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P36924

- AMYB_BACCE

UniProt

P36924 - AMYB_BACCE

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Protein

Beta-amylase

Gene

spoII

Organism
Bacillus cereus
Status
Reviewed - 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+Note: Binds 1 Ca(2+) ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791Substrate
Metal bindingi86 – 861Calcium
Metal bindingi90 – 901Calcium
Metal bindingi91 – 911Calcium
Binding sitei119 – 1191Substrate
Binding sitei127 – 1271Substrate
Metal bindingi171 – 1711Calcium
Metal bindingi174 – 1741Calcium
Active sitei202 – 2021Proton donor
Binding sitei317 – 3171Substrate
Binding sitei322 – 3221Substrate
Binding sitei360 – 3601Substrate
Active sitei397 – 3971Proton acceptor
Binding sitei427 – 4271Substrate

GO - Molecular functioni

  1. beta-amylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. starch binding Source: InterPro

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Keywords - Ligandi

Calcium, Metal-binding

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1941Y → E: Reduces activity by 60%. 1 Publication
Mutagenesisi194 – 1941Y → F: Reduces activity by 64%. 1 Publication
Mutagenesisi194 – 1941Y → H: Reduces activity by 97%. 1 Publication
Mutagenesisi194 – 1941Y → Q: Reduces activity by 80%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Add
BLAST
Chaini31 – 546516Beta-amylasePRO_0000001453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi121 ↔ 1291 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1
546
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 343Combined sources
Beta strandi42 – 465Combined sources
Helixi52 – 543Combined sources
Helixi58 – 7013Combined sources
Beta strandi73 – 819Combined sources
Helixi82 – 854Combined sources
Helixi96 – 10712Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi121 – 1244Combined sources
Helixi135 – 1406Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi146 – 1494Combined sources
Helixi165 – 18218Combined sources
Helixi184 – 1896Combined sources
Beta strandi193 – 1953Combined sources
Helixi199 – 2013Combined sources
Beta strandi202 – 2043Combined sources
Turni210 – 2134Combined sources
Helixi227 – 24115Combined sources
Helixi244 – 2518Combined sources
Helixi258 – 2603Combined sources
Helixi267 – 2726Combined sources
Helixi274 – 2763Combined sources
Helixi278 – 30629Combined sources
Turni307 – 3104Combined sources
Beta strandi314 – 3185Combined sources
Turni323 – 3264Combined sources
Beta strandi328 – 3303Combined sources
Turni331 – 3344Combined sources
Helixi335 – 3384Combined sources
Helixi343 – 35311Combined sources
Beta strandi356 – 3605Combined sources
Turni370 – 3723Combined sources
Helixi376 – 39015Combined sources
Beta strandi394 – 3974Combined sources
Helixi405 – 41713Combined sources
Beta strandi421 – 4266Combined sources
Helixi428 – 4325Combined sources
Helixi435 – 44410Combined sources
Beta strandi449 – 45810Combined sources
Beta strandi466 – 4738Combined sources
Helixi474 – 4763Combined sources
Turni477 – 4793Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi489 – 4913Combined sources
Turni492 – 4954Combined sources
Beta strandi496 – 5049Combined sources
Beta strandi509 – 5168Combined sources
Beta strandi522 – 5254Combined sources
Beta strandi530 – 5345Combined sources
Beta strandi541 – 5455Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 31-546.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36924.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini444 – 546103CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni398 – 3992Substrate binding

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
Entry Method Resolution (Å) Chain Positions PDBsum
1B90 X-ray 2.50 A 31-546 [» ]
1B9Z X-ray 2.10 A 31-546 [» ]
1CQY X-ray 1.95 A 448-546 [» ]
1ITC X-ray 2.10 A 31-546 [» ]
1J0Y X-ray 2.10 A/B/C/D 31-546 [» ]
1J0Z X-ray 2.20 A/B/C/D 31-546 [» ]
1J10 X-ray 2.10 A/B/C/D 31-546 [» ]
1J11 X-ray 2.00 A/B/C/D 31-546 [» ]
1J12 X-ray 2.10 A/B/C/D 31-546 [» ]
1J18 X-ray 2.00 A 31-546 [» ]
1VEM X-ray 1.85 A 31-546 [» ]
1VEN X-ray 2.02 A 31-546 [» ]
1VEO X-ray 2.12 A 31-546 [» ]
1VEP X-ray 2.06 A 31-546 [» ]
5BCA X-ray 2.20 A/B/C/D 31-546 [» ]
ProteinModelPortali P36924.
SMRi P36924. Positions 31-546.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P36924.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR002044. 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 ]
Pfami PF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view ]
PRINTSi PR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTi SM01065. CBM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme."
    Nanmori T., Nagai M., Shimizu Y., Shinke R., Mikami B.
    Appl. Environ. Microbiol. 59:623-627(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: BQ10-S1.
  2. Nanmori T., Mikami B., Shimizu Y.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose."
    Mikami B., Adachi M., Kage T., Sarikaya E., Nanmori T., Shinke R., Utsumi S.
    Biochemistry 38:7050-7061(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  4. "Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents."
    Oyama T., Miyake H., Kusunoki M., Nitta Y.
    J. Biochem. 133:467-474(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-546 IN COMPLEXES WITH SUBSTRATE ANALOGS.
  5. "Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type."
    Hirata A., Adachi M., Utsumi S., Mikami B.
    Biochemistry 43:12523-12531(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-546 IN COMPLEX WITH CALCIUM IONS AND MALTOSE, MUTAGENESIS OF TYR-194, DISULFIDE BOND.

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 26, 2014
This is version 94 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