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CAZyme Information: MGYG000001416_00754

You are here: Home > Sequence: MGYG000001416_00754

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Cellulomonas massiliensis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas massiliensis
CAZyme ID MGYG000001416_00754
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
691 MGYG000001416_1|CGC12 71744.53 6.01
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001416 3245988 Isolate not provided not provided
Gene Location Start: 814020;  End: 816095  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1 3.2.1.41

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 71 335 1.1e-101 0.9962825278810409
CBM20 599 680 1.8e-31 0.9111111111111111
CBM25 491 564 7.5e-25 0.9615384615384616

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11317 AmyAc_bac_euk_AmyA 3.32e-157 46 391 1 329
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
cd11315 AmyAc_bac1_AmyA 6.97e-58 46 393 1 347
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
cd05808 CBM20_alpha_amylase 5.40e-42 599 691 2 95
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
pfam00686 CBM_20 5.85e-35 599 688 2 95
Starch binding domain.
cd05467 CBM20 2.51e-33 600 690 2 96
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ARK04721.1 0.0 45 691 73 727
QDP76525.1 0.0 45 691 73 727
QUB99931.1 0.0 45 691 73 726
QDW64271.1 0.0 36 691 47 701
QJW35995.1 0.0 45 691 82 734

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1G94_A 1.46e-113 50 472 6 442
CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1JD9_A 1.71e-113 50 472 6 442
ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1AQH_A 1.71e-113 50 472 6 442
ALPHA-AMYLASEFROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis],1AQM_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS [Pseudoalteromonas haloplanktis],1B0I_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis]
1JD7_A 2.41e-113 50 472 6 442
ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1KXH_A 8.10e-113 50 472 6 442
ChainA, alpha-amylase [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P22998 2.35e-176 31 691 17 568
Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml PE=2 SV=1
P09794 9.04e-170 32 691 21 565
Alpha-amylase OS=Streptomyces limosus OX=1947 GN=aml PE=3 SV=1
P30270 1.02e-168 32 691 21 565
Alpha-amylase OS=Streptomyces griseus OX=1911 GN=amy PE=3 SV=1
P27350 1.55e-147 31 477 13 459
Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
P29750 5.88e-130 32 691 25 605
Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.034005 0.964450 0.000344 0.000573 0.000320 0.000296

TMHMM  Annotations      download full data without filtering help

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