CAZyme Information: MGYG000003846_00336

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; CAG-312; CAG-312
• CAZyme ID: MGYG000003846_00336
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
474	MGYG000003846_3|CGC4	53613.09	7.9576

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003846	2141960	MAG	United States	North America

• Gene Location: Start: 73096; End: 74520 Strand: -

Full Sequence      

MGVLNMLKIFRLVFSCALCTGVVFIYNSLYSSNAAGETAPYANVDFSKKAGIIKPLHGVN
ESPIVFNGSLPEFIEAGIPYVRLHDVGGRYGGSCFVDIPNVFPDFNADPEDPNSYDFAFT
DAYIATLVNSGVKVFYRLGVTIENYHKIKAYRIHPPVDNLKWAKICEGIIRHYNEGWAKG
FKYGIEYWEIWNEPEIPQMWTGTKEQFFELYRVAANYLKKRFPEIKVGGYASCGFYAITG
ENTSSFNKSLVQYFNDFLKYISAPGTRAPLDFFSWHLYFANPDTIAKHAEYVRSKLDENG
FANVESIFNEWNDNTRIDESDLRRTYLGASNVGAAFCIMQDAPIDKAMYYNARPGGVYCG
LYEPPNKLAKSYFVFKAFNELKKLGNAALCESSRDRGIYVCAAISDSGKERAILVSNNSP
DRKRVKMSFNGKLKSCLIIDDRYSYAELNFMYDKKNSTLDMRGKSVALLKIEAP

Enzyme Prediction     

No EC number prediction in MGYG000003846_00336.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	108	416	4.9e-37	0.7308584686774942

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01229	Glyco_hydro_39	2.26e-13	75	313	45	263	Glycosyl hydrolases family 39.
cd21510	agarase_cat	3.36e-09	173	278	87	187	alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM69820.1	1.10e-117	44	427	5	397
QJD82796.1	5.65e-95	48	431	9	392
QTH43246.1	8.42e-91	51	429	12	390
QJD85864.1	9.51e-85	46	435	8	402
QEL16017.1	9.32e-73	53	419	38	408

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z3K_A	6.90e-34	43	417	10	376	Crystalstructure of glucosidase from Croceicoccus marinus at 1.8 Angstrom resolution [Croceicoccus marinus],5Z3K_B Crystal structure of glucosidase from Croceicoccus marinus at 1.8 Angstrom resolution [Croceicoccus marinus]
1W91_A	3.62e-14	86	278	46	230	crystalstructure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_B crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_C crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_D crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_E crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_F crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_G crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_H crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct]
2BS9_A	3.62e-14	86	278	46	230	Nativecrystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_B Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_C Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_D Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_E Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_F Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_G Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_H Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
2BFG_A	1.99e-13	86	278	46	230	crystalstructure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus],2BFG_B crystal structure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus],2BFG_C crystal structure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus],2BFG_D crystal structure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus],2BFG_E crystal structure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus],2BFG_F crystal structure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus],2BFG_G crystal structure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus],2BFG_H crystal structure of beta-xylosidase (fam GH39) in complex with dinitrophenyl-beta-xyloside and covalently bound xyloside [Geobacillus stearothermophilus]
4M29_A	1.91e-12	75	433	53	404	Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZFM2	1.99e-13	86	278	46	230	Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
P23552	2.29e-10	75	232	51	203	Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB PE=3 SV=1
T2KM23	9.86e-06	139	318	145	304	Alpha-1,4-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22200 PE=2 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
0.999311	0.000659	0.000048	0.000003	0.000002	0.000017

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003846_00336.