CAZyme Information: MGYG000003590_00102

Basic Information

• Species: Sodaliphilus sp900770215
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Sodaliphilus; Sodaliphilus sp900770215
• CAZyme ID: MGYG000003590_00102
• CAZy Family: GH53
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
434		47113.93	6.1814

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003590	3134564	MAG	Fiji	Oceania

• Gene Location: Start: 3478; End: 4782 Strand: +

Full Sequence      

MTKFKHIAALAATLLIATSGARAGATGDINGDGTINVTDVTALVNKILGTASYDDTTCDT
NGDGLVNVTDVTVLVNTILGGGGTHDMRLVGGDISMLPRHEAAGAKYYAESGLVSDMIAY
YKSAGWNTMRVRLFVDPSQAPAAHQREGVVQDLAYVKALGRRIKQAGLQLVLDFHYSDTW
ADPGKQTMPSRWSSLTSPAQIADSVYAYTAASLRALAAAGAMPDYVQVGNEITYGMLWPT
GHCWPGGGNPDGGSWDNLALYLKAGCRAVRQVCPQAKIIIHTELSKMDNPAHFYSQTQDR
GIDYDIIGLSYYPAYHGTIEALSQELDTLEHRFPAKLIVLAELGYSYAWPLGGTQHDITA
TYPYTEAGQAQFIADLVTCLHNRHSHVKGLLWWWPEHNEYGNTGTQVTSGWWNASLVDSR
NGHIEQGTRELGKF

Enzyme Prediction     

No EC number prediction in MGYG000003590_00102.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH53	91	421	3.2e-92	0.9649122807017544

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07745	Glyco_hydro_53	3.55e-76	90	423	2	325	Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.
COG3867	GanB	7.09e-64	91	423	42	383	Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
cd14256	Dockerin_I	1.70e-11	27	79	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.
pfam00404	Dockerin_1	5.45e-11	27	79	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.
cd14254	Dockerin_II	7.18e-09	27	74	1	49	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
AGB28452.1	2.49e-110	88	434	22	367
ADE83762.1	6.00e-107	84	434	20	368
QUT66820.1	1.01e-95	83	434	19	363
VEH14955.1	1.29e-95	88	434	47	397
QVJ80245.1	3.20e-74	84	434	20	375

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7OSK_A	1.17e-49	91	418	53	379	ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230]
1R8L_A	5.63e-37	91	395	27	322	Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis]
2GFT_A	3.95e-36	91	395	27	322	ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis]
1HJQ_A	1.01e-33	91	405	6	308	Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]
1HJS_A	2.60e-32	91	405	6	308	Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_A Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48843	1.09e-44	89	425	7	341	Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1
Q65CX5	4.78e-36	91	395	52	347	Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1
O07013	3.43e-34	91	395	56	351	Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1
P83691	5.53e-33	91	405	6	308	Arabinogalactan endo-beta-1,4-galactanase OS=Humicola insolens OX=34413 PE=1 SV=1
P83692	1.42e-31	91	405	6	308	Arabinogalactan endo-beta-1,4-galactanase OS=Thermothelomyces thermophilus OX=78579 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000252	0.999102	0.000166	0.000159	0.000153	0.000140

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003590_00102.