CAZyme Information: MGYG000001208_00180

Basic Information

• Species: Enterococcus_C dispar
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_C; Enterococcus_C dispar
• CAZyme ID: MGYG000001208_00180
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
429	MGYG000001208_1|CGC3	48672.45	4.3319

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001208	2570475	MAG	Austria	Europe

• Gene Location: Start: 200928; End: 202217 Strand: +

Full Sequence      

MTYKDIPKSIQQFMVEITTKCGSEHADWAENFNAAFANTLLTTVKRHDDGSTFLLTGDIP
AMWLRDSTAQVRPYLVVAKEDEDLAAMISGLVKKQFYYINIDPYANAFNEEANGAGHQSD
HTTMNDWIWERKYEIDSLCYPVQLAYLLYKNTGRTDQFNEDFVSGVDKILTVFTTEQDHS
NSPYTFVRDTDRKEDTLINEGKGAEVVPTGMTWSGFRPSDDACDYGYLVPSNMFAVVILG
YLEEIFSTVLKDEEVVAWAHKLKVQIEAGIKEYGRTTNQAGETIFAYEVDGKGNATIQDD
SNVPNLISAPYLGYGTMDDPQYLATRQTLLSKENPYFYEGKFAKGIGSSHTPENYVWPIA
MAMEGMTTADKAEKERILNQLVATDAGTHLMHEGFDVDDPNQYTREWFSWANMMFCELVM
DYFDIQVKK

Enzyme Prediction     

No EC number prediction in MGYG000001208_00180.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	26	420	6.9e-175	0.9950248756218906

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	0.0	4	429	4	429	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	0.0	27	420	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCA84653.1	3.35e-305	1	429	1	429
QXJ60842.1	3.99e-281	1	429	1	429
QCT93268.1	8.20e-274	1	429	1	429
AYY08467.1	1.17e-273	1	429	1	429
QGR81824.1	1.17e-273	1	429	1	429

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QPF_A	3.09e-190	10	426	8	426	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]
6RQK_A	3.49e-137	16	421	10	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	1.08e-136	16	421	10	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	1.99e-136	16	421	10	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	4.82e-132	16	421	10	421	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q10449	8.57e-80	8	421	62	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000075	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001208_00180.