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O87172

- MALQ_THETH

UniProt

O87172 - MALQ_THETH

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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-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5005004-alpha-glucanotransferasePRO_0000170132Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi262724.TTC0897.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi13 – 153Combined sources
Beta strandi19 – 224Combined sources
Helixi27 – 3812Combined sources
Beta strandi43 – 453Combined sources
Beta strandi60 – 623Combined sources
Helixi69 – 713Combined sources
Helixi75 – 795Combined sources
Beta strandi92 – 943Combined sources
Helixi97 – 11822Combined sources
Helixi121 – 15030Combined sources
Turni151 – 1533Combined sources
Helixi156 – 1583Combined sources
Helixi161 – 1644Combined sources
Helixi168 – 17710Combined sources
Helixi179 – 20527Combined sources
Beta strandi209 – 2179Combined sources
Beta strandi220 – 2223Combined sources
Helixi223 – 2275Combined sources
Helixi229 – 2313Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi256 – 2616Combined sources
Helixi265 – 2706Combined sources
Turni271 – 2733Combined sources
Helixi274 – 28613Combined sources
Beta strandi288 – 2936Combined sources
Helixi295 – 2984Combined sources
Beta strandi300 – 3056Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi315 – 3184Combined sources
Helixi321 – 33212Combined sources
Beta strandi337 – 3393Combined sources
Helixi347 – 3559Combined sources
Beta strandi360 – 3634Combined sources
Helixi364 – 3663Combined sources
Beta strandi367 – 3704Combined sources
Helixi378 – 3803Combined sources
Beta strandi387 – 3915Combined sources
Helixi399 – 4057Combined sources
Helixi408 – 42013Combined sources
Helixi428 – 4303Combined sources
Helixi431 – 44111Combined sources
Beta strandi445 – 4506Combined sources
Helixi451 – 4544Combined sources
Helixi459 – 4613Combined sources
Beta strandi469 – 4713Combined sources
Turni479 – 4813Combined sources
Helixi484 – 49613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO87172.

Family & Domainsi

Sequence similaritiesi

Belongs to the disproportionating enzyme family.Curated

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

        10         20         30         40         50
MELPRAFGLL LHPTSLPGPY GVGVLGREAR DFLRFLKEAG GRYWQVLPLG
60 70 80 90 100
PTGYGDSPYQ SFSAFAGNPY LIDLRPLAER GYVRLEDPGF PQGRVDYGLL
110 120 130 140 150
YAWKWPALKE AFRGFKEKAS PEEREAFAAF REREAWWLED YALFMALKGA
160 170 180 190 200
HGGLPWNRWP LPLRKREEKA LREAKSALAE EVAFHAFTQW LFFRQWGALK
210 220 230 240 250
AEAEALGIRI IGDMPIFVAE DSAEVWAHPE WFHLDEEGRP TVVAGVPPDY
260 270 280 290 300
FSETGQRWGN PLYRWDVLER EGFSFWIRRL EKALELFHLV RIDHFRGFEA
310 320 330 340 350
YWEIPASCPT AVEGRWVKAP GEKLFQKIQE VFGEVPVLAE DLGVITPEVE
360 370 380 390 400
ALRDRFGLPG MKVLQFAFDD GMENPFLPHN YPAHGRVVVY TGTHDNDTTL
410 420 430 440 450
GWYRTATPHE KAFMARYLAD WGITFREEEE VPWALMHLGM KSVARLAVYP
460 470 480 490 500
VQDVLALGSE ARMNYPGRPS GNWAWRLLPG ELSPEHGARL RAMAEATERL
Length:500
Mass (Da):57,222
Last modified:November 1, 1998 - v1
Checksum:i6E7175A38E0A5D61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016244 Genomic DNA. Translation: BAA33728.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016244 Genomic DNA. Translation: BAA33728.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 80 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