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P19531

- AMYM_GEOSE

UniProt

P19531 - AMYM_GEOSE

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Protein

Maltogenic alpha-amylase

Gene

amyM

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

        10         20         30         40         50
MKKKTLSLFV GLMLLIGLLF SGSLPYNPNA AEASSSASVK GDVIYQIIID
60 70 80 90 100
RFYDGDTTNN NPAKSYGLYD PTKSKWKMYW GGDLEGVRQK LPYLKQLGVT
110 120 130 140 150
TIWLSPVLDN LDTLAGTDNT GYHGYWTRDF KQIEEHFGNW TTFDTLVNDA
160 170 180 190 200
HQNGIKVIVD FVPNHSTPFK ANDSTFAEGG ALYNNGTYMG NYFDDATKGY
210 220 230 240 250
FHHNGDISNW DDRYEAQWKN FTDPAGFSLA DLSQENGTIA QYLTDAAVQL
260 270 280 290 300
VAHGADGLRI DAVKHFNSGF SKSLADKLYQ KKDIFLVGEW YGDDPGTANH
310 320 330 340 350
LEKVRYANNS GVNVLDFDLN TVIRNVFGTF TQTMYDLNNM VNQTGNEYKY
360 370 380 390 400
KENLITFIDN HDMSRFLSVN SNKANLHQAL AFILTSRGTP SIYYGTEQYM
410 420 430 440 450
AGGNDPYNRG MMPAFDTTTT AFKEVSTLAG LRRNNAAIQY GTTTQRWINN
460 470 480 490 500
DVYIYERKFF NDVVLVAINR NTQSSYSISG LQTALPNGSY ADYLSGLLGG
510 520 530 540 550
NGISVSNGSV ASFTLAPGAV SVWQYSTSAS APQIGSVAPN MGIPGNVVTI
560 570 580 590 600
DGKGFGTTQG TVTFGGVTAT VKSWTSNRIE VYVPNMAAGL TDVKVTAGGV
610 620 630 640 650
SSNLYSYNIL SGTQTSVVFT VKSAPPTNLG DKIYLTGNIP ELGNWSTDTS
660 670 680 690 700
GAVNNAQGPL LAPNYPDWFY VFSVPAGKTI QFKFFIKRAD GTIQWENGSN
710
HVATTPTGAT GNITVTWQN
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