CAZyme Information: MGYG000002365_01531

Basic Information

• Species: Bifidobacterium globosum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium globosum
• CAZyme ID: MGYG000002365_01531
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1618	MGYG000002365_1|CGC23	170537.74	5.1063

Genome Property

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

• Gene Location: Start: 1755888; End: 1760744 Strand: -

Full Sequence      

MAPLSEEHGASPVSDKRPSRRGFLKKTIAGFAAAATLAGGMVVGSTTAVAADHVGPTTSY
DRTLGNAQFEAARKQYGLAREMSYGSILHAWMWSFNTIKQKMPEIAAAGYTSIQTAPISE
IKGPVNGMQFDENWYYVYQPTGTKIGNKVVGTEDDLKAMTAEAHKYGIRVIVDGVINHFS
SDWNAIDSDWRSENNFHQAWGICDKQENTSHNGDRIDYSNRWKVTQCHLLGLWDLNTQNQ
TVADRMHDYLTRAVEDGVDGFRYDAAKHIELPDEFDTHSPYFDTILSNGAQYQYGEVLQG
DSGLNAAAYPALFDKYSSNGGGNTGSKYGGAVRAAINSGSMNAQSLRNLQGDGVRDNQLV
TWVESHDNYANKEVDTEIGKVGVSTRISADKIRKGWAIIASRAGGAPLFFNRPVGSGGTN
NNQFAERTTLGMAGDDEWKHPEVTWVNKFRNAMEGSPENMQNCQGDNSCLMIERGIGDGS
PDNNGVVVVNSGGDKDLNGISTTLDDGQYKDQVNGGQITVSGGKITSGRAPGGKVAVFWN
NKGGTTIDAETISAAPINTTFTGSGIEVTVRAQNATNLKWTTSDGKSGTFVSGDKITVGA
NAEVGDVITLTLTGKGTGATGKDLKVEYTYEKIERSQQQLAKYYSTNTAGQKKKKTISVD
GSASDWDSSMLIAQGTANDDPRVYRPNSMYEMPIDLYALYGTYDDDNLYLMWEMTNVQDV
VDPGDDFPLNRPVHTEKGPAAWIALDTGRSDNRVGKNANLQTGGTIWDSRISWEQNVNNV
IGLALKKGENGPWMYSGDETGLNANAIYGPGAAPAVGTQKTKMQYAAGTGLLSNEVWGLD
NAWGAQNGRVPGDVKNDNGNWVNFKSKGHNPGAQDSICELAIPLEELGITAADVEKTGVG
VQIVATYGLSGMDSLPYDLAANDNADLPDTQSQENNSYEKSDDDSYSAPLARIGAAGGVI
ETIPVESVTINEGSSMSIDLGTSRTAKLSATVAPSNASNKKVTWSSSNEQIATVDSKGNV
KANKAGTVTITAKAGDKTSTITITVTGELNLPTTTTVYYPAAKFGASSTYLHYRVNKGGT
AGTWTTVPGVKMEAACDGYVKYTVDNPDQDEVEFVFNNGSGQWDNNGEANYKGTGESLLV
KNGQLTVDNPPCTVTVPVSSVSIAGGDFELKEGASKQLSATVAPANATDRAVSWKSSDTS
VATVDASGKVTAVQAGTATVTATAGGQSSSVSVTVIKDEPVIVPVSSVSISGTGVSGNRA
SIKVGAGLALSATVLPVDATDRAVSWKSTNSAVATVDADGNVRGVAAGNAGITATAGGKS
ASIIVTVQPNGTVATAITINGDGVANGKLTMDMGTNKQLKVALTPANAEQGVVYWSSSND
AIATVNGNGKVTAIKNGKVAITATMGDLHSSILLTVNGVAPGRFKDVPVSHQFYGDIEWL
AQSGITTGDGNGNFLPSGKVTRAQMAAFLYRHAVALGDASASSFQPSLADYRKFKDVGAD
HLFAKEILWAASVGITSGDGAGGFSPEAVCTRAQMTAFLRRFVALQGDASASSFQPSAAD
YRKFKDVGADHLFASDILWAASVGITSGDGAGGFSPSSSVLREQMAAFLHRTHNHLNK

Enzyme Prediction     

No EC number prediction in MGYG000002365_01531.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM74	643	952	6.2e-107	0.9967948717948718
GH13	93	373	2.9e-96	0.9924812030075187
CBM25	1054	1132	1.5e-24	0.9487179487179487

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	7.44e-145	84	460	1	352	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.
cd11317	AmyAc_bac_euk_AmyA	8.16e-33	85	368	2	238	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.
cd11320	AmyAc_AmyMalt_CGTase_like	1.76e-25	98	367	49	313	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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.
COG0366	AmyA	9.33e-23	92	367	25	315	Glycosidase [Carbohydrate transport and metabolism].
cd11319	AmyAc_euk_AmyA	3.01e-21	94	376	41	308	Alpha amylase catalytic domain found in 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASW24745.1	0.0	1	1618	1	1613
ATU19782.1	0.0	1	1611	1	1608
ATO39557.1	0.0	41	1611	1	1485
ASW24731.1	0.0	1	1618	1	1393
ATO39556.1	0.0	1	1611	1	1392

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	8.32e-98	85	526	6	408	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	8.15e-97	79	526	3	411	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DC0_A	1.01e-96	85	526	6	408	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1B2Y_A	1.53e-14	75	368	1	301	StructureOf Human Pancreatic Alpha-amylase In Complex With The Carbohydrate Inhibitor Acarbose [Homo sapiens]
1XGZ_A	2.03e-14	86	368	12	301	ChainA, Alpha-amylase, pancreatic [Homo sapiens],1XH0_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],1XH1_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],1XH2_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],3BAK_A Chain A, Pancreatic alpha-amylase [Homo sapiens],3BAX_A Chain A, Pancreatic alpha-amylase [Homo sapiens],3BAY_A Chain A, Pancreatic alpha-amylase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	1.58e-99	67	662	31	586	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.90e-63	85	553	54	475	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P30269	4.84e-56	85	542	148	622	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
O77021	4.20e-17	83	273	29	217	Alpha-amylase-related protein OS=Drosophila dossoui OX=60716 GN=Amyrel PE=3 SV=2
Q9GQV3	7.40e-17	86	273	32	217	Alpha-amylase-related protein OS=Drosophila jambulina OX=111875 GN=Amyrel PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as TAT

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000001	0.000003	0.000000	0.994507	0.005467	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002365_01531.