGGWST EYGDFFLSWY SQMLMEHGDR ILTGASSVFS ASPVEVSVKV AGIHWHYGTR SHAPELTAGY YNTRHHDGYL PVARLLARHG AVLNFTCVEM RDHEQPQDAQ CMPEALVRQV GAAARAAGVG LAGENALPRY DGAAHDQVVS TAAERAAEDR MVAFTYLRMG ADLFHPDNWH RFAAFVRRMD GAGSCREAAE REARSVAQAT GSLVHEAAVA LRS //