SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O87172

- MALQ_THETH

UniProt

O87172 - MALQ_THETH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
4-alpha-glucanotransferase
Gene
malQ
Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.

GO - Molecular functioni

  1. 4-alpha-glucanotransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Names & Taxonomyi

Protein namesi
Recommended name:
4-alpha-glucanotransferase (EC:2.4.1.25)
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name:
D-enzyme
Gene namesi
Name:malQ
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5005004-alpha-glucanotransferase
PRO_0000170132Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi262724.TTC0897.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106
Helixi13 – 153
Beta strandi19 – 224
Helixi27 – 3812
Beta strandi43 – 453
Beta strandi60 – 623
Helixi69 – 713
Helixi75 – 795
Beta strandi92 – 943
Helixi97 – 11822
Helixi121 – 15030
Turni151 – 1533
Helixi156 – 1583
Helixi161 – 1644
Helixi168 – 17710
Helixi179 – 20527
Beta strandi209 – 2179
Beta strandi220 – 2223
Helixi223 – 2275
Helixi229 – 2313
Beta strandi240 – 2434
Beta strandi256 – 2616
Helixi265 – 2706
Turni271 – 2733
Helixi274 – 28613
Beta strandi288 – 2936
Helixi295 – 2984
Beta strandi300 – 3056
Beta strandi309 – 3113
Beta strandi315 – 3184
Helixi321 – 33212
Beta strandi337 – 3393
Helixi347 – 3559
Beta strandi360 – 3634
Helixi364 – 3663
Beta strandi367 – 3704
Helixi378 – 3803
Beta strandi387 – 3915
Helixi399 – 4057
Helixi408 – 42013
Helixi428 – 4303
Helixi431 – 44111
Beta strandi445 – 4506
Helixi451 – 4544
Helixi459 – 4613
Beta strandi469 – 4713
Turni479 – 4813
Helixi484 – 49613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWYX-ray2.00A1-500[»]
1ESWX-ray1.90A1-500[»]
1FP8X-ray2.30A1-500[»]
1FP9X-ray3.10A1-500[»]
2OWCX-ray2.05A1-500[»]
2OWWX-ray2.20A1-500[»]
2OWXX-ray2.50A1-500[»]
ProteinModelPortaliO87172.
SMRiO87172. Positions 1-500.

Miscellaneous databases

EvolutionaryTraceiO87172.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR00217. malQ. 1 hit.

Sequencei

Sequence statusi: Complete.

O87172-1 [UniParc]FASTAAdd to Basket

« Hide

MELPRAFGLL LHPTSLPGPY GVGVLGREAR DFLRFLKEAG GRYWQVLPLG    50
PTGYGDSPYQ SFSAFAGNPY LIDLRPLAER GYVRLEDPGF PQGRVDYGLL 100
YAWKWPALKE AFRGFKEKAS PEEREAFAAF REREAWWLED YALFMALKGA 150
HGGLPWNRWP LPLRKREEKA LREAKSALAE EVAFHAFTQW LFFRQWGALK 200
AEAEALGIRI IGDMPIFVAE DSAEVWAHPE WFHLDEEGRP TVVAGVPPDY 250
FSETGQRWGN PLYRWDVLER EGFSFWIRRL EKALELFHLV RIDHFRGFEA 300
YWEIPASCPT AVEGRWVKAP GEKLFQKIQE VFGEVPVLAE DLGVITPEVE 350
ALRDRFGLPG MKVLQFAFDD GMENPFLPHN YPAHGRVVVY TGTHDNDTTL 400
GWYRTATPHE KAFMARYLAD WGITFREEEE VPWALMHLGM KSVARLAVYP 450
VQDVLALGSE ARMNYPGRPS GNWAWRLLPG ELSPEHGARL RAMAEATERL 500
Length:500
Mass (Da):57,222
Last modified:November 1, 1998 - v1
Checksum:i6E7175A38E0A5D61
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB016244 Genomic DNA. Translation: BAA33728.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB016244 Genomic DNA. Translation: BAA33728.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CWY X-ray 2.00 A 1-500 [» ]
1ESW X-ray 1.90 A 1-500 [» ]
1FP8 X-ray 2.30 A 1-500 [» ]
1FP9 X-ray 3.10 A 1-500 [» ]
2OWC X-ray 2.05 A 1-500 [» ]
2OWW X-ray 2.20 A 1-500 [» ]
2OWX X-ray 2.50 A 1-500 [» ]
ProteinModelPortali O87172.
SMRi O87172. Positions 1-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262724.TTC0897.

Protein family/group databases

CAZyi GH77. Glycoside Hydrolase Family 77.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O87172.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02446. Glyco_hydro_77. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR00217. malQ. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning, expression and characterization of amylomaltase from Thermus aquaticus ATCC33923."
    Terada Y., Fujii K., Takaha T., Okada S.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33923 / DSM 674 / AT-62.
  2. "Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans."
    Przylas I., Tomoo K., Terada Y., Takaha T., Fujii K., Saenger W., Strater N.
    J. Mol. Biol. 296:873-886(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiMALQ_THETH
AccessioniPrimary (citable) accession number: O87172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 77 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi