CAZyme Information: MGYG000000111_00999

Basic Information

• Species: Cutibacterium acnes
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Cutibacterium; Cutibacterium acnes
• CAZyme ID: MGYG000000111_00999
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
431	MGYG000000111_2|CGC3	47913.56	4.3546

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000111	2484103	Isolate	Canada	North America

• Gene Location: Start: 168134; End: 169429 Strand: +

Full Sequence      

MRACELTPALRQRLDEIGAQISQGVGKGLDEAMGRQAASRFVAWMTDTWTRTMSRDEHGV
FVVTGDIPAMWLRDSSAQLWPFLMMCDLPEVARQIGDVIARQWHCIDVDPYANAFNSGPT
GAHFDADDLDVADELWERKYEVDSLAFPVDLAWRYWQATGSSEHLNGAIHQGCIRIIDIW
SLEQDHAQSTYRHVRPAEPSDTLGRDGSGTPVGHTGMTWSGFRPSDDACRYGYNIPAQFM
AMRALRQIREFCRVWDDEDLAERATKLADEIDAGVRQFGIVEDHLAYEVDGLGSVLEMDD
ANMPSLLSLPLTSDLGRDDPLYQSTRRWVLSAANPYLFSGPVARGIGSPHSPKGYIWHIG
LAVQGLTGDDAEACDCLETILATDGGTGWTHESFDPTDPTRFTRGWFSWSNSMACLLMMN
VADIDDIIGAN

Enzyme Prediction     

No EC number prediction in MGYG000000111_00999.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	45	418	3.8e-126	0.9676616915422885

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06824	Glyco_hydro_125	9.25e-167	42	419	20	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	5.23e-164	45	424	35	425	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALD68840.1	0.0	1	431	1	431
ALU22646.1	0.0	1	431	1	431
AER05489.1	0.0	1	431	1	431
ALT41254.1	0.0	1	431	1	431
AID35074.1	0.0	1	431	1	431

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RQK_A	2.65e-113	7	413	5	414	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	4.12e-113	7	413	5	414	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	1.50e-112	7	413	5	414	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	1.09e-109	7	413	5	414	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A	1.73e-100	25	424	8	425	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	1.65e-61	47	423	93	498	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
1.000071	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000111_00999.