Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-amylase

Gene

spoII

Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei79Substrate2 Publications1
Metal bindingi86Calcium1 Publication1
Metal bindingi90Calcium1 Publication1
Metal bindingi91Calcium1 Publication1
Binding sitei119Substrate2 Publications1
Binding sitei127Substrate2 Publications1
Metal bindingi171Calcium1 Publication1
Metal bindingi174Calcium1 Publication1
Active sitei202Proton donorPROSITE-ProRule annotation2 Publications1
Binding sitei317Substrate2 Publications1
Binding sitei322Substrate2 Publications1
Binding sitei360Substrate2 Publications1
Active sitei397Proton acceptor2 Publications1
Binding sitei427Substrate2 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.2. 648.

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-amylase (EC:3.2.1.2)
Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Gene namesi
Name:spoII
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi194Y → E: Reduces activity by 60%. 1 Publication1
Mutagenesisi194Y → F: Reduces activity by 64%. 1 Publication1
Mutagenesisi194Y → H: Reduces activity by 97%. 1 Publication1
Mutagenesisi194Y → Q: Reduces activity by 80%. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Add BLAST30
ChainiPRO_000000145331 – 546Beta-amylaseAdd BLAST516

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi121 ↔ 1291 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1546
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 34Combined sources3
Beta strandi42 – 46Combined sources5
Helixi52 – 54Combined sources3
Helixi58 – 70Combined sources13
Beta strandi73 – 81Combined sources9
Helixi82 – 85Combined sources4
Helixi96 – 107Combined sources12
Beta strandi111 – 117Combined sources7
Beta strandi121 – 124Combined sources4
Helixi135 – 140Combined sources6
Beta strandi142 – 144Combined sources3
Beta strandi146 – 149Combined sources4
Helixi165 – 182Combined sources18
Helixi184 – 189Combined sources6
Beta strandi193 – 195Combined sources3
Helixi199 – 201Combined sources3
Beta strandi202 – 204Combined sources3
Turni210 – 213Combined sources4
Helixi227 – 241Combined sources15
Helixi244 – 251Combined sources8
Helixi258 – 260Combined sources3
Helixi267 – 272Combined sources6
Helixi274 – 276Combined sources3
Helixi278 – 306Combined sources29
Turni307 – 310Combined sources4
Beta strandi314 – 318Combined sources5
Turni323 – 326Combined sources4
Beta strandi328 – 330Combined sources3
Turni331 – 334Combined sources4
Helixi335 – 338Combined sources4
Helixi343 – 353Combined sources11
Beta strandi356 – 360Combined sources5
Turni370 – 372Combined sources3
Helixi376 – 390Combined sources15
Beta strandi394 – 397Combined sources4
Helixi405 – 417Combined sources13
Beta strandi421 – 426Combined sources6
Helixi428 – 432Combined sources5
Helixi435 – 444Combined sources10
Beta strandi449 – 458Combined sources10
Beta strandi466 – 473Combined sources8
Helixi474 – 476Combined sources3
Turni477 – 479Combined sources3
Beta strandi481 – 484Combined sources4
Beta strandi489 – 491Combined sources3
Turni492 – 495Combined sources4
Beta strandi496 – 504Combined sources9
Beta strandi509 – 516Combined sources8
Beta strandi522 – 525Combined sources4
Beta strandi530 – 534Combined sources5
Beta strandi541 – 545Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B90X-ray2.50A31-546[»]
1B9ZX-ray2.10A31-546[»]
1CQYX-ray1.95A448-546[»]
1ITCX-ray2.10A31-546[»]
1J0YX-ray2.10A/B/C/D31-546[»]
1J0ZX-ray2.20A/B/C/D31-546[»]
1J10X-ray2.10A/B/C/D31-546[»]
1J11X-ray2.00A/B/C/D31-546[»]
1J12X-ray2.10A/B/C/D31-546[»]
1J18X-ray2.00A31-546[»]
1VEMX-ray1.85A31-546[»]
1VENX-ray2.02A31-546[»]
1VEOX-ray2.12A31-546[»]
1VEPX-ray2.06A31-546[»]
5BCAX-ray2.20A/B/C/D31-546[»]
ProteinModelPortaliP36924.
SMRiP36924.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36924.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini444 – 546CBM20PROSITE-ProRule annotationAdd BLAST103

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni398 – 399Substrate binding1 Publication2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR002044. CBM_fam20.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36924-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK
60 70 80 90 100
KIPEVTNWET FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR
110 120 130 140 150
FAQSVKNAGM KMIPIISTHQ CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS
160 170 180 190 200
ETGTVNKETL NPLASDVIRK EYGELYTAFA AAMKPYKDVI AKIYLSGGPA
210 220 230 240 250
GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK YGSLNEVNKA
260 270 280 290 300
WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE
310 320 330 340 350
LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF
360 370 380 390 400
KSAKLDVTFT CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL
410 420 430 440 450
SIGNEEEYKR VAEMAFNYNF AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV
460 470 480 490 500
MQTIVVKNVP TTIGDTVYIT GNRAELGSWD TKQYPIQLYY DSHSNDWRGN
510 520 530 540
VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT SHTSSW
Length:546
Mass (Da):61,629
Last modified:July 11, 2002 - v2
Checksum:iA8F7CFC96ED6979B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024519 Genomic DNA. Translation: BAA75890.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024519 Genomic DNA. Translation: BAA75890.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B90X-ray2.50A31-546[»]
1B9ZX-ray2.10A31-546[»]
1CQYX-ray1.95A448-546[»]
1ITCX-ray2.10A31-546[»]
1J0YX-ray2.10A/B/C/D31-546[»]
1J0ZX-ray2.20A/B/C/D31-546[»]
1J10X-ray2.10A/B/C/D31-546[»]
1J11X-ray2.00A/B/C/D31-546[»]
1J12X-ray2.10A/B/C/D31-546[»]
1J18X-ray2.00A31-546[»]
1VEMX-ray1.85A31-546[»]
1VENX-ray2.02A31-546[»]
1VEOX-ray2.12A31-546[»]
1VEPX-ray2.06A31-546[»]
5BCAX-ray2.20A/B/C/D31-546[»]
ProteinModelPortaliP36924.
SMRiP36924.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.2. 648.

Miscellaneous databases

EvolutionaryTraceiP36924.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR002044. CBM_fam20.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMYB_BACCE
AccessioniPrimary (citable) accession number: P36924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 11, 2002
Last modified: November 2, 2016
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.