CAZyme Information: MGYG000004044_00316

Basic Information

• Species: UMGS1633 sp900553645
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1633; UMGS1633 sp900553645
• CAZyme ID: MGYG000004044_00316
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
442		50062.53	5.2708

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004044	2665198	MAG	United Kingdom	Europe

• Gene Location: Start: 18199; End: 19527 Strand: -

Full Sequence      

MGKIKFDFEKVTGPMRPLHGICNAPILGTDDALFHYLGEAGIPYSRLHDTGGRYGGYVFV
DIENIFRNFDADVNDPASYDFPFTDWLLAELMKQGAEPFYRLGATIENSYALNAYRIIPP
KDPHKWAEICTHIIAHYNEGWASGFHYNIKYWEIWNEPDNSPDMMNNPMWRGTKEQYFEL
YEVTAKLLKARFPDIKVGGYASCGFYAIDDENLVAAANVDERTQHFLDFAHDFLAWITSD
AHRAPIDFFSWHSYANAQRNVRFAQYARKILTDVGLDNVESIFNEWNPGIANRGLLWDAA
LIAEMMCVMHRESDVSLMTYYDGQVNTSYGGMFDPVHERPFKAYYPFKAFNELYKLGQAV
ELSIHGGHITALAAKGEGKRAIMLVNTSKRAEKCVLEGLPDGDMQLKLIDHRHDLTDAGS
VSVTDGHAEINVGGYNVALLMA

Enzyme Prediction     

No EC number prediction in MGYG000004044_00316.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	68	387	3.4e-33	0.7378190255220418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01229	Glyco_hydro_39	1.84e-15	3	388	2	391	Glycosyl hydrolases family 39.
cd21510	agarase_cat	2.58e-09	120	254	73	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.
pfam12891	Glyco_hydro_44	8.27e-05	120	207	101	185	Glycoside hydrolase family 44. This is a family of bacterial glycoside hydrolases formerly known as cellulase family J, and now known as Cel44A. It is one of the major enzymatic components of the cellulosome of Clostridium thermocellum strain F1 and of many other Firmicutes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM69820.1	5.06e-137	4	440	3	446
QJD85864.1	6.03e-76	1	430	1	435
QJD82796.1	3.33e-65	9	386	8	378
QTH43246.1	7.37e-63	9	386	8	378
AVM46100.1	1.97e-57	7	415	7	407

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z3K_A	8.76e-19	1	287	6	266	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	2.29e-15	51	266	47	242	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	2.29e-15	51	266	47	242	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	5.40e-15	51	266	47	242	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]
1PX8_A	1.22e-12	79	258	77	234	Crystalstructure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1PX8_B Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_A Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_B Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_C Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_D Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZFM2	2.98e-15	51	352	47	307	Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
O30360	1.56e-11	79	258	77	234	Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=xynB PE=3 SV=1
P36906	8.58e-11	79	258	77	234	Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynB 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
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004044_00316.