CAZyme Information: MGYG000000064_01531

Basic Information

• Species: Clostridium baratii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium baratii
• CAZyme ID: MGYG000000064_01531
• CAZy Family: GH170
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
366	MGYG000000064_1|CGC18	41894.76	5.6394

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000064	3139911	Isolate	United Kingdom	Europe

• Gene Location: Start: 1486331; End: 1487431 Strand: -

Full Sequence      

MARLGISIYPEHSIKEKDIEYIRLAGKYGFKRVFTCLLSIGKKTRRELIDEFRELIDVAH
EEGMEVILDVNPVVFKDLNVSYDDLSLFSEIHADGIRLDEGFDGLKESLMTYNEGGLKIE
LNASGGKGYLDNVMSNFPNKDNIITCHNFYPQRYTGLSLEHFNNCNKAMKDYGLHTAAFV
SSNNNYTFGPWPVREGLCTLEMHRDLPIDLQVRHLFATRMIDDVMIGNAYASEEELEACS
KVNPGILTFGIELDKELTKSEYEILYYKQNHANRGDVSEYMARSSAPRVAFANESIPKAN
AVDMKRGDVVILNDEYSRYKGELHIVLKDMPNDGRKNVVGHIPKEELFLLDYMEPRKIFT
FKKINK

Enzyme Prediction     

No EC number prediction in MGYG000000064_01531.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH170	3	361	5e-126	0.9942857142857143

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3589	COG3589	7.58e-127	1	363	1	358	Uncharacterized protein [Function unknown].
pfam19200	DUF871_N	4.29e-124	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	2.67e-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	1.48e-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.
cd11326	AmyAc_Glg_debranch	5.71e-04	49	75	108	131	Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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
SEU06379.1	4.22e-186	1	364	1	364
QRV22156.1	1.21e-185	1	361	1	361
ADL03119.1	1.21e-185	1	361	1	361
QIX89835.1	8.91e-181	1	362	1	362
ANU44542.1	2.55e-180	1	362	1	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1X7F_A	5.76e-125	3	360	28	382	Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]
2P0O_A	1.18e-22	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	2.01e-14	5	366	3	348	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 MGYG000000064_01531.