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CAZyme Information: MGYG000000437_02230

You are here: Home > Sequence: MGYG000000437_02230

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

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      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000437_02230.

CAZyme Signature Domains help

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

CDD Domains      download full data without filtering help

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      help

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      download full data without filtering help

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      help

has no Swissprot hit.

SignalP and Lipop Annotations help

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      help

There is no transmembrane helices in MGYG000000437_02230.