logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002473_01117

You are here: Home > Sequence: MGYG000002473_01117

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 Victivallis vadensis
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis
CAZyme ID MGYG000002473_01117
CAZy Family GH27
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
428 48549.22 5.2975
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002473 4576885 Isolate not provided not provided
Gene Location Start: 5356;  End: 6642  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002473_01117.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 173 405 9.8e-31 0.9126637554585153

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14792 GH27 1.42e-60 9 340 1 270
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
PLN02899 PLN02899 2.27e-60 7 339 29 376
alpha-galactosidase
PLN03231 PLN03231 1.89e-57 9 348 1 355
putative alpha-galactosidase; Provisional
cd14791 GH36 1.52e-18 9 284 2 262
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
PLN02808 PLN02808 1.20e-13 9 348 32 304
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUP78535.1 1.30e-105 5 428 32 460
BCG58239.1 2.58e-96 2 428 15 451
ANQ52567.2 1.41e-86 9 414 290 724
QGH36570.1 1.33e-72 9 413 10 412
QCC19991.1 2.23e-72 9 348 36 372

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4NX0_A 4.74e-68 9 405 25 418
Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4NXK_A 7.18e-67 9 405 25 418
Crystalstructure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
3CC1_A 2.55e-62 9 427 12 428
ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
3H53_A 1.48e-11 7 348 7 300
ChainA, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H53_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens]
4NZJ_A 1.34e-10 9 412 100 453
Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q99172 4.29e-12 9 341 29 317
Alpha-galactosidase OS=Lachancea cidri OX=29831 GN=MEL PE=3 SV=1
Q8VXZ7 5.15e-11 9 423 73 422
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
P17050 6.31e-11 7 348 24 317
Alpha-N-acetylgalactosaminidase OS=Homo sapiens OX=9606 GN=NAGA PE=1 SV=2
Q9QWR8 8.40e-10 9 358 26 328
Alpha-N-acetylgalactosaminidase OS=Mus musculus OX=10090 GN=Naga PE=1 SV=2
Q66H12 1.12e-09 9 420 26 402
Alpha-N-acetylgalactosaminidase OS=Rattus norvegicus OX=10116 GN=Naga PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000044 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002473_01117.