CAZyme Information: MGYG000003504_00054

Basic Information

• Species: CAG-1435 sp003537755
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-314; CAG-1435; CAG-1435 sp003537755
• CAZyme ID: MGYG000003504_00054
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
943		106610.96	6.1815

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003504	2246614	MAG	Fiji	Oceania

• Gene Location: Start: 23683; End: 26514 Strand: +

Full Sequence      

MKKIHLINGTHWDREWRHTAEQSKLRLVDLMDNIINLLETKPEYKYFCVDGGTIVIEDYL
TIRPENKQRIIDLIKAKRMFVVNWYTLPETNTVAPESLVRNLLWGHKMASELGGGMKSGY
TATSYGQPSQLPQLYRGFGITDAIFYRGTNKHVLTPLFTWVGADGTTIDTLRTFDEVTRT
NWFFYVHGPAVLGKGQKDLTYTYNRSQIPVHMADMQSYEKAFTLLHEDFDYIHDVNVQKN
AIDNLLKQAEPYAIGNHILALNMEDNDEPYKYLPELIADMNKIYPDVQIEQCSMDEYMAE
IKAVKGYKKAEHHGELRYTTMEYNNFNALLGATHSSRIKIKLLNDECENNLLNIAEPLAS
YAEAYGKEYPRKNIDRAWEYLLKCHAHDSICGAAVDRAHDDMLYNFSLAKTVAEEVANRS
CVALYGNINTAEHFLSTDHTLTVFNTLPFSRKEVIEVVFDTPKGGGQAVDIGVGGASSVG
DFYDIVDEKGNKVPYVELTRDDSAIGVEREMDTKAIKFNADRKRVLVEVTVPQNGFKTYA
LRFREPDLAYHPEVMPPRKLIARDNGVLENEFVKVAINSNGTFDLTDKTTGRVMPQQLYF
TDNGEVGSAHISVKPKRNATYTSLGSAATITLTESNELRGVYKIDIAMDLPAEATIDGND
RSRGFKTLAITTTLTLNKGEKFLRIRTTLDNRIRDHKLVVNFPSGLTAAEWVDCESAWDV
AHRTINHLDTKDNFDKFLPFQPMQNFVDVSDGKDGLAVMTKGLREYEVDDDKLRTIKITL
IRTQRAYMTANSKMTYEELDRYTGQHSFGKMTYEMCLYPHQGNFEAAHVWNAAYAAKVPL
KAIQGVATNGVLPDCASFVTFSQEGKVMTSALKQAENGDGLTLRVYNTTDETLPLTISTI
LPVKEVLRVHLDESNAEKTNFDGKAWSLDIGAKKIETFVLKLK

Enzyme Prediction     

No EC number prediction in MGYG000003504_00054.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	3	306	1.6e-44	0.9442379182156134

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	2.41e-138	2	923	4	858	mannosylglycerate hydrolase.
COG0383	AMS1	3.00e-83	1	942	3	941	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10815	GH38N_AMII_EcMngB_like	2.87e-70	3	317	1	267	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.
cd10814	GH38N_AMII_SpGH38_like	5.26e-67	3	318	1	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	7.68e-45	3	303	1	254	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQQ69680.1	0.0	2	941	5	939
ARN55766.1	0.0	3	937	7	946
AQQ70157.1	9.90e-253	2	941	5	959
QHI68002.1	7.98e-248	2	922	6	925
QHI69929.1	2.10e-219	50	916	14	889

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	3.72e-91	2	894	7	856	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	8.52e-88	2	894	7	856	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
2WYH_A	1.86e-76	2	934	26	922	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	4.97e-08	1	455	301	699	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
P54746	6.47e-75	1	923	4	862	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	1.75e-72	2	887	3	845	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
P22855	2.71e-07	1	455	288	686	Alpha-mannosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=AMS1 PE=1 SV=2

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
1.000047	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003504_00054.