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P19531

- AMYM_GEOSE

UniProt

P19531 - AMYM_GEOSE

Protein

Maltogenic alpha-amylase

Gene

amyM

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (15 Aug 2003)
      Previous versions | rss
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    Functioni

    Converts starch into maltose.

    Catalytic activityi

    Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains.

    Cofactori

    Binds 3 calcium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi54 – 541Calcium 1
    Metal bindingi56 – 561Calcium 1; via carbonyl oxygen
    Metal bindingi59 – 591Calcium 1
    Metal bindingi60 – 601Calcium 1
    Metal bindingi81 – 811Calcium 1; via carbonyl oxygen
    Metal bindingi83 – 831Calcium 1
    Metal bindingi109 – 1091Calcium 2
    Metal bindingi110 – 1101Calcium 2; via carbonyl oxygen
    Metal bindingi112 – 1121Calcium 2
    Metal bindingi134 – 1341Calcium 2
    Metal bindingi135 – 1351Calcium 2
    Metal bindingi164 – 1641Calcium 3
    Metal bindingi217 – 2171Calcium 3; via carbonyl oxygen
    Metal bindingi231 – 2311Calcium 3
    Active sitei261 – 2611NucleophileBy similarity
    Metal bindingi265 – 2651Calcium 3; via carbonyl oxygen
    Active sitei289 – 2891Proton donorBy similarity
    Sitei362 – 3621Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. glucan 1,4-alpha-maltohydrolase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. starch binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.2.1.133. 623.

    Protein family/group databases

    CAZyiCBM20. Carbohydrate-Binding Module Family 20.
    GH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maltogenic alpha-amylase (EC:3.2.1.133)
    Alternative name(s):
    Glucan 1,4-alpha-maltohydrolase
    Gene namesi
    Name:amyM
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Pathology & Biotechi

