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Protein

Oligo-1,6-glucosidase

Gene

malL

Organism
Bacillus cereus
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi21CalciumBy similarity1
Metal bindingi23CalciumBy similarity1
Metal bindingi25CalciumBy similarity1
Metal bindingi29CalciumBy similarity1
Active sitei199NucleophileBy similarity1
Active sitei255Proton donorBy similarity1
Sitei329Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000543131 – 558Oligo-1,6-glucosidaseAdd BLAST558

Interactioni

Protein-protein interaction databases

STRINGi226900.BC4015.

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Beta strandi11 – 14Combined sources4
Helixi16 – 18Combined sources3
Beta strandi22 – 27Combined sources6
Helixi30 – 34Combined sources5
Helixi37 – 43Combined sources7
Beta strandi47 – 50Combined sources4
Turni59 – 62Combined sources4
Beta strandi66 – 71Combined sources6
Helixi73 – 75Combined sources3
Helixi78 – 90Combined sources13
Beta strandi94 – 99Combined sources6
Helixi109 – 114Combined sources6
Helixi123 – 125Combined sources3
Beta strandi132 – 135Combined sources4
Beta strandi145 – 152Combined sources8
Turni153 – 156Combined sources4
Beta strandi157 – 160Combined sources4
Helixi175 – 190Combined sources16
Beta strandi195 – 198Combined sources4
Helixi201 – 203Combined sources3
Helixi224 – 226Combined sources3
Turni227 – 229Combined sources3
Helixi233 – 243Combined sources11
Helixi245 – 247Combined sources3
Beta strandi251 – 255Combined sources5
Helixi261 – 268Combined sources8
Helixi270 – 272Combined sources3
Helixi282 – 284Combined sources3
Beta strandi292 – 296Combined sources5
Helixi301 – 314Combined sources14
Beta strandi316 – 319Combined sources4
Helixi333 – 336Combined sources4
Helixi344 – 356Combined sources13
Beta strandi358 – 365Combined sources8
Helixi368 – 370Combined sources3
Helixi380 – 382Combined sources3
Helixi386 – 397Combined sources12
Helixi403 – 413Combined sources11
Helixi415 – 418Combined sources4
Turni428 – 431Combined sources4
Helixi443 – 446Combined sources4
Helixi450 – 455Combined sources6
Helixi460 – 473Combined sources14
Helixi475 – 479Combined sources5
Beta strandi481 – 486Combined sources6
Beta strandi490 – 499Combined sources10
Beta strandi502 – 509Combined sources8
Beta strandi511 – 513Combined sources3
Beta strandi515 – 518Combined sources4
Beta strandi528 – 535Combined sources8
Beta strandi543 – 547Combined sources5
Beta strandi552 – 557Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP21332.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiENOG4105CG3. Bacteria.
COG0366. LUCA.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16657. Malt_amylase_C. 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.
RefSeqiWP_000415199.1. NZ_LOQC01000169.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53507 Genomic DNA. Translation: CAA37583.1.
PIRiS13579.
RefSeqiWP_000415199.1. NZ_LOQC01000169.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi226900.BC4015.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CG3. Bacteria.
COG0366. LUCA.

Enzyme and pathway databases

SABIO-RKP21332.

Miscellaneous databases

EvolutionaryTraceiP21332.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16657. Malt_amylase_C. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 100 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

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.