CAZyme Information: MGYG000002365_00993

Basic Information

• Species: Bifidobacterium globosum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium globosum
• CAZyme ID: MGYG000002365_00993
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
546	MGYG000002365_1|CGC14	59116.53	4.9854

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002365	2036949	Isolate	Kenya	Africa

• Gene Location: Start: 1116766; End: 1118406 Strand: -

Full Sequence      

MTTRTPHTAPSILRGPVGAVRRTVVRACAACAGMALVLAPLAACGHADTGSTALPRKTDV
EVIAFQQPWNSIARECTQTYGPAGVAYVEISPPQESIRGTQWWTSYQPVSYRLDSKLGTE
KELAHMIEECSAAGVGIIADVVLNQTTGAGEDKELTGVAGTRYNPGTGSYPGFTGNEDQY
PEGVNSHDFHDYNNGASISNYRDQDEVQQGRLSGMWDFDSSSAKVRDLQSDYLARLYRLG
VRGFRMDAVKHIDGEDVKALKQEMAKKIEVPEQDIYWIQEVIGNAGEAKGIQPSNYFDTG
TVTQFAFAGAMKSNVPGSLNALSDLRERLSDTKRNPYAIPTDKANVFVTNWDTERNGQAL
SYKDGAAFALANAFSLAYDYGTPRLISDYRFTDNDAGAPGATETSVPDVNFNEACATNDG
PWNCEQRWTPTRGMIAFHNYVHGTAVDHWQEGADAAVIAFSRTGKGFIAMNGGDEEASVE
FETSMPDGEYCNVYAVQDCSKTVRVRKGKVRTSVPARSAVALYAGATAKAHPSSPVAVDP
STPRQD

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	84	378	1.1e-87	0.9925650557620818

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11317	AmyAc_bac_euk_AmyA	3.64e-128	59	441	2	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	4.21e-49	61	445	2	349	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.
smart00642	Aamy	2.34e-19	69	150	18	99	Alpha-amylase domain.
PRK09441	PRK09441	9.18e-14	116	464	76	415	cytoplasmic alpha-amylase; Reviewed
cd00551	AmyAc_family	1.38e-13	84	383	38	249	Alpha amylase catalytic domain family. 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; and 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 this 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIZ16360.1	0.0	20	546	1	527
ASW23987.1	0.0	1	546	1	545
ATO39952.1	0.0	34	546	1	513
ATU20665.1	2.40e-261	21	544	7	531
ATU20663.1	1.38e-232	19	543	9	536

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JD7_A	5.60e-68	65	493	9	404	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1G94_A	1.35e-67	65	493	9	404	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]
1AQH_A	1.54e-67	65	493	9	404	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]
1JD9_A	2.15e-67	65	493	9	404	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1KXH_A	7.27e-67	65	493	9	404	ChainA, alpha-amylase [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P22998	2.77e-88	21	527	3	457	Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml PE=2 SV=1
P27350	7.96e-85	22	527	4	458	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
P08486	2.17e-82	55	527	33	448	Alpha-amylase OS=Streptomyces hygroscopicus OX=1912 PE=3 SV=1
P09794	1.52e-81	38	526	10	456	Alpha-amylase OS=Streptomyces limosus OX=1947 GN=aml PE=3 SV=1
P30270	4.19e-81	38	526	10	456	Alpha-amylase OS=Streptomyces griseus OX=1911 GN=amy PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.019086	0.305281	0.657052	0.009281	0.008338	0.000951

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002365_00993.