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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Calcium 1By similarity
Metal bindingi196 – 1961Calcium 2By similarity
Metal bindingi196 – 1961SodiumBy similarity
Metal bindingi219 – 2191Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi221 – 2211Calcium 2By similarity
Metal bindingi221 – 2211SodiumBy similarity
Metal bindingi232 – 2321Calcium 1By similarity
Metal bindingi232 – 2321SodiumBy similarity
Metal bindingi238 – 2381Calcium 1By similarity
Metal bindingi238 – 2381SodiumBy similarity
Metal bindingi240 – 2401Calcium 2By similarity
Metal bindingi242 – 2421Calcium 2By similarity
Active sitei269 – 2691NucleophileBy similarity
Metal bindingi273 – 2731Calcium 1; via carbonyl oxygenBy similarity
Active sitei299 – 2991Proton donorBy similarity
Sitei366 – 3661Transition state stabilizerBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 PublicationAdd
BLAST
Chaini34 – 518485Glucan 1,4-alpha-maltohexaosidasePRO_0000001421Add
BLAST

Structurei

Secondary structure

1
518
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443Combined sources
Beta strandi52 – 543Combined sources
Helixi56 – 7015Combined sources
Beta strandi74 – 774Combined sources
Beta strandi81 – 855Combined sources
Beta strandi92 – 954Combined sources
Beta strandi107 – 1093Combined sources
Helixi115 – 12713Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi145 – 15612Combined sources
Beta strandi159 – 1635Combined sources
Beta strandi168 – 1769Combined sources
Turni179 – 1835Combined sources
Helixi192 – 1943Combined sources
Beta strandi195 – 1995Combined sources
Turni202 – 2043Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi235 – 2395Combined sources
Helixi244 – 26118Combined sources
Beta strandi264 – 2685Combined sources
Helixi271 – 2733Combined sources
Helixi276 – 29015Combined sources
Beta strandi295 – 2984Combined sources
Helixi305 – 31410Combined sources
Turni315 – 3173Combined sources
Beta strandi319 – 3224Combined sources
Helixi324 – 33411Combined sources
Turni335 – 3384Combined sources
Helixi342 – 3443Combined sources
Turni345 – 3484Combined sources
Helixi350 – 3534Combined sources
Helixi355 – 3573Combined sources
Beta strandi358 – 3603Combined sources
Turni365 – 3673Combined sources
Beta strandi368 – 3714Combined sources
Turni379 – 3813Combined sources
Helixi382 – 3909Combined sources
Beta strandi391 – 40010Combined sources
Helixi401 – 4055Combined sources
Helixi408 – 4103Combined sources
Helixi416 – 42813Combined sources
Beta strandi434 – 4374Combined sources
Beta strandi440 – 4489Combined sources
Beta strandi459 – 4679Combined sources
Beta strandi469 – 4746Combined sources
Helixi477 – 4793Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi489 – 4913Combined sources
Beta strandi493 – 4964Combined sources
Beta strandi501 – 5077Combined sources
Beta strandi511 – 5166Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 38-518.
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
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. Positions 38-518.
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: May 11, 2016
This is version 100 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.