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CAZyme Information: MGYG000003112_00788

You are here: Home > Sequence: MGYG000003112_00788

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E;
CAZyme ID MGYG000003112_00788
CAZy Family GH125
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
218 MGYG000003112_134|CGC1 24574.85 4.5368
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003112 1402119 MAG Sweden Europe
Gene Location Start: 54;  End: 710  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003112_00788.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH125 1 209 2.3e-87 0.5174129353233831

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam06824 Glyco_hydro_125 1.21e-125 1 210 207 416
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 9.28e-113 1 209 211 419
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
ASS66075.1 2.08e-93 1 211 212 422
QOT07875.1 3.45e-92 1 211 211 421
BBH86003.1 2.61e-91 1 210 209 418
QDM44646.1 4.93e-91 1 213 211 423
AYB45662.1 5.55e-91 1 211 211 421

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6RQK_A 4.95e-83 1 218 211 428
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]
3QT3_A 1.12e-82 1 216 211 426
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]
5M7I_A 2.79e-82 1 218 211 428
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 5.65e-79 2 218 212 428
X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A 1.96e-68 1 211 209 421
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q10449 1.31e-60 4 211 288 495
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
1.000018 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003112_00788.