CAZyme Information: MGYG000002592_01995

Basic Information

• Species: Alistipes sp902388705
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp902388705
• CAZyme ID: MGYG000002592_01995
• CAZy Family: GT80
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
498		55639.5	4.3697

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002592	2965227	MAG	China	Asia

• Gene Location: Start: 4985; End: 6481 Strand: -

Full Sequence      

MKNLFRLFLCLALLPGAMACSDDDTQRPTVIVNGGEDFLSLDGLARAGKLTVLASAPWRV
TAAAGDTWFTLSPTEGPAGYSEVEISLDENKGAARSARLAFSSGDVIVPFGLSQSALTNG
YDSPDYYFYVTFATMPALYAGLHVLSHNKPSYFFYSRSRTFDPDKFPSYVKVTTSADRTA
DATADEKQEAIREMRRRILEINNADPTAVFGLYVDDLRCRLGYDCFVEQGIDSARVKVSL
LSDGTATYNNFYNYFGDAATAEQNWNDYAAEVEALDWNHGGRYPVTRAQFELDSWTWVYY
LATRPGYRLVMQNSVLLESSCPFITEKLGEMTIESIQPYEMLSALPETARQQFYDMAGFD
YDKFAALFDASPKKNLVIIGTSHAGSTSEQQQYDYVARIMEQYGEGYDVFFKPHPADTSS
AGYETDFAGLTLLPGQMPFEIFVWSLMEHVDMIGGYPSTVFLTVPVDKVRFIFAANAESL
VRPLNILFRDAANVEWMQ

Enzyme Prediction     

No EC number prediction in MGYG000002592_01995.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT80	238	479	8.3e-38	0.6385224274406333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	4.65e-09	36	115	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL01105.1	2.03e-302	1	498	1	498
BBL09010.1	2.46e-111	310	498	1	189
BBL11802.1	2.46e-111	310	498	1	189
AWK81336.1	2.84e-14	123	480	111	467
BAA25316.1	2.61e-12	123	480	111	467

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4R9V_A	6.71e-14	129	480	26	376	Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae]
4R83_A	7.20e-14	123	480	117	473	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]

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
0.000310	0.144618	0.854857	0.000072	0.000072	0.000061

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002592_01995.