CAZyme Information: MGYG000001637_00870

Basic Information

• Species: Agathobacter sp900543445
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Agathobacter; Agathobacter sp900543445
• CAZyme ID: MGYG000001637_00870
• CAZy Family: CE17
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
382	MGYG000001637_5|CGC1	42834.08	5.0624

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001637	2652425	MAG	China	Asia

• Gene Location: Start: 37367; End: 38515 Strand: +

Full Sequence      

MYRYNLKREADRTVKALEYERGISNTGNWYRMKRLFERAKAGEELTIGFLGGSITQGCLA
TKPELCYAYRVYEWWVKTFPQATFHYVNAGIGGTTSHFASARVEADLLSHHVDFAIVEFS
VNDDSTEFFRETYEGVVRHVWQDPCKPAVMLVHNVYYNTGANAQIMHAQIGRHYDLPSVS
MQSSIYPEVVAGRIPNRAITQDDLHPNDNGHELVASVIIYALEQMLENPSADSEVSLPAP
LTENAYEKAFRLDNRNYEPVCDGFTKDERTQTDITDCFKNGWSATSQGAKLIFTVEASEL
AVQYRRCVSKPAPVALAIVDGDEANAVRLDANFDEDWGDKLELTPVLIHGEKKSHTLEIR
LVSGDASMPSTFDVISVIGSVK

Enzyme Prediction     

No EC number prediction in MGYG000001637_00870.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE17	49	212	3.6e-74	0.9939393939393939
CBM35inCE17	233	380	1.3e-59	0.9865771812080537

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00229	SGNH_hydrolase	5.05e-16	47	221	1	187	SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
pfam13472	Lipase_GDSL_2	5.49e-15	49	213	1	176	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd01834	SGNH_hydrolase_like_2	3.24e-09	49	221	6	191	SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EEV02614.1	1.46e-159	17	380	5	369
CBL10432.1	4.81e-158	17	380	5	369
CBL12377.1	4.81e-158	17	380	5	369
AEN97394.1	2.74e-151	17	380	5	381
BCN32107.1	2.89e-132	17	380	5	370

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HH9_A	6.57e-161	17	380	5	369	Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82]
6HFZ_A	6.19e-159	17	380	5	369	Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82]

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
1.000050	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001637_00870.