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Protein

Malto-oligosyltrehalose trehalohydrolase

Gene

treZ

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan.

Pathwayi: trehalose biosynthesis

This protein is involved in the pathway trehalose biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway trehalose biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei275NucleophileCurated1
Active sitei308Proton donorCurated1
Binding sitei376Substrate1 Publication1
Sitei400Transition state stabilizerCurated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi3.2.1.141. 1856.
UniPathwayiUPA00299.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Malto-oligosyltrehalose trehalohydrolase (EC:3.2.1.141)
Short name:
MTHase
Alternative name(s):
4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase
Maltooligosyl trehalose trehalohydrolase
Gene namesi
Name:treZ
Ordered Locus Names:DR_0464
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003937501 – 600Malto-oligosyltrehalose trehalohydrolaseAdd BLAST600

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi243230.DR_0464.

Structurei

Secondary structure

1600
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 23Combined sources3
Beta strandi25 – 29Combined sources5
Helixi31 – 33Combined sources3
Beta strandi36 – 41Combined sources6
Beta strandi46 – 52Combined sources7
Beta strandi55 – 58Combined sources4
Beta strandi60 – 63Combined sources4
Beta strandi66 – 72Combined sources7
Beta strandi78 – 83Combined sources6
Beta strandi86 – 88Combined sources3
Helixi109 – 111Combined sources3
Helixi124 – 126Combined sources3
Beta strandi129 – 132Combined sources4
Helixi134 – 137Combined sources4
Beta strandi138 – 140Combined sources3
Helixi143 – 148Combined sources6
Helixi150 – 156Combined sources7
Beta strandi160 – 163Combined sources4
Beta strandi170 – 172Combined sources3
Beta strandi181 – 185Combined sources5
Helixi187 – 189Combined sources3
Helixi192 – 204Combined sources13
Beta strandi208 – 213Combined sources6
Beta strandi220 – 222Combined sources3
Helixi225 – 228Combined sources4
Helixi230 – 232Combined sources3
Beta strandi233 – 238Combined sources6
Beta strandi240 – 245Combined sources6
Helixi250 – 267Combined sources18
Beta strandi270 – 274Combined sources5
Helixi277 – 279Combined sources3
Beta strandi284 – 286Combined sources3
Helixi288 – 297Combined sources10
Beta strandi304 – 308Combined sources5
Helixi315 – 318Combined sources4
Beta strandi323 – 326Combined sources4
Helixi329 – 339Combined sources11
Helixi344 – 348Combined sources5
Helixi353 – 362Combined sources10
Beta strandi363 – 365Combined sources3
Beta strandi367 – 371Combined sources5
Beta strandi378 – 381Combined sources4
Helixi389 – 391Combined sources3
Beta strandi392 – 396Combined sources5
Helixi399 – 403Combined sources5
Helixi411 – 413Combined sources3
Helixi419 – 430Combined sources12
Beta strandi431 – 437Combined sources7
Helixi440 – 442Combined sources3
Helixi456 – 469Combined sources14
Turni470 – 472Combined sources3
Helixi474 – 477Combined sources4
Helixi487 – 491Combined sources5
Helixi498 – 501Combined sources4
Helixi503 – 521Combined sources19
Turni523 – 526Combined sources4
Helixi530 – 532Combined sources3
Beta strandi533 – 538Combined sources6
Beta strandi541 – 548Combined sources8
Beta strandi551 – 558Combined sources8
Beta strandi560 – 562Combined sources3
Helixi566 – 568Combined sources3
Beta strandi578 – 582Combined sources5
Beta strandi587 – 591Combined sources5
Beta strandi596 – 600Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BHUX-ray1.10A1-600[»]
2BHYX-ray1.50A1-600[»]
2BHZX-ray1.20A1-600[»]
2BXYX-ray1.75A1-600[»]
2BXZX-ray1.75A1-600[»]
2BY0X-ray1.55A1-600[»]
2BY1X-ray1.55A1-600[»]
2BY2X-ray1.50A1-600[»]
2BY3X-ray1.50A1-600[»]
ProteinModelPortaliQ9RX51.
SMRiQ9RX51.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RX51.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni273 – 278Substrate bindingBy similarity6
Regioni328 – 332Substrate binding1 Publication5
Regioni399 – 404Substrate bindingBy similarity6

