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Protein

Glucan 1,4-alpha-maltohexaosidase

Gene
N/A
Organism
Bacillus sp. (strain 707)
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 linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity
  • Na+By similarityNote: Binds 1 sodium ion per subunit.By similarity

Pathwayi: starch degradation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi139Calcium 1By similarity1
Metal bindingi196Calcium 2By similarity1
Metal bindingi196SodiumBy similarity1
Metal bindingi219Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi221Calcium 2By similarity1
Metal bindingi221SodiumBy similarity1
Metal bindingi232Calcium 1By similarity1
Metal bindingi232SodiumBy similarity1
Metal bindingi238Calcium 1By similarity1
Metal bindingi238SodiumBy similarity1
Metal bindingi240Calcium 2By similarity1
Metal bindingi242Calcium 2By similarity1
Active sitei269NucleophileBy similarity1
Metal bindingi273Calcium 1; via carbonyl oxygenBy similarity1
Active sitei299Proton donorBy similarity1
Sitei366Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.98. 691.
UniPathwayiUPA00153.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,4-alpha-maltohexaosidase (EC:3.2.1.98By similarity)
Alternative name(s):
Exo-maltohexaohydrolase
G6-amylase
Maltohexaose-producing amylase
OrganismiBacillus sp. (strain 707)
Taxonomic identifieri1416 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 331 PublicationAdd BLAST33
ChainiPRO_000000142134 – 518Glucan 1,4-alpha-maltohexaosidaseAdd BLAST485

Structurei

Secondary structure

1518
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 44Combined sources3
Beta strandi52 – 54Combined sources3
Helixi56 – 70Combined sources15
Beta strandi74 – 77Combined sources4
Beta strandi81 – 85Combined sources5
Beta strandi92 – 95Combined sources4
Beta strandi107 – 109Combined sources3
Helixi115 – 127Combined sources13
Beta strandi131 – 136Combined sources6
Beta strandi139 – 141Combined sources3
Beta strandi145 – 156Combined sources12
Beta strandi159 – 163Combined sources5
Beta strandi168 – 176Combined sources9
Turni179 – 183Combined sources5
Helixi192 – 194Combined sources3
Beta strandi195 – 199Combined sources5
Turni202 – 204Combined sources3
Beta strandi210 – 213Combined sources4
Beta strandi222 – 224Combined sources3
Beta strandi235 – 239Combined sources5
Helixi244 – 261Combined sources18
Beta strandi264 – 268Combined sources5
Helixi271 – 273Combined sources3
Helixi276 – 290Combined sources15
Beta strandi295 – 298Combined sources4
Helixi305 – 314Combined sources10
Turni315 – 317Combined sources3
Beta strandi319 – 322Combined sources4
Helixi324 – 334Combined sources11
Turni335 – 338Combined sources4
Helixi342 – 344Combined sources3
Turni345 – 348Combined sources4
Helixi350 – 353Combined sources4
Helixi355 – 357Combined sources3
Beta strandi358 – 360Combined sources3
Turni365 – 367Combined sources3
Beta strandi368 – 371Combined sources4
Turni379 – 381Combined sources3
Helixi382 – 390Combined sources9
Beta strandi391 – 400Combined sources10
Helixi401 – 405Combined sources5
Helixi408 – 410Combined sources3
Helixi416 – 428Combined sources13
Beta strandi434 – 437Combined sources4
Beta strandi440 – 448Combined sources9
Beta strandi459 – 467Combined sources9
Beta strandi469 – 474Combined sources6
Helixi477 – 479Combined sources3
Beta strandi483 – 486Combined sources4
Beta strandi489 – 491Combined sources3
Beta strandi493 – 496Combined sources4
Beta strandi501 – 507Combined sources7
Beta strandi511 – 516Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WP6X-ray2.10A34-518[»]
1WPCX-ray1.90A34-518[»]
2D3LX-ray2.30A34-518[»]
2D3NX-ray1.90A34-518[»]
2GJPX-ray1.90A34-516[»]
2GJRX-ray2.10A34-516[»]
ProteinModelPortaliP19571.
SMRiP19571.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19571.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19571-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMRTGKKGF LSILLAFLLV ITSIPFTLVD VEAHHNGTNG TMMQYFEWYL
60 70 80 90 100
PNDGNHWNRL NSDASNLKSK GITAVWIPPA WKGASQNDVG YGAYDLYDLG
110 120 130 140 150
EFNQKGTVRT KYGTRSQLQA AVTSLKNNGI QVYGDVVMNH KGGADATEMV
160 170 180 190 200
RAVEVNPNNR NQEVTGEYTI EAWTRFDFPG RGNTHSSFKW RWYHFDGVDW
210 220 230 240 250
DQSRRLNNRI YKFRGHGKAW DWEVDTENGN YDYLMYADID MDHPEVVNEL
260 270 280 290 300
RNWGVWYTNT LGLDGFRIDA VKHIKYSFTR DWINHVRSAT GKNMFAVAEF
310 320 330 340 350
WKNDLGAIEN YLQKTNWNHS VFDVPLHYNL YNASKSGGNY DMRNIFNGTV
360 370 380 390 400
VQRHPSHAVT FVDNHDSQPE EALESFVEEW FKPLAYALTL TREQGYPSVF
410 420 430 440 450
YGDYYGIPTH GVPAMRSKID PILEARQKYA YGKQNDYLDH HNIIGWTREG
460 470 480 490 500
NTAHPNSGLA TIMSDGAGGS KWMFVGRNKA GQVWSDITGN RTGTVTINAD
510
GWGNFSVNGG SVSIWVNK
Length:518
Mass (Da):59,009
Last modified:February 1, 1991 - v1
Checksum:i3A961E21612682C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18862 Genomic DNA. Translation: AAA22231.1.
PIRiA27705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18862 Genomic DNA. Translation: AAA22231.1.
PIRiA27705.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WP6X-ray2.10A34-518[»]
1WPCX-ray1.90A34-518[»]
2D3LX-ray2.30A34-518[»]
2D3NX-ray1.90A34-518[»]
2GJPX-ray1.90A34-516[»]
2GJRX-ray2.10A34-516[»]
ProteinModelPortaliP19571.
SMRiP19571.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00153.
BRENDAi3.2.1.98. 691.

Miscellaneous databases

EvolutionaryTraceiP19571.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMT6_BACS7
AccessioniPrimary (citable) accession number: P19571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 102 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, Direct protein sequencing

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.