CAZyme Information: MGYG000003077_00119

Basic Information

• Species: CAG-196 sp002102975
• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; CAG-196; CAG-196 sp002102975
• CAZyme ID: MGYG000003077_00119
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
700	MGYG000003077_1|CGC1	81748.1	5.9507

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003077	2204918	MAG	Spain	Europe

• Gene Location: Start: 123162; End: 125264 Strand: +

Full Sequence      

MRKQVIAYLHTHWDREWYREFEIFRMRLLRVFDNVLEMLAKNKIPCFYFDGQVSALEDYL
AMRPEREELVISLIRHKRLFIGPFYCLVDEFLTDQTCFRKNLEIGLKTAQKYGCKDFIGY
LADTFGHSQNIVDVLRDFGIDKCMVWRGVNDFPSEFSWCGMDTINLVRGYFNDIFSLKTS
IEKKAEILKNNLDKIAEKSGNVLLLPIGADHLGVETDINDQIEAVNEILKNDYFIRLGSP
FDYFKRIENRFKDFVWNDELRDNSKTFTLQGCYSSRLDLKRENIECTYLLDLASRFVKQQ
KDNSYNTILEYAYKMLLQNQAHDSICGCSTDDVHAENKIRYKKIKQIANTIIDELKFKNH
FEEKRILNLSGEAYSGIIEFKTSRIIEGYDRIGFENGFDRYLLTDTQRIPVTEDYTKINT
YLADVENLKPDEIEYIMPAINKSDLKITETRIENSNISLRIENGQIFINGIKFSLYDFAD
LGDSYNFGPQKDDYGTELHIIRSKPILKTASRVTLKIDFEGRWDVIPLFVSLDKNASHLH
FRFDWINSQKNHLLQAVFNLSNPIREVFSEDMNILIKRNFNPEYDIRQNLPENRGIEVKN
NTAPMQRGLLIDEEGNNLGIITKGLTQYEVFQNKLFLPILRSTGQISNPQNPARTTPAGP
PIEVESLQQIGRNTAEFYVFFGNHNAFKDVLNHVYNYIVV

Enzyme Prediction     

No EC number prediction in MGYG000003077_00119.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	5	255	3.4e-44	0.9442379182156134

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10814	GH38N_AMII_SpGH38_like	3.66e-68	10	264	7	271	N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38). The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular.
PRK09819	PRK09819	2.23e-60	1	681	2	746	mannosylglycerate hydrolase.
cd10815	GH38N_AMII_EcMngB_like	4.10e-57	10	262	7	268	N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial homologs; glycoside hydrolase family 38 (GH38). The bacterial subfamily is represented by Escherichia coli alpha-mannosidase MngB, which is encoded by the mngB gene (previously called ybgG). MngB exhibits alpha-mannosidase activity that converts 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. A divalent metal ion is required for its activity.
cd10790	GH38N_AMII_1	6.77e-49	10	276	7	272	N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase.
COG0383	AMS1	3.12e-33	1	346	2	392	Alpha-mannosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOR37692.1	3.61e-239	1	695	17	654
ANC78687.1	2.22e-66	10	685	12	738
ALM76549.1	7.82e-66	1	697	17	796
ADT82990.1	5.19e-65	1	697	17	796
ADD01829.1	1.60e-62	10	671	9	736

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	6.55e-47	2	648	6	759	Thecrystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],5KBP_B The crystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
3LVT_A	2.38e-44	2	648	6	759	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
2WYH_A	1.53e-42	3	383	26	445	Structureof the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYH_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYI_A Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS],2WYI_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS]
5JM0_A	5.84e-06	10	167	309	473	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9KER1	1.82e-47	1	677	1	774	Putative mannosylglycerate hydrolase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=mngB PE=3 SV=2
P54746	7.47e-33	10	352	12	368	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q54K67	9.90e-10	4	356	256	606	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG 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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003077_00119.