    Biotechnological usei

    Used in the food industry to prevent bread from staling. Sold under the name Novamyl by Novozymes.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 33331 PublicationAdd
    BLAST
    Chaini34 – 719686Maltogenic alpha-amylasePRO_0000001422Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    719
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 474
    Helixi49 – 513
    Helixi57 – 593
    Helixi63 – 653
    Helixi84 – 896
    Helixi91 – 977
    Beta strandi101 – 1044
    Beta strandi108 – 1103
    Helixi121 – 1233
    Beta strandi126 – 1338
    Turni135 – 1373
    Helixi140 – 15213
    Beta strandi156 – 1616
    Beta strandi165 – 1706
    Turni177 – 1804
    Beta strandi182 – 1843
    Beta strandi187 – 1904
    Beta strandi192 – 1943
    Turni196 – 1983
    Helixi213 – 2186
    Turni224 – 2263
    Beta strandi227 – 2326
    Helixi237 – 25216
    Beta strandi257 – 2604
    Helixi263 – 2653
    Helixi268 – 28114
    Beta strandi285 – 2884
    Helixi300 – 30910
    Beta strandi313 – 3153
    Helixi317 – 32711
    Helixi334 – 34714
    Helixi351 – 3533
    Helixi366 – 3694
    Helixi373 – 38412
    Beta strandi387 – 3937
    Helixi396 – 3983
    Turni405 – 4084
    Helixi420 – 43415
    Helixi436 – 4405
    Beta strandi442 – 4487
    Beta strandi450 – 45910
    Beta strandi462 – 4698
    Beta strandi476 – 4783
    Beta strandi487 – 4904
    Turni493 – 4986
    Beta strandi503 – 5064
    Beta strandi513 – 5153
    Beta strandi520 – 5256
    Beta strandi533 – 54210
    Beta strandi547 – 5537
    Beta strandi561 – 5644
    Beta strandi571 – 5744
    Beta strandi576 – 5827
    Beta strandi589 – 5979
    Beta strandi605 – 6095
    Beta strandi611 – 62313
    Beta strandi632 – 6398
    Helixi640 – 6423
    Turni643 – 6453
    Turni663 – 6664
    Beta strandi667 – 6759
    Beta strandi679 – 6879
    Beta strandi693 – 6953
    Beta strandi701 – 7044
    Beta strandi707 – 71610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QHOX-ray1.70A34-719[»]
    1QHPX-ray1.70A34-719[»]
    ProteinModelPortaliP19531.
    SMRiP19531. Positions 34-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19531.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini532 – 60877IPT/TIGAdd
    BLAST
    Domaini609 – 719111CBM20PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated
    Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation
    Contains 1 IPT/TIG domain.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    IPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    PF00686. CBM_20. 1 hit.
    PF01833. TIG. 1 hit.
    [Graphical view]
    PRINTSiPR00110. ALPHAAMYLASE.
    SMARTiSM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    SM01065. CBM_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49452. SSF49452. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS51166. CBM20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P19531-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKKTLSLFV GLMLLIGLLF SGSLPYNPNA AEASSSASVK GDVIYQIIID    50
    RFYDGDTTNN NPAKSYGLYD PTKSKWKMYW GGDLEGVRQK LPYLKQLGVT 100
    TIWLSPVLDN LDTLAGTDNT GYHGYWTRDF KQIEEHFGNW TTFDTLVNDA 150
    HQNGIKVIVD FVPNHSTPFK ANDSTFAEGG ALYNNGTYMG NYFDDATKGY 200
    FHHNGDISNW DDRYEAQWKN FTDPAGFSLA DLSQENGTIA QYLTDAAVQL 250
    VAHGADGLRI DAVKHFNSGF SKSLADKLYQ KKDIFLVGEW YGDDPGTANH 300
    LEKVRYANNS GVNVLDFDLN TVIRNVFGTF TQTMYDLNNM VNQTGNEYKY 350
    KENLITFIDN HDMSRFLSVN SNKANLHQAL AFILTSRGTP SIYYGTEQYM 400
    AGGNDPYNRG MMPAFDTTTT AFKEVSTLAG LRRNNAAIQY GTTTQRWINN 450
    DVYIYERKFF NDVVLVAINR NTQSSYSISG LQTALPNGSY ADYLSGLLGG 500
    NGISVSNGSV ASFTLAPGAV SVWQYSTSAS APQIGSVAPN MGIPGNVVTI 550
    DGKGFGTTQG TVTFGGVTAT VKSWTSNRIE VYVPNMAAGL TDVKVTAGGV 600
    SSNLYSYNIL SGTQTSVVFT VKSAPPTNLG DKIYLTGNIP ELGNWSTDTS 650
    GAVNNAQGPL LAPNYPDWFY VFSVPAGKTI QFKFFIKRAD GTIQWENGSN 700
    HVATTPTGAT GNITVTWQN 719
    Length:719
    Mass (Da):78,676
    Last modified:August 15, 2003 - v2
    Checksum:iB40B61AD964F7D89
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091D → N in AAA22233. 1 PublicationCurated
    Sequence conflicti254 – 2563Missing in AAA22233. 1 PublicationCurated
    Sequence conflicti371 – 3711S → SK in AAA22233. 1 PublicationCurated
    Sequence conflicti379 – 39113ALAFI…RGTPS → RLLSFSLRGVRPP1 PublicationCuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36539 Genomic DNA. Translation: AAA22233.1.
    PIRiS28784.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36539 Genomic DNA. Translation: AAA22233.1 .
    PIRi S28784.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QHO X-ray 1.70 A 34-719 [» ]
    1QHP X-ray 1.70 A 34-719 [» ]
    ProteinModelPortali P19531.
    SMRi P19531. Positions 34-719.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM20. Carbohydrate-Binding Module Family 20.
    GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.2.1.133. 623.

    Miscellaneous databases

    EvolutionaryTracei P19531.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    IPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    PF00686. CBM_20. 1 hit.
    PF01833. TIG. 1 hit.
    [Graphical view ]
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    SM01065. CBM_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49452. SSF49452. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS51166. CBM20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus."
      Diderichsen B., Christiansen L.
      FEMS Microbiol. Lett. 56:53-60(1988)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-45.
      Strain: C599.
    2. "X-ray structure of Novamyl, the five-domain ''maltogenic'' alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7-A resolution."
      Dauter Z., Dauter M., Brzozowski A.M., Christensen S., Borchert T.V., Beier L., Wilson K.S., Davies G.J.
      Biochemistry 38:8385-8392(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SEQUENCE REVISION.

    Entry informationi

    Entry nameiAMYM_GEOSE
    AccessioniPrimary (citable) accession number: P19531
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: August 15, 2003
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3