CAZyme Information: MGYG000001063_05248

Basic Information

• Species: Robinsoniella sp900540475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900540475
• CAZyme ID: MGYG000001063_05248
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
852	MGYG000001063_134|CGC3	98906.32	5.2049

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001063	7637037	MAG	Sweden	Europe

• Gene Location: Start: 34932; End: 37490 Strand: -

Full Sequence      

MVEKIILVFKTHFDIGFTDLAANVVEQYAGKMLQEVLETCKSTEDMGPLKYVWTMPAWPL
KIILERCRGKQLEDLEHYIKNGQIAWHALPFTSHTDFCGEEEYLEGLRYGRMLSEKYEKP
YPIAAKMTDVPGHGFMLPELLSASGIPFLHLGCNEFATPPRVPDLFFWEAPSGRKVLTMY
SKGGYGSGLKAPEDWNFPVWMAMMHTHDNSGPHSARLILEMAEQAKKLYPNAQVVCGTMD
DFYRELSKHDLSHLPVVQKDLADTWIHGVGSYPEEAGRIREMRRKSIRLQKLNAMSADSE
NSYGERKKELLISDYYEHMHLFGEHTWGADVKTWLGPQRVFEKESFKEARGQENYRFMEK
SWQEQRNRANCCMEDLQQYKEQLELQKGEQLSFFNPNAMPFTGWVPLKEYEESLTDANLE
INGTPMQMGTMYGTAACFVEDLLPLQTTPVTIQRNKIQPQPVKEDNGKKDEGSLIFLRDG
ENTWVENHRYMLYFDESSGIILRLFDKELDKNILESKDGTGILSYEYTRYGIEQITEFLR
TYGYRFSTWGIQDYGRENYPECKNKTFHPRFRNYKIEVDTITFYYENDISADCYGDAREI
IIEITMPKTGDELFAAVHLKGKQETPFVESGTIRIPLGENPRHFRINKSGVVIDPAQDII
EDGNHVFYALENFAAASYKDAGVCIVPWDTPLMSIGENGVYQYRHQYEQTRPVMCFNLYN
NMWGTNFPQWIGGDFTYRFLLFGYKQEEEKALMERCAYVTEGIEVTELSVNPNSRLKLPE
HMQLMNIKREGKGYFIWLRDVEGAEADCTLELPGYRITPVDYYMRRTAESREEKLSFLKK
PFGIASFYIEHQ

Enzyme Prediction     

No EC number prediction in MGYG000001063_05248.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	3.46e-60	4	267	1	254	N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which 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.
pfam16477	DUF5054	6.80e-09	324	366	46	110	Domain of unknown function (DUF5054). This family consists of Glycosyl hydrolase family 38 proteins around 700 residues in length and is mainly found in various Clostridium and Rhizobium species. The function of this family is unknown.
cd10814	GH38N_AMII_SpGH38_like	3.21e-06	73	263	66	269	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.
cd10790	GH38N_AMII_1	1.52e-04	68	194	60	187	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.
cd10789	GH38N_AMII_ER_cytosolic	1.71e-04	129	249	121	252	N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Members in this family are retaining glycosyl hydrolases of family GH38 that employs 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS95533.1	4.17e-166	3	812	5	813
AIA19246.1	2.57e-129	2	737	5	711
AOW10778.1	1.13e-105	2	745	34	778
AQT68768.1	5.75e-103	2	813	243	1058
QKJ63408.1	1.50e-93	2	813	30	844

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000042	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001063_05248.