CAZyme Information: MGYG000000151_02021

Basic Information

• Species: Clostridium paraputrificum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium paraputrificum
• CAZyme ID: MGYG000000151_02021
• CAZy Family: GH170
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
365	MGYG000000151_5|CGC1	41670.32	5.0305

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000151	3486414	Isolate	United Kingdom	Europe

• Gene Location: Start: 25321; End: 26418 Strand: +

Full Sequence      

MTRLGISIYPEHSTKEKDIEYIRLAGKYGFKRVFTCLLSIGKKTREELIDEFRELIDVAH
EEGMEVILDVNPVVFKDLGVSYDDLSLFSEIHADGIRLDEGFDGVKESLMTYNQGGLKIE
LNASGGSGYLDNVMSNFPNKDKVITCHNFYPQRYTGLSLEHFNNCNKAMKEYGLHTAAFV
SSNNNDTFGPWPVREGLCTLEMHRDLPIDLQVRHLFATRMIDDVMIGNAYASEEELEACS
KINPGILTFGIELDKELTEVEYEILYYKENHANRGDVSEYMARSSAPRGTFANESIQKAN
AVDMKRGDVVILNDEYSRYKGELHIVLKDMPNDGRKNVIGHIPKEELFLLNYMEPRKIFT
FKKNL

Enzyme Prediction     

No EC number prediction in MGYG000000151_02021.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH170	3	361	8.9e-126	0.9942857142857143

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3589	COG3589	3.96e-126	1	364	1	359	Uncharacterized protein [Function unknown].
pfam19200	DUF871_N	1.56e-125	4	241	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.
pfam05913	DUF871	8.81e-44	247	362	1	116	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	1.09e-05	49	99	75	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.
cd11325	AmyAc_GTHase	1.48e-04	50	107	104	167	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV22156.1	3.68e-189	1	361	1	361
ADL03119.1	3.68e-189	1	361	1	361
SEU06379.1	8.61e-188	1	361	1	361
QIX89835.1	5.20e-182	1	362	1	362
ANU44542.1	1.49e-181	1	362	1	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1X7F_A	2.59e-128	3	360	28	382	Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]
2P0O_A	6.88e-24	5	360	6	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	1.89e-17	5	363	3	345	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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000151_02021.