CAZyme Information: MGYG000001393_02118

Basic Information

• Species: Hafnia paralvei
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Hafnia; Hafnia paralvei
• CAZyme ID: MGYG000001393_02118
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
884	MGYG000001393_38|CGC2	101289.11	5.903

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001393	4880992	Isolate	not provided	not provided

• Gene Location: Start: 230385; End: 233039 Strand: +

Full Sequence      

MTNSTTQTTSRVHITPHMHWDREWYFTTEESRVLLVNNMEEILQRLEQDADYKFYVLDGQ
TAVLEDYFAVCPHNRERVKALVQSGKLIVGPWYTQTDTMMVSAESIVRNLMYGMRDCLSL
GEPMKIGYLPDSFSMSSQLPHIFNGFGITRAMFWRGCSERHGTDKTEFRWQSNDGSEVTA
QVLPLGYAIGKYLPSDEAGLRDRLDKYFPVLEQASITKDILLPNGHDQMPLQQNIFAVMD
KLREIYPDREFILSRFEKVFERIEAIHDQLPVLRGEFNDGKYMRVHRTISSTRMDIKQAH
AAIENKIVNILEPLCAIAWSLGFDYHHGLFEKMWKEILKNHAHDSISCCCSDKVHQEVMS
RFTLADDMAESLIQFTLRKIADNLHNQHEISDSLTLFNFSPYARDEVINTTIRIRANAFR
LTDNEGKEVPYFIRASREIDPGLVDRQIVHYGNYDPFMEFDIQLERRLPAMGYTTLRITQ
AEAQRLSNEDNHDQALENAFYRITVNANGSLNIFDKQAGIHYERALLLENGGDDGDEYDY
SPPREEWLMTSEQAQAQTEFIHQSLQSIAVIQFAQPVPASLAERATHCASLSMPVTLCVT
LAKNSRRIDIDITLENLAEDHRLRVLIPTPFPSQNVLADNPFGTMTRPTRDPAMQHWQQE
DWKEAPIPVWQMLNFVALQGDKAGMALFTQGLREFEIVGEQNDTFALTLFRSVGVLGKEE
LLLRPGRPSGIKLPTPDSQMKGKHRFQFALFGFTGTALEAGVPQFAHDYLTPIRCYNKMP
YNAMKLNLAPHQTPHHYSLLEMPRIGVMLSALKKAEDREELIIRCYNPSEQAPAMGKVSI
HPQTIHWSEAGMDEILREETQHQSGDMGNFAPCQSKTFSFALKK

Enzyme Prediction     

No EC number prediction in MGYG000001393_02118.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	12	275	1.1e-73	0.9702602230483272

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	0.0	8	880	2	874	mannosylglycerate hydrolase.
COG0383	AMS1	0.0	11	880	5	939	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10815	GH38N_AMII_EcMngB_like	1.55e-157	11	281	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.
cd10790	GH38N_AMII_1	6.11e-129	11	281	1	273	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.
cd10814	GH38N_AMII_SpGH38_like	1.31e-89	11	281	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQE41940.1	0.0	1	884	1	884
AJQ98087.1	0.0	1	884	1	884
AMH16596.1	0.0	1	884	1	884
QXN63405.1	0.0	10	880	5	876
ALX93266.1	0.0	10	880	5	876

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WYH_A	3.10e-106	9	829	25	876	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]
5KBP_A	3.74e-100	4	831	1	853	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	3.55e-95	4	831	1	853	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
5JM0_A	6.45e-13	7	356	299	652	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	0.0	10	882	5	876	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	6.90e-95	12	862	5	880	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
Q9NTJ4	5.55e-16	12	408	253	638	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q91W89	9.95e-14	12	362	252	595	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q54K67	1.75e-13	3	880	250	1084	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
1.000057	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001393_02118.