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Protein

4-alpha-glucanotransferase

Gene

malQ

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: 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

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi2.4.1.25. 2305.

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001701321 – 5004-alpha-glucanotransferaseAdd BLAST500

Interactioni

Protein-protein interaction databases

STRINGi262724.TTC0897.

Structurei

Secondary structure

1500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi13 – 15Combined sources3
Beta strandi19 – 22Combined sources4
Helixi27 – 38Combined sources12
Beta strandi43 – 45Combined sources3
Beta strandi60 – 62Combined sources3
Helixi69 – 71Combined sources3
Helixi75 – 79Combined sources5
Beta strandi92 – 94Combined sources3
Helixi97 – 118Combined sources22
Helixi121 – 150Combined sources30
Turni151 – 153Combined sources3
Helixi156 – 158Combined sources3
Helixi161 – 164Combined sources4
Helixi168 – 177Combined sources10
Helixi179 – 205Combined sources27
Beta strandi209 – 217Combined sources9
Beta strandi220 – 222Combined sources3
Helixi223 – 227Combined sources5
Helixi229 – 231Combined sources3
Beta strandi240 – 243Combined sources4
Beta strandi256 – 261Combined sources6
Helixi265 – 270Combined sources6
Turni271 – 273Combined sources3
Helixi274 – 286Combined sources13
Beta strandi288 – 293Combined sources6
Helixi295 – 298Combined sources4
Beta strandi300 – 305Combined sources6
Beta strandi309 – 311Combined sources3
Beta strandi315 – 318Combined sources4
Helixi321 – 332Combined sources12
Beta strandi337 – 339Combined sources3
Helixi347 – 355Combined sources9
Beta strandi360 – 363Combined sources4
Helixi364 – 366Combined sources3
Beta strandi367 – 370Combined sources4
Helixi378 – 380Combined sources3
Beta strandi387 – 391Combined sources5
Helixi399 – 405Combined sources7
Helixi408 – 420Combined sources13
Helixi428 – 430Combined sources3
Helixi431 – 441Combined sources11
Beta strandi445 – 450Combined sources6
Helixi451 – 454Combined sources4
Helixi459 – 461Combined sources3
Beta strandi469 – 471Combined sources3
Turni479 – 481Combined sources3
Helixi484 – 496Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO87172.

Family & Domainsi

Sequence similaritiesi

Belongs to the disproportionating enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4107SBB. Bacteria.
COG1640. LUCA.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC0897.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107SBB. Bacteria.
COG1640. LUCA.

Enzyme and pathway databases

BRENDAi2.4.1.25. 2305.

Miscellaneous databases

EvolutionaryTraceiO87172.

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.
ProtoNetiSearch...

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 2, 2016
This is version 89 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

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.