CAZyme Information: MGYG000003369_00596

Basic Information

• Species: Anaerococcus sp900258475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; Anaerococcus sp900258475
• CAZyme ID: MGYG000003369_00596
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
426	MGYG000003369_30|CGC1	48936.24	4.4613

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003369	1844507	MAG	United States	North America

• Gene Location: Start: 21515; End: 22795 Strand: +

Full Sequence      

MKEIVRDLVEKVEKSDQLTDEIKKIFKKAINNTFTTTIKETDRGDAFVITGDIEAMWLRD
SSGQIRPLFYIDSKEANDLIKKVLARQIFCLDKDLYANAFNIEANGRCWTDKDITDFESP
WVWERKYELDSLCYVMELAYLYYEKTKDGTIFDGEFLRVLNDMVDLIKLEQNHDNSPYIF
ERPDPWAPSDSLRGGPRGTDVSYTGMSWTGFRPSDDSCIYQYLIPANAFCVVALRRLAAC
LDEESLANELSEKMKKLADEIDCGIKKYGIVEDSDFGKVYAYETDGLGSYNLMDDANIPS
LLSLPYLGYLAKDDPIYKSTRAFILSDKNENYYEGKAAKGIGSNHTPENYIWHLALSMQL
MTATDKKEQEEILGYFEKTHAGTYLCHEGFDKDNPEKYTRDWFSWSNSIFVEAVLSYLGI
EMIKAS

Enzyme Prediction     

No EC number prediction in MGYG000003369_00596.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	21	415	5.4e-144	0.9925373134328358

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	0.0	21	422	26	427	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	0.0	21	415	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
QZO75647.1	3.02e-195	1	424	1	424
QUY64940.1	2.32e-193	1	424	5	428
AVR01162.1	8.80e-143	5	416	9	420
ASN07283.1	3.84e-142	5	416	1	412
QNF27513.1	1.16e-140	5	416	9	420

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RQK_A	3.32e-134	1	410	8	415	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	5.11e-134	1	410	8	415	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	1.89e-133	1	410	8	415	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	2.82e-130	1	410	8	415	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A	3.26e-116	2	421	5	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q10449	4.28e-75	16	418	73	497	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
1.000092	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003369_00596.