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Protein

Glucan 1,6-alpha-glucosidase

Gene

dexB

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The physiological substrates may be short isomaltosaccharides.

Catalytic activityi

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-alpha-D-glucans and derived oligosaccharides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei194 – 1941NucleophileBy similarity
Active sitei236 – 2361Proton donorBy similarity
Sitei313 – 3131Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-848-MONOMER.
BRENDAi3.2.1.70. 5941.
SABIO-RKQ99040.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,6-alpha-glucosidase (EC:3.2.1.70)
Alternative name(s):
Dextran glucosidase
Exo-1,6-alpha-glucosidase
Glucodextranase
Gene namesi
Name:dexB
Ordered Locus Names:SMU_883
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002512 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Glucan 1,6-alpha-glucosidasePRO_0000054339Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU_883.

Structurei

Secondary structure

1
536
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Beta strandi11 – 144Combined sources
Helixi16 – 183Combined sources
Beta strandi22 – 276Combined sources
Helixi30 – 4314Combined sources
Beta strandi46 – 505Combined sources
Turni59 – 624Combined sources
Beta strandi66 – 716Combined sources
Turni73 – 753Combined sources
Helixi78 – 9013Combined sources
Beta strandi94 – 996Combined sources
Helixi109 – 1168Combined sources
Helixi121 – 1255Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi140 – 1478Combined sources
Turni148 – 1514Combined sources
Beta strandi152 – 1554Combined sources
Helixi170 – 18516Combined sources
Beta strandi190 – 1934Combined sources
Helixi196 – 1983Combined sources
Helixi203 – 2053Combined sources
Helixi214 – 22411Combined sources
Turni225 – 2306Combined sources
Beta strandi232 – 2365Combined sources
Helixi242 – 2498Combined sources
Helixi251 – 2533Combined sources
Beta strandi257 – 2604Combined sources
Helixi265 – 2684Combined sources
Helixi284 – 29714Combined sources
Turni300 – 3023Combined sources
Beta strandi305 – 3095Combined sources
Helixi317 – 3204Combined sources
Helixi328 – 34013Combined sources
Beta strandi342 – 3498Combined sources
Helixi352 – 3543Combined sources
Helixi364 – 3663Combined sources
Helixi370 – 38011Combined sources
Turni381 – 3833Combined sources
Helixi386 – 39611Combined sources
Helixi398 – 4014Combined sources
Beta strandi408 – 4103Combined sources
Helixi411 – 4144Combined sources
Beta strandi417 – 4204Combined sources
Helixi427 – 4304Combined sources
Helixi434 – 4396Combined sources
Helixi444 – 45714Combined sources
Helixi460 – 4634Combined sources
Beta strandi465 – 4684Combined sources
Beta strandi475 – 4828Combined sources
Beta strandi485 – 4928Combined sources
Beta strandi494 – 4963Combined sources
Beta strandi506 – 5149Combined sources
Helixi516 – 5227Combined sources
Beta strandi523 – 5253Combined sources
Beta strandi530 – 5356Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZICX-ray2.20A1-536[»]
2ZIDX-ray2.20A1-536[»]
4WLCX-ray2.40A1-536[»]
4XB3X-ray2.09A1-536[»]
ProteinModelPortaliQ99040.
SMRiQ99040. Positions 1-535.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99040.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiENOG4105CG3. Bacteria.
COG0366. LUCA.
KOiK01215.
OMAiVADNYYN.
PhylomeDBiQ99040.

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.

Q99040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKHWWHKAT VYQIYPKSFM DTNGDGIGDL KGITSKLDYL QKLGVMAIWL
60 70 80 90 100
SPVYDSPMDD NGYDIANYEA ITDIFGNMAD MDNLLTQAKM RGIKIIMDLV
110 120 130 140 150
VNHTSDEHAW FIEAREHPDS SERDYYIWCD QPNDLESIFG GSAWQYDDKS
160 170 180 190 200
DQYYLHFFSK KQPDLNWENA NLRQKIYDMM NFWIDKGIGG FRMDVIDMIG
210 220 230 240 250
KIPAQHIVSN GPKLHAYLKE MNAASFGQHD LLTVGETWGA TPEIAKQYSN
260 270 280 290 300
PVNHELSMVF QFEHIGLQHK PEAPKWDYVK ELNVPALKTI FNKWQTELEL
310 320 330 340 350
GQGWNSLFWN NHDLPRVLSI WGNTGKYREK SAKALAILLH LMRGTPYIYQ
360 370 380 390 400
GEEIGMTNYP FKDLNELDDI ESLNYAKEAF TNGKSMETIM DSIRMIGRDN
410 420 430 440 450
ARTPMQWDAS QNAGFSTADK TWLPVNPNYK DINVQAALKN SNSIFYTYQQ
460 470 480 490 500
LIQLRKENDW LVDADFELLP TADKVFAYLR KVREERYLIV VNVSDQEEVL
510 520 530
EIDVDKQETL ISNTNESAAL ANHKLQPWDA FCIKIN
Length:536
Mass (Da):62,030
Last modified:November 28, 2002 - v2
Checksum:iF3287CD6C8DBD8D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721T → A in AAA26939 (PubMed:2380687).Curated
Sequence conflicti92 – 921G → D in AAA26939 (PubMed:2380687).Curated
Sequence conflicti109 – 1091A → T in AAA26939 (PubMed:2380687).Curated
Sequence conflicti259 – 2591V → I in AAA26939 (PubMed:2380687).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77351 Genomic DNA. Translation: AAA26939.1.
AE014133 Genomic DNA. Translation: AAN58598.1.
PIRiA37231.
RefSeqiNP_721292.1. NC_004350.2.
WP_002262877.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN58598; AAN58598; SMU_883.
GeneIDi1028248.
KEGGismu:SMU_883.
PATRICi19663913. VBIStrMut61772_0789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77351 Genomic DNA. Translation: AAA26939.1.
AE014133 Genomic DNA. Translation: AAN58598.1.
PIRiA37231.
RefSeqiNP_721292.1. NC_004350.2.
WP_002262877.1. NC_004350.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZICX-ray2.20A1-536[»]
2ZIDX-ray2.20A1-536[»]
4WLCX-ray2.40A1-536[»]
4XB3X-ray2.09A1-536[»]
ProteinModelPortaliQ99040.
SMRiQ99040. Positions 1-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_883.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN58598; AAN58598; SMU_883.
GeneIDi1028248.
KEGGismu:SMU_883.
PATRICi19663913. VBIStrMut61772_0789.

Phylogenomic databases

eggNOGiENOG4105CG3. Bacteria.
COG0366. LUCA.
KOiK01215.
OMAiVADNYYN.
PhylomeDBiQ99040.

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-848-MONOMER.
BRENDAi3.2.1.70. 5941.
SABIO-RKQ99040.

Miscellaneous databases

EvolutionaryTraceiQ99040.

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 nameiDEXB_STRMU
AccessioniPrimary (citable) accession number: Q99040
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 28, 2002
Last modified: September 7, 2016
This is version 117 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, Complete proteome, Reference proteome

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.