CAZyme Information: MGYG000000437_02230

Basic Information

• Species: Alistipes sp001941065
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp001941065
• CAZyme ID: MGYG000000437_02230
• CAZy Family: GT80
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
504		56462.13	4.2675

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000437	3341375	MAG	Sweden	Europe

• Gene Location: Start: 3131; End: 4645 Strand: +

Full Sequence      

MKRLFRLFLASALLTGAWACSDDKTSEVRINDGAEFLSLDYLARSGKITVNAPAPWNVVL
TTGTYGGAEKPDWVTLSTENGPEGYSEIEVTFAKNPGPARSAVLLFSCEGKVSPFTLSQS
ADNTGFDAPDYYFYAAFGTMPALYSGLHLLSHDKPSYFFYERPQTFDPELFPDYAKVFTA
ANPNAGATTEEIYEMGRQMKRRILEINAEDPTAVFGLYVTDLACRAGYDWFVGQGIDSAR
VKVTMLSDGTGTYNNFHTFFGDPATAEQNWNDYAAQVEALDWNHGGRYPETRAPEDLVSD
EWIAYLSTRPNYRLMLQNSSLMESSGPFMTQKLAEMKMESVQPYELLTALPEDAKQEFYR
MANFSYDHFKDLFDASSKGNLIVLGTSHTTDESRQQQAAYVQRIMDQYGSEYDVFFKPHP
ADNSSSDYEERFPGLTLLPGQMPFEIFVWSLLDEIDLIGGYPSTTFISVPLDKVGFLFAA
DAASLPRPLNLLFQDAPNVEWMQP

Enzyme Prediction     

No EC number prediction in MGYG000000437_02230.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT80	342	483	8.1e-36	0.39841688654353563

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	1.07e-09	35	120	7	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.
pfam11477	PM0188	1.75e-04	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	5.69e-243	1	503	1	498
BBL09010.1	2.36e-88	315	503	1	189
BBL11802.1	2.36e-88	315	503	1	189
AWK81336.1	2.61e-06	243	477	224	459
BAA25316.1	5.31e-06	343	477	315	459

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4R9V_A	1.38e-07	343	477	224	368	Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae]
4R83_A	1.65e-07	343	477	321	465	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
0.000487	0.089479	0.909842	0.000067	0.000071	0.000059

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000437_02230.