CAZyme Information: MGYG000001296_00107

Basic Information

• Species: Pediococcus acidilactici
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Pediococcus; Pediococcus acidilactici
• CAZyme ID: MGYG000001296_00107
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
877	MGYG000001296_1|CGC4	99758.13	6.3515

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001296	1929633	Isolate	not provided	not provided

• Gene Location: Start: 105311; End: 107944 Strand: +

Full Sequence      

MKKVYAVAHTHWDFEWYFSRQEARVQFIFHMDDVFKALAENKLEYYMLDGQMAIVDDYLK
TCPEKRATLEKYVKAGRLFVGPWYTQIDEMVTLGESAVRNLRLGLKASRKLGKSTKVGYL
PDSFGQSKDMPKIYNGFGIKDAVFWRGLPADQKVRYFYWTSEDGSKVLTANIKNGYYAGV
DLVEKDNFKELMQNISTDTNVEDLVLPIGGDQRAVDFNLKKRLKLANRELAGEYEIIESN
YPEYFNALEQNGVLPELSGEFIDPSVSKIHRGIYSSRYDLKQIYDELEQLMIYQVEPLSA
ISRQQGMEVKQGLIDEVWQIIAKGQAHDSSGGSNSDKTNRDIYNRAVEAQQLARSLKDYL
LRKLSVSVKNGDDLFLWNPLPMSVDEVRELEVSTTTPSFEIISQDGKIGFDLIEQKQCNA
ATLRRNPAEMDNEYYYVSRIAMRVQIKATDWTSFRIKEGTAGKEILAASVTNEIQNEKYQ
IEFENGQLNITDKLNHCTYTNALSFEDGGDEGDTYDYSPAYKDWIINLGFANATITTKAG
KQTQIMLLEGTWHVPYDLQERAAKKSNGAITYRIKLQLDQGGDLIKFKMNVNNQVLDHRL
RLVMNTGVKAQNTFADTQFGVAQRPVIDPKMDNWQAIGYREEPTALRPMLHFANVHDREK
SFSFITAGMREFQAIGDQFDKLAVTLFRGVGFLGRPDLKRRPGDASGLVMKSVATPDSQL
MGEQSFQGAIVITHDWDPRQLQCMHLQVSQSGLYYQRQVINRFTTPLQYFAVNELANEVK
HRPIVKINNLKVTLSSFQTSVDQTGYELRLYNPTQQTVANPGNLQFTQNVNVSLMDLKGE
VQQTVANAVKNYSLPKFKPGEIRTIGLFPIGEIIGGD

Enzyme Prediction     

No EC number prediction in MGYG000001296_00107.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	3	253	4e-59	0.9442379182156134

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	0.0	2	865	4	872	mannosylglycerate hydrolase.
cd10815	GH38N_AMII_EcMngB_like	1.47e-135	3	265	1	270	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	5.60e-79	3	265	1	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.
COG0383	AMS1	1.61e-63	1	858	3	940	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10790	GH38N_AMII_1	3.84e-56	3	263	1	271	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
AZP90425.1	0.0	1	877	1	877
QAT21054.1	0.0	1	877	1	877
QHS03997.1	0.0	1	877	1	877
APR28206.1	0.0	1	877	1	877
ASN59220.1	0.0	1	870	1	873

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	3.49e-77	2	727	7	777	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	2.67e-74	2	727	7	777	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
2WYH_A	1.61e-54	2	694	26	784	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	8.80e-09	1	333	301	645	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	3.25e-129	1	864	4	871	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	4.12e-47	2	816	3	849	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
Q91W89	1.98e-12	4	390	252	639	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	6.86e-11	4	333	252	582	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q54K67	9.39e-09	3	342	256	594	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
1.000086	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001296_00107.