CAZyme Information: MGYG000003431_00267

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; HUN007
• CAZyme ID: MGYG000003431_00267
• CAZy Family: CE1
• CAZyme Description: Endo-1,4-beta-xylanase Z

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
308		33242.52	4.395

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003431	2512610	MAG	Fiji	Oceania

• Gene Location: Start: 35; End: 961 Strand: +

Full Sequence      

MNHGVMGSENDLLSGWSIREMASNLIEKGEVQPFIIVFTQMYTNPAADRPSGINQDDMDR
YDDFLYDLTESLMPYMAENYSAAEGRENTAIAGFSMGGRESLYIGMMACDKIGYVCASSP
APGIVPAQDMFLNHRGSMTEAEFGFKTAPYLLMIGGGTNDSVVGTFPKQYSELYTKKGQD
HIWFEVQGGGHDASVGTPLFYNFFRNLFKTGSTQEPAVTTVTTVTEPVPAETTPTTTEKP
SVTQPPATEIVAGDADGNGAVTVADVVKLMQHLIGKVTLSGDNAKAADMNGDGKISIIDL
IKLKNKLL

Enzyme Prediction     

EC	3.2.1.8	3.1.1.73

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE1	2	194	2.8e-21	0.7841409691629956

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14256	Dockerin_I	1.02e-19	253	308	2	57	Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
COG2382	Fes	4.64e-14	24	210	121	298	Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism].
pfam00404	Dockerin_1	1.71e-12	253	308	1	56	Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.
cd14252	Dockerin_like	2.89e-12	253	308	1	57	Dockerin repeat domains and domains resembling dockerin repeats. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.
cd14254	Dockerin_II	1.66e-06	253	301	1	47	Type II dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II dockerins, which are responsible for mediating attachment of the cellulosome complex to the bacterial cell wall.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADU21606.1	8.41e-67	3	209	132	341
CAB93667.1	1.61e-62	3	209	583	792
ADZ47894.1	2.00e-54	3	208	63	270
AAR39816.1	4.50e-48	3	180	600	782
CAA90271.1	4.50e-48	3	180	600	782

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5CXU_A	7.29e-56	3	208	63	270	Structureof the CE1 ferulic acid esterase AmCE1/Fae1A, from the anaerobic fungi Anaeromyces mucronatus in the absence of substrate [Anaeromyces mucronatus],5CXX_A Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus],5CXX_B Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus],5CXX_C Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus]
1JJF_A	4.09e-32	3	215	69	265	ChainA, Endo-1,4-beta-xylanase Z [Acetivibrio thermocellus]
1JT2_A	1.12e-31	3	215	69	265	ChainA, PROTEIN (ENDO-1,4-BETA-XYLANASE Z) [Acetivibrio thermocellus]
6RZO_A	4.34e-08	1	209	154	344	Crystalstructure of the N-terminal carbohydrate binding module family 48 and ferulic acid esterase from the multi-enzyme CE1-GH62-GH10 [uncultured bacterium]
6RZO_B	4.35e-08	1	209	154	344	Crystalstructure of the N-terminal carbohydrate binding module family 48 and ferulic acid esterase from the multi-enzyme CE1-GH62-GH10 [uncultured bacterium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P10478	2.38e-29	3	215	88	284	Endo-1,4-beta-xylanase Z OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xynZ PE=1 SV=3
D5EXZ4	3.54e-09	1	189	470	660	Carbohydrate acetyl esterase/feruloyl esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe1-6A PE=1 SV=1
P31471	8.53e-06	3	209	181	389	Uncharacterized protein YieL OS=Escherichia coli (strain K12) OX=83333 GN=yieL PE=4 SV=3

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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003431_00267.