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CAZyme Information: MGYG000001159_00252

You are here: Home > Sequence: MGYG000001159_00252

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 Bifidobacterium pullorum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium pullorum
CAZyme ID MGYG000001159_00252
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
992 MGYG000001159_12|CGC1 108065.09 3.979
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001159 2232439 MAG Austria Europe
Gene Location Start: 123613;  End: 126591  Strand: -

Full Sequence      Download help

MGASHVFPQG  GTTVKRRIAA  IAAGIATAAM  ALGGVVAPPA  TAYADEPAAA  DVSSVTNPNN60
RHFMVYYRAW  RDVTMKGVNT  DLPDENWISM  YDIPYGVDVV  NVFSYVPAGQ  EAAAQPFYDK120
LKAEYAPYLH  SRGIKLVRGI  NYEQVTVEGF  RDYMADLGKT  ADEATEADYD  AYALEIIDEY180
MTSVGLDGLD  IDMETYPTDA  DVAISDNVIR  ALSKHIGPKS  DDPDGTMFLY  DTNGSNTKPF240
ANVADCFDYV  AYQQYGSTST  RTAGAVADYS  PYIGADKFVP  GLAFPEEGDH  NRWYDATEPY300
TDSHIYDIAS  YVRDNGLGGM  FLYALDRDGR  TYEAEDWSHI  VPSNLLWTKT  AIAESQDMTM360
EQAKAAANHY  IERMSLTEEG  AAGVALNAED  ALEAVEQATN  LYEVNKAVLG  GDYDEGFSNT420
YDPTLEVGLL  GVDTTELMDR  ISAADNILAG  DVMSDDVKSA  VRQSRDAAVE  GLTGRTYTAD480
EVAMWTADLQ  ADIEAAMASL  TGVESSDRHF  MVYYRAWRDV  TMKGVNTDLP  DENWISMYDI540
PYGVDVVNVF  SYVPAGQEAA  AQPYYDKLKS  DYAPYLHSRG  IKLVRGVDYT  GVIVDGFRDF600
IEAKGLTEQE  ATEADYDEYA  LQVIDEYMTS  VGLDGLDIDM  ETHPDEADVA  VSDNVIRALS660
KHIGPKSDNP  DGTMFLYDTN  ASDLAPFRNV  ADCFDYVAYQ  QYGSNAERTD  DAFGDYAPHI720
GSEFVPGLTF  PEEGDMNNRW  YDATEPYEES  NFYQVASYVN  EHKLGGMFVY  ALDRDGRDYE780
DDLTRIVPSN  LLWTKTAIAE  SQGMPLDQAK  AAAKHYIERM  SLASAEGVAL  NADEAGAAVA840
AAANLYEVNK  AVLGGDYGEG  FSNTYDPTLE  AGLLDIDIDE  LMSLIEQADK  ALEAEDDDTV900
RTARDAAMDG  LTGKIYTADE  VGQWVDALTA  ALKGEETPSG  PDDTSKPNTD  VQKPADEKPL960
ASSGSAVAAV  LSVAVAAAVA  GIGLTVWRRR  KV992

Enzyme Prediction      help

EC 3.2.1.96

CDD Domains      download full data without filtering help

Created with Snap499914819824829734739644649654559564469474479384389294262336GH18_EndoS-like509781GH18_EndoS-like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06542 GH18_EndoS-like 1.60e-45 62 336 2 249
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
cd06542 GH18_EndoS-like 6.31e-44 509 781 2 247
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.

CAZyme Hits      help

Created with Snap4999148198248297347396446496545595644694744793843892942491989BAJ70116.1|GH18491989QKY14302.1|GH18491989VEG44861.1|GH18491989ACJ53522.1|GH18|3.2.1.96491989QTB92326.1|GH18
Hit ID E-Value Query Start Query End Hit Start Hit End
BAJ70116.1 2.50e-228 491 989 34 543
QKY14302.1 2.50e-228 491 989 34 543
VEG44861.1 2.50e-228 491 989 34 543
ACJ53522.1 2.50e-228 491 989 34 543
QTB92326.1 7.07e-228 491 989 34 543

PDB Hits      download full data without filtering help

Created with Snap49991481982482973473964464965455956446947447938438929425059327PUJ_A4957986KPL_A4957986KPN_A663456E58_A663384NUY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
7PUJ_A 1.54e-151 505 932 8 429
ChainA, Beta-N-acetylhexosaminidase [Enterococcus faecalis],7PUK_A Chain A, Beta-N-acetylhexosaminidase [Enterococcus faecalis],7PUK_C Chain C, Beta-N-acetylhexosaminidase [Enterococcus faecalis]
6KPL_A 1.89e-31 495 798 16 292
CrystalStructure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris in apo form [Cordyceps militaris CM01],6KPM_A Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris in complex with L-fucose [Cordyceps militaris CM01]
6KPN_A 2.16e-30 495 798 16 292
CrystalStructure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris D154N/E156Q mutant in complex with fucosyl-N-acetylglucosamine [Cordyceps militaris CM01],6KPO_A Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris D154N/E156Q mutant in complex with fucosyl-N-acetylglucosamine-Asn [Cordyceps militaris CM01]
6E58_A 5.03e-18 66 345 28 319
Crystalstructure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2) [Streptococcus pyogenes M49 591],6E58_B Crystal structure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2) [Streptococcus pyogenes M49 591],6MDS_A Crystal structure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2) with complex biantennary glycan [Streptococcus pyogenes],6MDS_B Crystal structure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2) with complex biantennary glycan [Streptococcus pyogenes],6MDV_A Crystal structure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2) with high-mannose glycan [Streptococcus pyogenes],6MDV_B Crystal structure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2) with high-mannose glycan [Streptococcus pyogenes]
4NUY_A 1.21e-12 66 338 20 320
Crystalstructure of EndoS, an endo-beta-N-acetyl-glucosaminidase from Streptococcus pyogenes [Streptococcus pyogenes serotype M1]

Swiss-Prot Hits      download full data without filtering help

Created with Snap4999148198248297347396446496545595644694744793843892942491989sp|B7GPC7|EBI1_BIFLS497775sp|P36912|EBA2_ELIME
Hit ID E-Value Query Start Query End Hit Start Hit End Description
B7GPC7 5.00e-229 491 989 34 543
Endo-beta-N-acetylglucosaminidase OS=Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) OX=391904 GN=Blon_2468 PE=1 SV=1
P36912 3.16e-29 497 775 49 307
Endo-beta-N-acetylglucosaminidase F2 OS=Elizabethkingia meningoseptica OX=238 GN=endOF2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.004387 0.978949 0.000457 0.015394 0.000497 0.000295

TMHMM  Annotations      download full data without filtering help

start end
21 43
965 987