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CAZyme Information: MGYG000003279_00005

You are here: Home > Sequence: MGYG000003279_00005

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 sp900541585
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900541585
CAZyme ID MGYG000003279_00005
CAZy Family GT80
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
503 55999.83 4.4395
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003279 3216844 MAG United States North America
Gene Location Start: 5015;  End: 6526  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003279_00005.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT80 341 484 1.6e-43 0.40369393139841686

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14948 BACON 3.54e-10 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.
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBL01105.1 7.16e-253 1 503 1 498
BBL09010.1 8.88e-94 315 503 1 189
BBL11802.1 8.88e-94 315 503 1 189
AWK81336.1 1.35e-09 243 483 224 465
BAA25316.1 8.88e-09 128 483 111 465

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4R83_A 2.63e-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 6.38e-10 134 483 26 374
Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [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
0.001144 0.192919 0.805465 0.000179 0.000151 0.000135

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003279_00005.