CAZyme Information: MGYG000000773_01978

Basic Information

• Species: Bulleidia sp900539965
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Bulleidia; Bulleidia sp900539965
• CAZyme ID: MGYG000000773_01978
• CAZy Family: GH170
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
392	MGYG000000773_58|CGC1	45373.71	4.5144

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000773	2056602	MAG	Japan	Asia

• Gene Location: Start: 1921; End: 3099 Strand: +

Full Sequence      

MKLKSFGVSVYPDIESLEDITKYLERASKFGCEYVFSSMFSVEGTKEEVLDYFKEFIKVA
HSFNIKVVLDLNPPFLKKMGVDYDDVSLMHDIGCDVMRMDMPFGAEKDLVLVNNPYNISI
MFNASGSFADELAYFEEHGVPKEKVLLGHNFYPQPYTGLKWKNFLETNRILKQYGYPVQA
FISSRNPEATGVWDANYGLPTVESLRNLPIDTQARIIEATGDVDMVWIGNAFATEEEMES
LIEVQKDVRPIEDSPVYEMFKSFGLLRRERKEDRKIRVVLDEGITDTEQYQLFEMFPQLD
MGDSSEWIWRSRTGRMVQPDVPFRKCEKDMFEVGDVLIVNNNYQHYAGEIQIVRIPFKND
GQRNYLGHLAEGEELILDLLKNFDEVTFLKAK

Enzyme Prediction     

No EC number prediction in MGYG000000773_01978.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH170	6	248	7.3e-67	0.6714285714285714

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam19200	DUF871_N	8.20e-78	6	243	1	235	DUF871 N-terminal domain. This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
COG3589	COG3589	4.27e-68	7	392	5	360	Uncharacterized protein [Function unknown].
pfam05913	DUF871	1.13e-19	276	381	3	108	Bacterial protein of unknown function (DUF871). This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
cd00551	AmyAc_family	0.005	44	91	73	124	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.
cd11320	AmyAc_AmyMalt_CGTase_like	0.005	44	91	101	149	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRT30117.1	1.24e-121	7	390	6	393
AMK55490.1	2.54e-86	7	391	21	409
BBH25090.1	8.45e-76	3	380	1	353
QAT39807.1	2.37e-75	3	381	1	353
QNM14116.1	9.15e-75	7	381	5	353

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1X7F_A	1.37e-59	4	387	27	382	Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000035	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000773_01978.