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P21332

- O16G_BACCE

UniProt

P21332 - O16G_BACCE

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Protein

Oligo-1,6-glucosidase

Gene

malL

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei199 – 1991Nucleophile
Active sitei255 – 2551Proton donor
Sitei329 – 3291Transition state stabilizerBy similarity

GO - Molecular functioni

  1. cation binding Source: InterPro
  2. oligo-1,6-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-3340-MONOMER.
SABIO-RKP21332.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Oligo-1,6-glucosidase (EC:3.2.1.10)
Alternative name(s):
Dextrin 6-alpha-D-glucanohydrolase
Oligosaccharide alpha-1,6-glucosidase
Sucrase-isomaltase
Short name:
Isomaltase
Gene namesi
Name:malL
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Oligo-1,6-glucosidasePRO_0000054313Add
BLAST

Structurei

Secondary structure

1
558
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Beta strandi11 – 144Combined sources
Helixi16 – 183Combined sources
Beta strandi22 – 276Combined sources
Helixi30 – 345Combined sources
Helixi37 – 437Combined sources
Beta strandi47 – 504Combined sources
Turni59 – 624Combined sources
Beta strandi66 – 716Combined sources
Helixi73 – 753Combined sources
Helixi78 – 9013Combined sources
Beta strandi94 – 996Combined sources
Helixi109 – 1146Combined sources
Helixi123 – 1253Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi145 – 1528Combined sources
Turni153 – 1564Combined sources
Beta strandi157 – 1604Combined sources
Helixi175 – 19016Combined sources
Beta strandi195 – 1984Combined sources
Helixi201 – 2033Combined sources
Helixi224 – 2263Combined sources
Turni227 – 2293Combined sources
Helixi233 – 24311Combined sources
Helixi245 – 2473Combined sources
Beta strandi251 – 2555Combined sources
Helixi261 – 2688Combined sources
Helixi270 – 2723Combined sources
Helixi282 – 2843Combined sources
Beta strandi292 – 2965Combined sources
Helixi301 – 31414Combined sources
Beta strandi316 – 3194Combined sources
Helixi333 – 3364Combined sources
Helixi344 – 35613Combined sources
Beta strandi358 – 3658Combined sources
Helixi368 – 3703Combined sources
Helixi380 – 3823Combined sources
Helixi386 – 39712Combined sources
Helixi403 – 41311Combined sources
Helixi415 – 4184Combined sources
Turni428 – 4314Combined sources
Helixi443 – 4464Combined sources
Helixi450 – 4556Combined sources
Helixi460 – 47314Combined sources
Helixi475 – 4795Combined sources
Beta strandi481 – 4866Combined sources
Beta strandi490 – 49910Combined sources
Beta strandi502 – 5098Combined sources
Beta strandi511 – 5133Combined sources
Beta strandi515 – 5184Combined sources
Beta strandi528 – 5358Combined sources
Beta strandi543 – 5475Combined sources
Beta strandi552 – 5576Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UOKX-ray2.00A1-558[»]
ProteinModelPortaliP21332.
SMRiP21332. Positions 1-558.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21332.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. 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.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

P21332-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEKQWWKESV VYQIYPRSFM DSNGDGIGDL RGIISKLDYL KELGIDVIWL
60 70 80 90 100
SPVYESPNDD NGYDISDYCK IMNEFGTMED WDELLHEMHE RNMKLMMDLV
110 120 130 140 150
VNHTSDEHNW FIESRKSKDN KYRDYYIWRP GKEGKEPNNW GAAFSGSAWQ
160 170 180 190 200
YDEMTDEYYL HLFSKKQPDL NWDNEKVRQD VYEMMKFWLE KGIDGFRMDV
210 220 230 240 250
INFISKEEGL PTVETEEEGY VSGHKHFMNG PNIHKYLHEM NEEVLSHYDI
260 270 280 290 300
MTVGEMPGVT TEEAKLYTGE ERKELQMVFQ FEHMDLDSGE GGKWDVKPCS
310 320 330 340 350
LLTLKENLTK WQKALEHTGW NSLYWNNHDQ PRVVSRFGND GMYRIESAKM
360 370 380 390 400
LATVLHMMKG TPYIYQGEEI GMTNVRFESI DEYRDIETLN MYKEKVMERG
410 420 430 440 450
EDIEKVMQSI YIKGRDNART PMQWDDQNHA GFTTGEPWIT VNPNYKEINV
460 470 480 490 500
KQAIQNKDSI FYYYKKLIEL RKNNEIVVYG SYDLILENNP SIFAYVRTYG
510 520 530 540 550
VEKLLVIANF TAEECIFELP EDISYSEVEL LIHNYDVENG PIENITLRPY

EAMVFKLK
Length:558
Mass (Da):66,013
Last modified:May 1, 1991 - v1
Checksum:i502336D7A77C7182
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53507 Genomic DNA. Translation: CAA37583.1.
PIRiS13579.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53507 Genomic DNA. Translation: CAA37583.1 .
PIRi S13579.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UOK X-ray 2.00 A 1-558 [» ]
ProteinModelPortali P21332.
SMRi P21332. Positions 1-558.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-3340-MONOMER.
SABIO-RK P21332.

Miscellaneous databases

EvolutionaryTracei P21332.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProi 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.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
[Graphical view ]
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene."
    Watanabe K., Kitamura K., Iha H., Suzuki Y.
    Eur. J. Biochem. 192:609-620(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
    Strain: ATCC 7064 / NRS 201.
  2. "Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0-A resolution X-ray analysis."
    Kizaki H., Hata Y., Watanabe K., Katsube Y., Suzuki Y.
    J. Biochem. 113:646-649(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    Strain: ATCC 7064 / NRS 201.
  3. "The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0-A resolution: structural characterization of proline-substitution sites for protein thermostabilization."
    Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y.
    J. Mol. Biol. 269:142-153(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    Strain: ATCC 7064 / NRS 201.

Entry informationi

Entry nameiO16G_BACCE
AccessioniPrimary (citable) accession number: P21332
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 26, 2014
This is version 89 of the entry and version 1 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