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CAZyme Information: MGYG000003447_01061

You are here: Home > Sequence: MGYG000003447_01061

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia;
CAZyme ID MGYG000003447_01061
CAZy Family GH109
CAZyme Description Glycosyl hydrolase family 109 protein 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
487 53954.41 5.9457
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003447 1841163 MAG Fiji Oceania
Gene Location Start: 725;  End: 2188  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.49

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH109 58 479 2.2e-157 0.9924812030075187

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0673 MviM 1.52e-18 62 414 4 330
Predicted dehydrogenase [General function prediction only].
pfam01408 GFO_IDH_MocA 4.32e-15 62 188 1 118
Oxidoreductase family, NAD-binding Rossmann fold. This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
COG4091 COG4091 0.003 62 158 18 128
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism].
cd17541 REC_CheB-like 0.003 120 172 32 113
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins. Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SEI00642.1 5.72e-240 29 486 35 474
QHV64416.1 4.63e-212 20 487 27 481
QHV71784.1 4.63e-212 20 487 27 481
QHV69330.1 4.63e-212 20 487 27 481
QHV66866.1 4.63e-212 20 487 27 481

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6T2B_A 2.52e-192 25 486 6 447
Glycosidehydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila],6T2B_B Glycoside hydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila],6T2B_C Glycoside hydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila],6T2B_D Glycoside hydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila]
2IXA_A 5.39e-73 53 479 15 433
A-zyme,N-acetylgalactosaminidase [Elizabethkingia meningoseptica],2IXB_A Crystal structure of N-ACETYLGALACTOSAMINIDASE in complex with GalNAC [Elizabethkingia meningoseptica]
3E18_A 3.94e-18 59 327 3 254
CRYSTALSTRUCTURE OF NAD-BINDING PROTEIN FROM Listeria innocua [Listeria innocua],3E18_B CRYSTAL STRUCTURE OF NAD-BINDING PROTEIN FROM Listeria innocua [Listeria innocua]
3EC7_A 6.56e-10 62 216 24 174
CrystalStructure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_B Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_C Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_D Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_E Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_F Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_G Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_H Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3IP3_A 2.48e-08 96 213 37 150
Structureof putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima],3IP3_B Structure of putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima],3IP3_C Structure of putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima],3IP3_D Structure of putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima],3IP3_E Structure of putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima],3IP3_F Structure of putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima],3IP3_G Structure of putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima],3IP3_H Structure of putative oxidoreductase (TM_0425) from Thermotoga maritima [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B2UL75 5.32e-212 20 487 27 481
Glycosyl hydrolase family 109 protein 1 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0017 PE=3 SV=1
B2UQL7 2.51e-191 25 486 31 472
Glycosyl hydrolase family 109 protein 2 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0920 PE=1 SV=1
Q8ECL7 9.77e-163 36 486 29 457
Alpha-N-acetylgalactosaminidase OS=Shewanella oneidensis (strain MR-1) OX=211586 GN=nagA PE=3 SV=1
A0KV43 5.59e-162 36 486 29 457
Glycosyl hydrolase family 109 protein 1 OS=Shewanella sp. (strain ANA-3) OX=94122 GN=Shewana3_1428 PE=3 SV=1
Q0HKG4 7.92e-162 36 486 29 457
Glycosyl hydrolase family 109 protein 1 OS=Shewanella sp. (strain MR-4) OX=60480 GN=Shewmr4_1375 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000377 0.998889 0.000204 0.000182 0.000171 0.000153

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003447_01061.