AMYB_IPOBA
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 03-AUG-2022, entry version 124.
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 -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="http://www.worthington-biochem.com/BA/";
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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 PDBsum; 1FA2; -.
DR PDBsum; 5WQS; -.
DR PDBsum; 5WQU; -.
DR AlphaFoldDB; P10537; -.
DR PCDDB; P10537; -.
DR SASBDB; P10537; -.
DR SMR; P10537; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR PRIDE; P10537; -.
DR BRENDA; 3.2.1.2; 2773.
DR EvolutionaryTrace; P10537; -.
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 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; PTHR31352; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
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 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:5WQS"
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..172
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 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 TURN 452..454
FT /evidence="ECO:0007829|PDB:1FA2"
FT HELIX 469..473
FT /evidence="ECO:0007829|PDB:5WQS"
FT HELIX 474..476
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
