logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002383_01918

You are here: Home > Sequence: MGYG000002383_01918

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 Lacticaseibacillus zeae
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus zeae
CAZyme ID MGYG000002383_01918
CAZy Family GH125
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
430 MGYG000002383_13|CGC12 47990.6 4.4194
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002383 3001027 Isolate Italy Europe
Gene Location Start: 600280;  End: 601572  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002383_01918.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH125 27 417 4.8e-134 0.9825870646766169

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam06824 Glyco_hydro_125 4.45e-171 21 418 2 416
Metal-independent alpha-mannosidase (GH125). This family, which contains bacterial and fungal glycoside hydrolases, is also known as GH125. They function as metal-independent alpha-mannosidases, with specificity for alpha-1,6-linked non-reducing terminal mannose residues. Structurally this family is part of the 6 hairpin glycosidase superfamily.
COG3538 COG3538 2.45e-161 26 422 28 424
Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ARY92634.1 0.0 1 430 1 430
BAN75645.1 1.50e-313 1 430 1 430
QPC15349.1 1.50e-313 1 430 1 430
QVI36720.1 1.75e-312 1 430 1 430
QXG58511.1 1.75e-312 1 430 1 430

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3QPF_A 1.59e-109 28 421 28 423
Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QPF_B Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QRY_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QRY_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QSP_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae],3QSP_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae]
3QT3_A 1.21e-103 46 413 48 415
Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Clostridium perfringens CPE0426 apo-structure [Clostridium perfringens],3QT9_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose [Clostridium perfringens]
6RQK_A 2.18e-103 46 427 48 429
Crystalstructure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13],6RQK_B Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13]
5M7I_A 1.23e-102 46 427 48 429
Crystalstructure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannobiose [Clostridium perfringens str. 13],5M7Y_A Crystal structure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannotriose [Clostridium perfringens str. 13]
2NVP_A 6.97e-99 46 427 48 429
X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q10449 3.32e-66 20 424 75 500
Meiotically up-regulated gene 157 protein OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mug157 PE=1 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
1.000066 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002383_01918.