CAZyme Information: MGYG000003362_01157

Basic Information

• Species: Dysgonomonas sp900079735
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas sp900079735
• CAZyme ID: MGYG000003362_01157
• CAZy Family: GT80
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
569	MGYG000003362_6|CGC3	65560.63	5.1088

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003362	3888864	MAG	United States	North America

• Gene Location: Start: 109461; End: 111170 Strand: -

Full Sequence      

MCLFLFILNSCAEDPERAIILKFLVNEKTIKVSDLEETKDIQIISNIEWIVETPDPWISI
EKKENSIIIKIEQNSSQVNREGNIYLKEKNKTGLGDHIVIEQMQQQPTIVINSGTNFLSS
NSESKEIELPIEANCEWAINLDANWIKTDIVNGTKETQSLKLTINENRQLPRHANLTFTY
GNGQTLNFKIQQNAANTGFEDISHCFYATFGTMPSLYAGLHVLTHSKPSYFFYERQGTYD
PEFFPNHVTIPITIGPNAVQSLMRDYMKNKILQINEKNPNAIFGVFIDDLRARIGYDWFV
AQGIDSSRVKVTLLSDGTGSYNEFYKHFGNASTGQTAWKNIEKEVNNLKWDVTTTANKTT
KSLPEFESWQWPWYMSSCPNYRYFLQNADLLTTENEYVKGEIKKMKAISMPPLEILNSLS
NERKEIFYKMVKFDWNKLNNMLDQSPKPNLVIISTNPSLPIRPYIQETMDLYSKDYDIFY
SAHPSDIYWYDYETRYPGLKLLPSPMPFEVFLWSFVDKIDAIGGSPSTVFLTVPIEKVKF
MYASGPESMTKPLDKIFSDAIENVNWMAK

Enzyme Prediction     

No EC number prediction in MGYG000003362_01157.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT80	308	549	1.2e-24	0.6490765171503958

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	2.50e-09	23	102	2	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
cd14948	BACON	2.18e-07	108	192	1	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam19190	BACON_2	9.24e-05	118	185	9	82	Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.
pfam13004	BACON	0.003	136	192	2	60	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.
pfam13004	BACON	0.006	48	102	2	60	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL01105.1	1.56e-130	106	567	27	497
BBL09010.1	5.46e-45	385	567	2	188
BBL11802.1	5.46e-45	385	567	2	188
BAA25316.1	4.70e-12	311	562	224	480
AWK81336.1	1.03e-10	311	562	224	480

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4R9V_A	8.69e-14	311	562	133	389	Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae]
4R83_A	1.27e-13	311	562	230	486	Crystalstructure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R83_B Crystal structure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R83_C Crystal structure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R83_D Crystal structure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R84_A Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae],4R84_B Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae],4R84_C Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae],4R84_D Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae]
2Z4T_A	8.83e-12	311	550	227	472	CrystalStructure of Vibrionaceae Photobacterium sp. JT-ISH-224 2,6-sialyltransferase in a Ternary Complex with Donor Product CMP and Accepter Substrate Lactose [Photobacterium sp. JT-ISH-224]

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
0.817974	0.179604	0.001353	0.000408	0.000216	0.000457

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003362_01157.