CAZyme Information: MGYG000000003_00294

Basic Information

• Species: Alistipes shahii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes shahii
• CAZyme ID: MGYG000000003_00294
• CAZy Family: GT80
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
503		55817.66	4.4333

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000003	3229518	Isolate	United Kingdom	Europe

• Gene Location: Start: 338090; End: 339601 Strand: -

Full Sequence      

MKRLFRLLLILGLAAGTWSCADDGTPSVSINGGTDFLSLDHLARSGKITVNAPAPWSVTL
APENYGQDEKPDWLTLSAEEGPAGYSEIDVTFAENPGPARSASLLFSCDGKTLAFTVSQS
AGGTGFDAPDYYFYISVGTMPTLYSGLHLLSHDKPSYVSYERASTFDAAEFPDRAFVYPV
ADPTGHATNEELRAMSEAMKRRILEINAEDPTAVFGLWVDDLRCRLGYDWFVAQGIDSAR
VKVTMLSDGTATYNNFHNYFGDAATAEQNWNDYAAEVEALDWNHGGRYPETRAPEEFASY
TWPYYLSTRPDYRLMLQNSSLMESSCPFIADRLAAMKMESVQPYKLLTALPEASKQQFYR
MAKFDYARFAGLFDLSPKKNLIIIGTSHSSAASEQQQAAYVERIIQQYGSDYDIFFKPHP
ADSSSAGYPDRFEGLTLLPGQMPFEIFVWALLDKIDMIGGYPSTTFISVPLDKVGFLFAA
DADGLVRPLNILFRDAANVEWIQ

Enzyme Prediction     

No EC number prediction in MGYG000000003_00294.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT80	341	484	1.9e-43	0.40369393139841686

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	2.88e-11	34	120	6	83	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.
pfam13004	BACON	2.61e-05	69	120	7	61	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.
pfam11477	PM0188	0.001	409	478	284	353	Sialyltransferase PMO188. PMO188 is a sialyltransferase from P.multocida. It transfers sialic acid from cytidine 5'-monophosphonuraminic acid to an acceptor sugar. It has important catalytic residues such as Asp141, His311, Glu338, Ser355 and Ser356.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL01105.1	3.40e-258	1	503	1	498
BBL09010.1	1.00e-92	315	503	1	189
BBL11802.1	1.00e-92	315	503	1	189
AWK81336.1	3.13e-09	243	483	224	465
BAA25316.1	1.17e-08	128	483	111	465

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4R83_A	3.48e-10	128	483	117	471	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]
4R9V_A	1.12e-09	237	483	124	374	Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000782	0.159971	0.838928	0.000126	0.000109	0.000101

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000003_00294.