CAZyme Information: MGYG000001562_00879

Basic Information

• Species: Alistipes timonensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes timonensis
• CAZyme ID: MGYG000001562_00879
• CAZy Family: GT80
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
505		56855.8	4.2961

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001562	3488594	Isolate	not provided	not provided

• Gene Location: Start: 314618; End: 316135 Strand: +

Full Sequence      

MKRLFRLFLMFTLLTGAWACSDDKTSEVRINDGAEFLSLDYLARSGKITVNAPAPWTVIL
SAGSYGGDERPDWVTLSAEEGPEGYSEIDVTFAANPGPARSALLLFICNGKTSVFTLSQS
AKDTGFDSPDYYFYAAFGTMPALYSGLHLLSHDKPSYFFYERPQTYDPELFPDYATVFTA
ANPNAGATTEEIYAMSEQMKRRILEINAEDPTAVFGLYVTDLACRAGYDWFVEQGIDSAR
VKVTMLSDGTGTYNNFYKFFGDPATAEQNWNDYAARVEALDWNHGGRYPETRAPQDLVSD
EWIAYLSTRPNYRLMLQNASLMESSGPFMTQKLAEMKMESVQPYELLTALPEEAKKEFYR
MANFDYDRFKALFDASPKGNLIILGTSHTTDESRQQQAAYVRRIMDQYGSEYDVFFKPHP
ADNSSSDYEERFPGLTLLPGQMPFEIFVWSLLDEVNLIGGYPSTTFLSLPLDKVGFLFAT
DAASLPRPLNLLFSDAPNVEWMQQP

Enzyme Prediction     

No EC number prediction in MGYG000001562_00879.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT80	342	483	3.3e-36	0.39841688654353563

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	2.31e-10	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	1.49e-04	409	480	284	355	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	2.40e-242	1	503	1	498
BBL09010.1	2.71e-90	315	503	1	189
BBL11802.1	2.71e-90	315	503	1	189
AWK81336.1	5.54e-09	243	485	224	467
BAA25316.1	1.09e-07	343	485	315	467

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4R9V_A	2.65e-09	343	485	224	376	Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae]
4R83_A	3.30e-09	343	485	321	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
0.000764	0.143562	0.855369	0.000103	0.000103	0.000095

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001562_00879.