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0296. LUCA.
HOGENOMiHOG000155669.
InParanoidiQ9RX51.
KOiK01236.
OMAiFTPMLFM.
OrthoDBiPOG091H0CAL.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR022567. DUF3459.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR012768. Trehalose_TreZ.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF11941. DUF3459. 1 hit.
[Graphical view]
PIRSFiPIRSF006337. Trehalose_TreZ. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR02402. trehalose_TreZ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9RX51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQTQPVTPT PPASFQTQHD PRTRLGATPL PGGAGTRFRL WTSTARTVAV
60 70 80 90 100
RVNGTEHVMT SLGGGIYELE LPVGPGARYL FVLDGVPTPD PYARFLPDGV
110 120 130 140 150
HGEAEVVDFG TFDWTDADWH GIKLADCVFY EVHVGTFTPE GTYRAAAEKL
160 170 180 190 200
PYLKELGVTA IQVMPLAAFD GQRGWGYDGA AFYAPYAPYG RPEDLMALVD
210 220 230 240 250
AAHRLGLGVF LDVVYNHFGP SGNYLSSYAP SYFTDRFSSA WGMGLDYAEP
260 270 280 290 300
HMRRYVTGNA RMWLRDYHFD GLRLDATPYM TDDSETHILT ELAQEIHELG
310 320 330 340 350
GTHLLLAEDH RNLPDLVTVN HLDGIWTDDF HHETRVTLTG EQEGYYAGYR
360 370 380 390 400
GGAEALAYTI RRGWRYEGQF WAVKGEEHER GHPSDALEAP NFVYCIQNHD
410 420 430 440 450
QIGNRPLGER LHQSDGVTLH EYRGAAALLL PMTPLLFQGQ EWAASTPFQF
460 470 480 490 500
FSDHAGELGQ AVSEGRKKEF GGFSGFSGED VPDPQAEQTF LNSKLNWAER
510 520 530 540 550
EGGEHARTLR LYRDLLRLRR EDPVLHNRQR ENLTTGHDGD VLWVRTVTGA
560 570 580 590 600
GERVLLWNLG QDTRAVAEVK LPFTVPRRLL LHTEGREDLT LGAGEAVLVG
Length:600
Mass (Da):66,910
Last modified:May 1, 2000 - v1
Checksum:i594091EC093F8A44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10042.1.
PIRiH75516.
RefSeqiNP_294187.1. NC_001263.1.
WP_010887109.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF10042; AAF10042; DR_0464.
GeneIDi1798275.
KEGGidra:DR_0464.
PATRICi21628450. VBIDeiRad64572_0641.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10042.1.
PIRiH75516.
RefSeqiNP_294187.1. NC_001263.1.
WP_010887109.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BHUX-ray1.10A1-600[»]
2BHYX-ray1.50A1-600[»]
2BHZX-ray1.20A1-600[»]
2BXYX-ray1.75A1-600[»]
2BXZX-ray1.75A1-600[»]
2BY0X-ray1.55A1-600[»]
2BY1X-ray1.55A1-600[»]
2BY2X-ray1.50A1-600[»]
2BY3X-ray1.50A1-600[»]
ProteinModelPortaliQ9RX51.
SMRiQ9RX51.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0464.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF10042; AAF10042; DR_0464.
GeneIDi1798275.
KEGGidra:DR_0464.
PATRICi21628450. VBIDeiRad64572_0641.

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0296. LUCA.
HOGENOMiHOG000155669.
InParanoidiQ9RX51.
KOiK01236.
OMAiFTPMLFM.
OrthoDBiPOG091H0CAL.

Enzyme and pathway databases

UniPathwayiUPA00299.
BRENDAi3.2.1.141. 1856.

Miscellaneous databases

EvolutionaryTraceiQ9RX51.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR022567. DUF3459.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR012768. Trehalose_TreZ.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF11941. DUF3459. 1 hit.
[Graphical view]
PIRSFiPIRSF006337. Trehalose_TreZ. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR02402. trehalose_TreZ. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTREZ_DEIRA
AccessioniPrimary (citable) accession number: Q9RX51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 111 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, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.