CAZyme Information: MGYG000001159_00260

Basic Information

• Species: Bifidobacterium pullorum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium pullorum
• CAZyme ID: MGYG000001159_00260
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
431	MGYG000001159_12|CGC1	48513.5	4.2425

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001159	2232439	MAG	Austria	Europe

• Gene Location: Start: 140471; End: 141766 Strand: +

Full Sequence      

MPYATIPPSVQRFMDRITELCGTEHAGWAEDFNAAFANTLTTTVNRHDDGTTFLLTGDIP
AMWLRDSTAQVRPYLVIAAEDPDLASMIEGLVRLQFRYIGIDPYANAFNEEPNGATWDPD
DRSDFSSPWLWERKYELDSLCYPIQLAWLLYANTGRTTQFDDTFLAGVRRILDVLETELD
HENSPYFFIRDCDIPTESLSREGKGSPVAPTGMTWSGFRPSDDACTYHYLVPANMFAVVV
MGYLERIFTEILDDADIAARARALRTSIDEGLRAHGTMRNAAGETIWAYEVDGLGNALLM
DDSNVPSLMAAPYLGCCDADDPLYLSTRRTLLSAENPFYYEGEHTRGIGSPHTPPRYVWP
IALSVQGMTSPSQEEKAAILDNLVAIDAGTHLMHEGVCVDDPTQYTREWFSWSNMMFCEL
VMDYFGIRVKR

Enzyme Prediction     

No EC number prediction in MGYG000001159_00260.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	28	422	1.9e-168	0.9900497512437811

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	0.0	6	430	6	428	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	0.0	28	422	4	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
QAY32589.1	9.03e-295	1	431	1	431
QOL31856.1	5.07e-260	1	431	1	432
SDO44769.1	1.88e-255	1	430	1	431
BAJ71444.1	7.63e-255	1	430	1	431
AUD83280.1	7.63e-255	1	430	1	431

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QPF_A	1.73e-163	10	428	8	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]
6RQK_A	1.82e-132	14	423	8	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	1.04e-131	14	423	8	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]
3QT3_A	3.21e-131	14	423	8	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]
2NVP_A	1.00e-126	14	423	8	421	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q10449	2.07e-85	9	423	63	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
1.000052	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001159_00260.