CAZyme Information: MGYG000001338_00520

Basic Information

• Species: Blautia_A wexlerae_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A wexlerae_A
• CAZyme ID: MGYG000001338_00520
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
431	MGYG000001338_1|CGC10	49616.18	4.8336

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001338	3930699	Isolate	not provided	not provided

• Gene Location: Start: 571492; End: 572787 Strand: -

Full Sequence      

MKQIEKIPESIRNILDKVKTFFPENPQIYEIFKNCYTNTLNTAVHSMENDTVYVVTGDIP
AMWLRDSAASLRPYLIPAKEDKNIADILVGVVHRQFLYICIDPYANAFNQKPNGNCWEKD
ETEMNDWLWERKYEVDSLCYPIQLAYLIWKNTGRTDQFDHTFVNGAWKILNVFRTEQYHE
EKSAYRFIRRNTYYTDTLSRDGKGTHVKSGIGMTWSGFRPSDDACTYGYLVPSNMFAVVV
LGYLEEIARLIVESSDLAKAAAELRKEIYDGIENFAITCKEGYGEVYAYEVDGYGQFNLM
DDANVPSLLSMDYLGYEGKNPQVAENTRNLILSEANPFYYRGAKAEGIGSPHTPVEYIWH
IALCMQGLTASTREEKKKMIDLAASTDGGKMLMHEGFCVKDDTQYTREWFAWANAMFSEL
VMDYCGYKIER

Enzyme Prediction     

No EC number prediction in MGYG000001338_00520.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	26	422	1.5e-168	0.9950248756218906

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	0.0	6	430	5	428	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	0.0	25	422	1	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
AWY97337.1	3.70e-207	7	431	3	426
ASM70396.1	4.14e-202	5	431	3	428
QJS18224.1	6.31e-202	5	430	3	428
ANU77102.1	1.30e-193	8	431	4	427
QJU17274.1	1.30e-193	8	431	4	427

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QT3_A	2.96e-152	24	423	24	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]
6RQK_A	1.11e-151	24	423	24	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]
5M7I_A	6.33e-151	24	423	24	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	8.90e-146	24	423	24	421	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A	5.32e-145	9	424	6	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	1.26e-83	9	423	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
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001338_00520.