CAZyme Information: MGYG000001632_01724

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-170
• CAZyme ID: MGYG000001632_01724
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
449		50473.05	4.5332

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001632	2419268	MAG	China	Asia

• Gene Location: Start: 159; End: 1508 Strand: +

Full Sequence      

MDYRVGFPAFALAPMSDHAGKSEWAQTEDGISYQISCEIDAKASQEEALTVFWGLGFEEV
AAATSAKEQLRRGWNWLYRKTADWLDKRTMQLPTTELTEVYNVNQFFCLFYATGRTFDTE
ELICATSRSTRYYVSAAYWDRDSLLWAFPTILRADAALAKEVLTYVFTRQRQNIGVHSRF
IDGTMLEPGFELDELVAPVLALQAYLSETHDEAFLQERFVQDGLSLILARLREARHPDTA
LYETFLQPTDDEIVHPYLTYDNVLVWRALQLLADWRPAQRGSLLAEADAVRAAIFTHCVK
KDADGQPYFAWSVDLAGHHDVYDEPPGSLQLLPYYGFCERTDVIWQNTVRMIRSADYKFS
FAGKPIAEIGCPHAPWPWVLSLCNSLLCGHAEQALRELTIMPMDNGIACESVDADTGECT
TGSAFATCAGFLCHALLTACKEGSSCGTI

Enzyme Prediction     

No EC number prediction in MGYG000001632_01724.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	239	436	1.6e-16	0.5223880597014925

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	3.22e-17	137	382	60	363	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	4.41e-15	190	383	122	358	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
QEY34932.1	1.55e-182	2	443	155	593
QIA31705.1	1.39e-180	2	436	155	588
QQR05501.1	1.39e-180	2	436	155	588
ANU41635.1	1.39e-180	2	436	155	588
QKN24824.1	1.98e-179	2	443	150	588

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QPF_A	3.10e-10	181	415	122	398	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]
3P2C_A	4.32e-09	137	379	87	384	Crystalstructure of an exo-alpha-1,6-mannosidase (bacova_03347) from bacteroides ovatus at 1.60 a resolution [Bacteroides ovatus ATCC 8483],3P2C_B Crystal structure of an exo-alpha-1,6-mannosidase (bacova_03347) from bacteroides ovatus at 1.60 a resolution [Bacteroides ovatus ATCC 8483]
6RQK_A	5.40e-09	187	398	129	377	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	1.64e-08	187	398	129	377	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]
2NVP_A	1.67e-08	187	398	129	377	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000069	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001632_01724.