CAZyme Information: MGYG000000032_01452

Basic Information

• Species: Hungatella effluvii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella effluvii
• CAZyme ID: MGYG000000032_01452
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
430	MGYG000000032_3|CGC2	48965.51	4.5638

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000032	6969476	Isolate	United Kingdom	Europe

• Gene Location: Start: 130958; End: 132250 Strand: -

Full Sequence      

MIERPEILTETADELENYYKKAYPPLAPLVKPCFLNTIDTTVKKLGEEEYFVITGDIEAM
WLRDSSFQVMHYVPFAAKDEKLRAILRGIIGKQASQILTDPYANAFNEVPDGRGHQDKTQ
LNDWVWERKYELDSLCAPLYLAHAYWKETGCADIFTEEFERMMAVLLAVVKTEQDHDNSA
YTFERSDCPETDTLPCGGLGNPVGLTGMSWSGFRPSDDCCTYGYLIPSNMMAVVALGYGE
EILRKVLKNISLAEEYAKTRKQIQEGIEAFGMVEHPRCGKMYAYETDGLGHYNLMDDANS
PSLLAMPYLHYCGCEDEFYVNTRKFILSGDNPFYYRGACADGVGSPHTPEDYIWHIAIVM
RALTSADREEILACLEQLAGTHAGLNFMHESFHKDDPTRFTRSWFAWANSLFSALMLKLK
EEEFFEFGEK

Enzyme Prediction     

No EC number prediction in MGYG000000032_01452.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	26	417	8.7e-164	0.9900497512437811

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	0.0	24	416	25	419	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	0.0	24	416	2	415	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
SET74067.1	2.64e-191	1	424	4	428
BCK01269.1	8.69e-185	5	426	6	428
QOV20899.1	3.88e-179	5	426	14	436
AUS97899.1	4.88e-164	24	422	23	423
AQZ46333.1	9.20e-162	24	419	22	419

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RQK_A	6.10e-151	26	413	28	416	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	1.88e-150	26	413	28	416	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	3.49e-150	26	413	28	416	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	1.98e-144	26	413	28	416	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A	1.21e-130	1	417	1	420	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	1.66e-87	26	423	80	500	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
1.000074	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000032_01452.