CAZyme Information: MGYG000001619_01218

Basic Information

• Species: UBA9502 sp900540335
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA9502; UBA9502 sp900540335
• CAZyme ID: MGYG000001619_01218
• CAZy Family: GH170
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
362	MGYG000001619_14|CGC2	40897.52	5.2955

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001619	2970880	MAG	China	Asia

• Gene Location: Start: 53473; End: 54561 Strand: +

Full Sequence      

MARLGISIYPEQSVLEEDLSYIRMAGKYGYQRVFTCLLSAGEKTKEELTEEFRLRIDEAH
RQGMEVILDVNPAVFAKLGASYENLEAFAEMHADGIRLDEGFDGMKTSRLSYNPQGLKVE
LNASTEMGYIEDVMSHFPDRKKLITCHNFYPQKYTGISLEHFTKCGEYIHSHGLNIAAFI
SSNQPGAYGPWPVNEGLCTLEMHRGLPADFQTRHLFATGLADDVILANAYGSEEELKTCA
SVNPSVLTFSMIPEKELTETERKILYFEEGHVVRGDMSEYMLRSTWPRVTFAGESIPAAN
TRDIVRGDVVILNDGYGRYKGELHIVLKDMPNDGRKNVIGHLPGYEQILLQYAKPWKPFA
FL

Enzyme Prediction     

No EC number prediction in MGYG000001619_01218.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH170	3	361	6.4e-113	0.9942857142857143

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3589	COG3589	2.89e-119	1	361	1	356	Uncharacterized protein [Function unknown].
pfam19200	DUF871_N	1.26e-107	4	240	1	234	DUF871 N-terminal domain. This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
pfam05913	DUF871	7.54e-47	247	361	1	115	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	7.36e-04	56	99	82	117	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.
cd11339	AmyAc_bac_CMD_like_2	0.003	56	99	105	156	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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
ANU44542.1	9.81e-198	1	361	1	361
ASN95847.1	5.66e-197	1	361	1	361
QRP39378.1	5.66e-197	1	361	1	361
QIX89835.1	9.35e-196	1	361	1	361
QJU19892.1	9.35e-196	1	361	1	361

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1X7F_A	2.27e-118	3	360	28	382	Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]
2P0O_A	3.00e-26	2	360	3	356	Crystalstructure of a conserved protein from locus EF_2437 in Enterococcus faecalis with an unknown function [Enterococcus faecalis V583]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0H2XHV5	1.44e-14	5	361	3	343	6-phospho-N-acetylmuramidase OS=Staphylococcus aureus (strain USA300) OX=367830 GN=mupG PE=1 SV=1

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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001619_01218.