CAZyme Information: MGYG000000193_01338

Basic Information

• Species: KLE1615 sp900066985
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; KLE1615; KLE1615 sp900066985
• CAZyme ID: MGYG000000193_01338
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
442	MGYG000000193_11|CGC1	50816.69	4.404

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000193	4116467	Isolate	China	Asia

• Gene Location: Start: 32964; End: 34292 Strand: +

Full Sequence      

MLTQKIQLGEEISVLAKKLAQEGKEVLCEKGFTKEQQEIFEEMFQKCFVSTADTTTKLLE
NGETYVFTGDIEAMWLRDSSAQVVHYLPFAKEFLQIRHMIAGLIQRQMRYITIDPYANAF
NEEENGHCWEKDDTESNDWEWERKYEVDSLCYPLWLLHSYYEATGDETVFSPEVKKAFRR
ILDTWKTEQHHDNESSYYFRRINCPPTDTLSNDGKGEPTAYTGMTWSGFRPSDDACRYGY
LVPSNMFASVVLGYLAEYAADKYHDEEMAKEALTLKKEIEMGIDSYAVRNLEGIGETYVY
ETDGYGNDVWMDDANVPNLLSMPWLGWCDASDERYQNTRKWVLSSKNPFYYEGSAAKGVG
SPHTPSGYIWHIALAMQGLTSNDEGEKTGLMQTLLATDAGTRLMHEGFNSNDPTAFTREW
FAWANSLFALYAMEYCGLTNRD

Enzyme Prediction     

No EC number prediction in MGYG000000193_01338.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	41	429	1.9e-161	0.9776119402985075

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	0.0	43	437	30	424	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	0.0	43	429	7	412	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHQ63498.1	1.17e-192	4	434	6	425
BCJ97505.1	1.21e-192	25	434	16	425
QTH43525.1	6.62e-175	43	429	38	424
AUS97899.1	1.21e-172	6	428	6	413
AQW22793.1	2.51e-172	41	434	29	421

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RQK_A	2.82e-172	41	434	29	421	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	4.29e-172	41	434	29	421	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	1.62e-171	41	434	29	421	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	8.14e-167	41	434	29	421	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A	8.02e-132	42	435	27	422	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q10449	2.97e-77	43	429	83	490	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000036	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000193_01338.