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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)DescriptionActionsGraphical viewLength
Active sitei194NucleophileBy similarity1
Active sitei236Proton donorBy similarity1
Sitei313Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000543391 – 536Glucan 1,6-alpha-glucosidaseAdd BLAST536

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU_883.

Structurei

Secondary structure

1536
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Beta strandi11 – 14Combined sources4
Helixi16 – 18Combined sources3
Beta strandi22 – 27Combined sources6
Helixi30 – 43Combined sources14
Beta strandi46 – 50Combined sources5
Turni59 – 62Combined sources4
Beta strandi66 – 71Combined sources6
Turni73 – 75Combined sources3
Helixi78 – 90Combined sources13
Beta strandi94 – 99Combined sources6
Helixi109 – 116Combined sources8
Helixi121 – 125Combined sources5
Beta strandi128 – 131Combined sources4
Beta strandi140 – 147Combined sources8
Turni148 – 151Combined sources4
Beta strandi152 – 155Combined sources4
Helixi170 – 185Combined sources16
Beta strandi190 – 193Combined sources4
Helixi196 – 198Combined sources3
Helixi203 – 205Combined sources3
Helixi214 – 224Combined sources11
Turni225 – 230Combined sources6
Beta strandi232 – 236Combined sources5
Helixi242 – 249Combined sources8
Helixi251 – 253Combined sources3
Beta strandi257 – 260Combined sources4
Helixi265 – 268Combined sources4
Helixi284 – 297Combined sources14
Turni300 – 302Combined sources3
Beta strandi305 – 309Combined sources5
Helixi317 – 320Combined sources4
Helixi328 – 340Combined sources13
Beta strandi342 – 349Combined sources8
Helixi352 – 354Combined sources3
Helixi364 – 366Combined sources3
Helixi370 – 380Combined sources11
Turni381 – 383Combined sources3
Helixi386 – 396Combined sources11
Helixi398 – 401Combined sources4
Beta strandi408 – 410Combined sources3
Helixi411 – 414Combined sources4
Beta strandi417 – 420Combined sources4
Helixi427 – 430Combined sources4
Helixi434 – 439Combined sources6
Helixi444 – 457Combined sources14
Helixi460 – 463Combined sources4
Beta strandi465 – 468Combined sources4
Beta strandi475 – 482Combined sources8
Beta strandi485 – 492Combined sources8
Beta strandi494 – 496Combined sources3
Beta strandi506 – 514Combined sources9
Helixi516 – 522Combined sources7
Beta strandi523 – 525Combined sources3
Beta strandi530 – 535Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZICX-ray2.20A1-536[»]
2ZIDX-ray2.20A1-536[»]
4WLCX-ray2.40A1-536[»]
4XB3X-ray2.09A1-536[»]
ProteinModelPortaliQ99040.
SMRiQ99040.
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)DescriptionActionsGraphical viewLength
Sequence conflicti72T → A in AAA26939 (PubMed:2380687).Curated1
Sequence conflicti92G → D in AAA26939 (PubMed:2380687).Curated1
Sequence conflicti109A → T in AAA26939 (PubMed:2380687).Curated1
Sequence conflicti259V → I in AAA26939 (PubMed:2380687).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZICX-ray2.20A1-536[»]
2ZIDX-ray2.20A1-536[»]
4WLCX-ray2.40A1-536[»]
4XB3X-ray2.09A1-536[»]
ProteinModelPortaliQ99040.
SMRiQ99040.
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

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: November 2, 2016
This is version 119 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.