ID AMYB_IPOBA Reviewed; 499 AA. AC P10537; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 02-SEP-2026, entry version 134. DE RecName: Full=Beta-amylase; DE EC=3.2.1.2; DE AltName: Full=1,4-alpha-D-glucan maltohydrolase; GN Name=BMY1; Synonyms=AMYB; OS Ipomoea batatas (Sweet potato) (Convolvulus batatas). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea. OX NCBI_TaxID=4120; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Kokei No. 14; TISSUE=Tuberous root; RX PubMed=1837016; DOI=10.1093/oxfordjournals.jbchem.a123556; RA Yoshida N., Nakamura K.; RT "Molecular cloning and expression in Escherichia coli of cDNA encoding the RT subunit of sweet potato beta-amylase."; RL J. Biochem. 110:196-201(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1383095; DOI=10.1016/0378-1119(92)90101-t; RA Yoshida N., Hayashi K., Nakamura K.; RT "A nuclear gene encoding beta-amylase of sweet potato."; RL Gene 120:255-259(1992). RN [3] RP PROTEIN SEQUENCE OF 2-499, AND ACTIVE SITE GLU-188. RC TISSUE=Tuberous root; RX PubMed=8103452; DOI=10.1111/j.1432-1033.1993.tb18112.x; RA Toda H., Nitta Y., Asanami S., Kim J.P., Sakiyama F.; RT "Sweet potato beta-amylase. Primary structure and identification of the RT active-site glutamyl residue."; RL Eur. J. Biochem. 216:25-38(1993). RN [4] RP CRYSTALLIZATION, AND X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=7777485; DOI=10.1002/prot.340210204; RA Cheong C.G., Eom S.H., Chang C., Shin D.H., Song H.Y., Min K., Moon J.H., RA Kim K.K., Hwang K.Y., Suh S.W.; RT "Crystallization, molecular replacement solution, and refinement of RT tetrameric beta-amylase from sweet potato."; RL Proteins 21:105-117(1995). 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5-6.; CC Temperature dependence: CC Optimum temperature is 50-55 degrees Celsius.; CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}. 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; D01022; BAA00828.1; -; mRNA. DR EMBL; D12882; BAA02286.1; -; Genomic_DNA. DR PIR; JC1447; JC1447. DR PDB; 1FA2; X-ray; 2.30 A; A=2-499. DR PDB; 5WQS; X-ray; 1.90 A; A=2-499. DR PDB; 5WQU; X-ray; 2.49 A; A=2-499. DR AlphaFoldDB; P10537; -. DR PCDDB; P10537; -. DR SASBDB; P10537; -. DR SMR; P10537; -. DR CAZy; GH14; Glycoside Hydrolase Family 14. DR BRENDA; 3.2.1.2; 2773. DR EvolutionaryTrace; P10537; -. DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro. DR FunFam; 3.20.20.80:FF:000066; Beta-amylase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR001554; Glyco_hydro_14. DR InterPro; IPR018238; Glyco_hydro_14_CS. DR InterPro; IPR001371; Glyco_hydro_14B_pln. DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31352:SF40; BETA-AMYLASE 6; 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. DR PDBsum; 1FA2; -. DR PDBsum; 5WQS; -. DR PDBsum; 5WQU; -. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing; KW Glycosidase; Hydrolase; Polysaccharide degradation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8103452" FT CHAIN 2..499 FT /note="Beta-amylase" FT /id="PRO_0000153934" FT ACT_SITE 188 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050" FT ACT_SITE 383 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 55 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 103 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 303 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 345 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 384..385 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT BINDING 423 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P10538" FT CONFLICT 238 FT /note="A -> T (in Ref. 2; BAA02286)" FT /evidence="ECO:0000305" FT CONFLICT 257..264 FT /note="YKTDMGKF -> LQDGYGQV (in Ref. 1; BAA00828)" FT /evidence="ECO:0000305" FT CONFLICT 372..374 FT /note="SGW -> RQV (in Ref. 1; BAA00828)" FT /evidence="ECO:0000305" FT CONFLICT 397 FT /note="M -> I (in Ref. 2; BAA02286)" FT /evidence="ECO:0000305" FT CONFLICT 400..401 FT /note="NV -> KL (in Ref. 1; BAA00828)" FT /evidence="ECO:0000305" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 10..12 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 16..19 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:1FA2" FT HELIX 34..46 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 72..83 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 111..119 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:1FA2" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:1FA2" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:1FA2" FT HELIX 152..166 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 168..173 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 176..181 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 213..225 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 231..234 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 248..252 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 260..288 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 294..298 FT /evidence="ECO:0007829|PDB:5WQS" FT TURN 304..307 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 312..317 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 329..337 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 351..353 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 362..375 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 391..401 FT /evidence="ECO:0007829|PDB:5WQS" FT STRAND 419..422 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 426..429 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 431..444 FT /evidence="ECO:0007829|PDB:5WQS" FT TURN 445..447 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 448..450 FT /evidence="ECO:0007829|PDB:5WQS" FT TURN 452..454 FT /evidence="ECO:0007829|PDB:1FA2" FT HELIX 456..466 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 469..473 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 474..476 FT /evidence="ECO:0007829|PDB:5WQS" FT HELIX 480..485 FT /evidence="ECO:0007829|PDB:5WQS" SQ SEQUENCE 499 AA; 56080 MW; B1F47E9D0FEA92F1 CRC64; MAPIPGVMPI GNYVSLYVML PLGVVNADNV FPDKEKVEDE LKQVKAGGCD GVMVDVWWGI IEAKGPKQYD WSAYRELFQL VKKCGLKIQA IMSFHQCGGN VGDAVFIPIP QWILQIGDKN PDIFYTNRAG NRNQEYLSLG VDNQRLFQGR TALEMYRDFM ESFRDNMADF LKAGDIVDIE VGCGAAGELR YPSYPETQGW VFPGIGEFQC YDKYMVADWK EAVKQAGNAD WEMPGKGAGT YNDTPDKTEF FRPNGTYKTD MGKFFLTWYS NKLIIHGDQV LEEANKVFVG LRVNIAAKVS GIHWWYNHVS HAAELTAGFY NVAGRDGYRP IARMLARHHA TLNFTCLEMR DSEQPAEAKS APQELVQQVL SSGWKEYIDV AGENALPRYD ATAYNQMLLN VRPNGVNLNG PPKLKMSGLT YLRLSDDLLQ TDNFELFKKF VKKMHADLDP SPNAISPAVL ERSNSAITID ELMEATKGSR PFPWYDVTDM PVDGSNPFD //