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CAZyme Information: MGYG000001261_00771

You are here: Home > Sequence: MGYG000001261_00771

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 Caulobacter sp903900155
Lineage Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; Caulobacteraceae; Caulobacter; Caulobacter sp903900155
CAZyme ID MGYG000001261_00771
CAZy Family GH47
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
461 51606.39 6.1187
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001261 5012197 MAG Italy Europe
Gene Location Start: 3247;  End: 4632  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH47 43 456 1.8e-109 0.9932735426008968

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01532 Glyco_hydro_47 1.07e-121 42 456 1 452
Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
PTZ00470 PTZ00470 1.19e-73 39 460 76 521
glycoside hydrolase family 47 protein; Provisional
cd04792 LanM-like 0.001 128 214 600 682
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
cd04791 LanC_SerThrkinase 0.002 128 218 94 178
Lanthionine synthetase C-like domain associated with serine/threonine kinases. Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADG09297.1 7.15e-312 1 460 1 461
AVQ01103.1 7.15e-312 1 460 1 461
QTC92579.1 3.16e-260 6 459 6 461
QDH72853.1 1.52e-251 5 458 5 470
QNA83392.1 1.15e-179 5 460 2 461

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4AYO_A 1.06e-290 31 461 9 439
Structureof The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 [Caulobacter sp. K31],4AYP_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with thiomannobioside [Caulobacter sp. K31],4AYQ_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with mannoimidazole [Caulobacter sp. K31],4AYR_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycin [Caulobacter sp. K31],5MEH_A Crystal structure of alpha-1,2-mannosidase from Caulobacter K31 strain in complex with 1-deoxymannojirimycin [Caulobacter sp. K31],5NE5_A Crystal structure of family 47 alpha-1,2-mannosidase from Caulobacter K31 strain in complex with kifunensine [Caulobacter sp. K31]
1NXC_A 2.52e-50 37 460 22 471
Structureof mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases) [Mus musculus]
5KKB_A 2.93e-50 37 453 24 463
Structureof mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus],5KKB_B Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus]
5KIJ_A 5.75e-46 43 441 13 434
Crystalstructure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A 6.10e-46 43 441 13 434
Crystalstructure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9SXC9 1.43e-59 39 438 41 460
Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
Q9FG93 1.23e-51 38 435 43 445
Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
P53624 3.04e-51 39 455 204 645
Mannosyl-oligosaccharide alpha-1,2-mannosidase IA OS=Drosophila melanogaster OX=7227 GN=alpha-Man-Ia PE=2 SV=2
P39098 4.13e-51 39 459 184 628
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Mus musculus OX=10090 GN=Man1a2 PE=1 SV=1
O60476 7.89e-51 39 455 184 624
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Homo sapiens OX=9606 GN=MAN1A2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as TAT

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000786 0.159402 0.000428 0.838633 0.000658 0.000084

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001261_00771.