CAZyme Information: MGYG000002908_00967

Basic Information

• Species: Lancefieldella parvula
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; Lancefieldella; Lancefieldella parvula
• CAZyme ID: MGYG000002908_00967
• CAZy Family: GH170
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
364	MGYG000002908_5|CGC1	41481.13	5.6939

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002908	1338544	MAG	United States	North America

• Gene Location: Start: 34078; End: 35172 Strand: -

Full Sequence      

MKRLGISIYPEKSTKEDILAYLDRAADAGFSRIFSCLLSVQDTKEAIVQKFSDINAHAHR
LGFEIIVDVNPRVFKELGISYDNLSFFKEIGADGFRLDLGFTGKEESFMTFNPEGLFVEL
NMSNDVDYLDTIMKYQPNRNKLIGCHNFYPHGYSGLGLEFFNRCTERFTKYGINTAAFVT
SQAQNSFGPWPVTEGLPTLEMHRHMPMHLQVEHYISMGTIDDVIISNCFATESEFEKIKS
LPHDLVSFGVKLVDAIPSIEKSIVLEELHCNRGDVSENLIRSSQSRVKYKEHTFDVFNAP
STIRRGDVIIESSLYGHYAGEMQIARTDMINTGKTNVVGHIPDEEHFLIDTLQPWQKFRL
HEVL

Enzyme Prediction     

No EC number prediction in MGYG000002908_00967.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH170	3	360	3.4e-116	0.9942857142857143

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3589	COG3589	6.73e-134	1	362	1	358	Uncharacterized protein [Function unknown].
pfam19200	DUF871_N	6.39e-124	4	239	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	2.24e-46	246	360	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	0.005	14	98	23	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.
cd11316	AmyAc_bac2_AmyA	0.008	70	98	159	184	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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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
ACV51680.1	3.92e-271	1	364	1	364
BBK63008.1	7.10e-182	1	363	1	363
BBK23266.1	1.01e-181	1	363	1	363
BBM59717.1	6.50e-180	1	358	1	358
BBM49503.1	1.31e-179	1	358	1	358

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1X7F_A	7.50e-120	2	358	27	381	Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]
2P0O_A	5.63e-32	5	360	6	357	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	2.67e-14	5	358	3	341	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
1.000035	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002908_00967.