AMYM_GEOSE
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-AUG-2022, entry version 132.
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; Firmicutes; 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}.
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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; cd05820; CBM20_novamyl; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
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 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; SSF49452; SSF49452; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 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
