ID AMYM_GEOSE Reviewed; 719 AA. AC P19531; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 2. DT 03-MAY-2023, entry version 135. DE RecName: Full=Maltogenic alpha-amylase; DE EC=3.2.1.133; DE AltName: Full=Glucan 1,4-alpha-maltohydrolase; DE Flags: Precursor; GN Name=amyM; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-45. RC STRAIN=C599; RA Diderichsen B., Christiansen L.; RT "Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus."; RL FEMS Microbiol. Lett. 56:53-60(1988). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 34-719 IN COMPLEX WITH RP OLIGOSACCHARIDE AND CALCIUM, COFACTOR, AND SEQUENCE REVISION. RX PubMed=10387084; DOI=10.1021/bi990256l; RA Dauter Z., Dauter M., Brzozowski A.M., Christensen S., Borchert T.V., RA Beier L., Wilson K.S., Davies G.J.; RT "X-ray structure of Novamyl, the five-domain ''maltogenic'' alpha-amylase RT from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7-A RT resolution."; RL Biochemistry 38:8385-8392(1999). CC -!- FUNCTION: Converts starch into maltose. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkages in CC polysaccharides so as to remove successive alpha-maltose residues CC from the non-reducing ends of the chains.; EC=3.2.1.133; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:10387084}; CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:10387084}; CC -!- SUBUNIT: Monomer. CC -!- BIOTECHNOLOGY: Used in the food industry to prevent bread from staling. CC Sold under the name Novamyl by Novozymes. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 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; M36539; AAA22233.1; -; Genomic_DNA. DR PIR; S28784; S28784. DR PDB; 1QHO; X-ray; 1.70 A; A=34-719. DR PDB; 1QHP; X-ray; 1.70 A; A=34-719. DR PDBsum; 1QHO; -. DR PDBsum; 1QHP; -. DR AlphaFoldDB; P19531; -. DR SMR; P19531; -. DR DrugBank; DB03971; Acarbose Derived Hexasaccharide. DR DrugBank; DB03323; Maltose. DR CAZy; CBM20; Carbohydrate-Binding Module Family 20. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; ag:AAA22233; -. DR BRENDA; 3.2.1.133; 623. DR EvolutionaryTrace; P19531; -. DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro. DR GO; GO:0043897; F:glucan 1,4-alpha-maltohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:2001070; F:starch binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR CDD; cd11320; AmyAc_AmyMalt_CGTase_like; 1. DR CDD; cd05820; CBM20_novamyl; 1. DR CDD; cd00604; IPT_CGTD; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR031319; A-amylase_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR013784; Carb-bd-like_fold. DR InterPro; IPR034849; CBM20_novamyl. DR InterPro; IPR002044; CBM_fam20. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_dom. DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR Pfam; PF00686; CBM_20; 1. DR Pfam; PF01833; TIG; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. DR SMART; SM01065; CBM_2; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR SUPFAM; SSF49452; Starch-binding domain-like; 1. DR PROSITE; PS51166; CBM20; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing; KW Glycosidase; Hydrolase; Metal-binding; Signal. FT SIGNAL 1..33 FT /evidence="ECO:0000269|Ref.1" FT CHAIN 34..719 FT /note="Maltogenic alpha-amylase" FT /id="PRO_0000001422" FT DOMAIN 532..608 FT /note="IPT/TIG" FT DOMAIN 609..719 FT /note="CBM20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594" FT ACT_SITE 261 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P13507" FT ACT_SITE 289 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P13507" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 56 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 59 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 60 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 81 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 83 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 109 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 110 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 112 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 126 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 134 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 164 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 231 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 264..265 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 265 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:10387084, FT ECO:0007744|PDB:1QHO" FT BINDING 292 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 362 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 409 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT SITE 362 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT CONFLICT 109 FT /note="D -> N (in Ref. 1; AAA22233)" FT /evidence="ECO:0000305" FT CONFLICT 254..256 FT /note="Missing (in Ref. 1; AAA22233)" FT /evidence="ECO:0000305" FT CONFLICT 371 FT /note="S -> SK (in Ref. 1; AAA22233)" FT /evidence="ECO:0000305" FT CONFLICT 379..391 FT /note="ALAFILTSRGTPS -> RLLSFSLRGVRPP (in Ref. 1)" FT /evidence="ECO:0000305" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 84..89 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 91..97 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:1QHP" FT STRAND 126..133 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 135..137 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 140..152 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 165..170 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 177..180 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 196..198 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 227..232 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 237..252 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 257..260 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 268..281 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 300..309 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 334..347 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 351..353 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 366..369 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 373..384 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 387..393 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 405..408 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 420..434 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 436..440 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 442..448 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 450..459 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 462..469 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 476..478 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 487..490 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 493..498 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 503..506 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 513..515 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 520..525 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 533..542 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 547..553 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 561..564 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 571..574 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 576..582 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 589..597 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 605..609 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 611..623 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 632..639 FT /evidence="ECO:0007829|PDB:1QHO" FT HELIX 640..642 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 643..645 FT /evidence="ECO:0007829|PDB:1QHO" FT TURN 663..666 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 667..675 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 679..687 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 693..695 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 701..704 FT /evidence="ECO:0007829|PDB:1QHO" FT STRAND 707..716 FT /evidence="ECO:0007829|PDB:1QHO" SQ SEQUENCE 719 AA; 78676 MW; B40B61AD964F7D89 CRC64; MKKKTLSLFV GLMLLIGLLF SGSLPYNPNA AEASSSASVK GDVIYQIIID RFYDGDTTNN NPAKSYGLYD PTKSKWKMYW GGDLEGVRQK LPYLKQLGVT TIWLSPVLDN LDTLAGTDNT GYHGYWTRDF KQIEEHFGNW TTFDTLVNDA HQNGIKVIVD FVPNHSTPFK ANDSTFAEGG ALYNNGTYMG NYFDDATKGY FHHNGDISNW DDRYEAQWKN FTDPAGFSLA DLSQENGTIA QYLTDAAVQL VAHGADGLRI DAVKHFNSGF SKSLADKLYQ KKDIFLVGEW YGDDPGTANH LEKVRYANNS GVNVLDFDLN TVIRNVFGTF TQTMYDLNNM VNQTGNEYKY KENLITFIDN HDMSRFLSVN SNKANLHQAL AFILTSRGTP SIYYGTEQYM AGGNDPYNRG MMPAFDTTTT AFKEVSTLAG LRRNNAAIQY GTTTQRWINN DVYIYERKFF NDVVLVAINR NTQSSYSISG LQTALPNGSY ADYLSGLLGG NGISVSNGSV ASFTLAPGAV SVWQYSTSAS APQIGSVAPN MGIPGNVVTI DGKGFGTTQG TVTFGGVTAT VKSWTSNRIE VYVPNMAAGL TDVKVTAGGV SSNLYSYNIL SGTQTSVVFT VKSAPPTNLG DKIYLTGNIP ELGNWSTDTS GAVNNAQGPL LAPNYPDWFY VFSVPAGKTI QFKFFIKRAD GTIQWENGSN HVATTPTGAT GNITVTWQN //