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CAZyme Information: MGYG000001508_00641

You are here: Home > Sequence: MGYG000001508_00641

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 Thalassobacillus devorans
Lineage Bacteria; Firmicutes; Bacilli; Bacillales_D; Halobacillaceae; Thalassobacillus; Thalassobacillus devorans
CAZyme ID MGYG000001508_00641
CAZy Family GH38
CAZyme Description Mannosylglycerate hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
871 MGYG000001508_4|CGC2 100246.15 4.7673
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001508 4066265 Isolate not provided not provided
Gene Location Start: 258754;  End: 261369  Strand: -

Full Sequence      Download help

MKQVHIVPHM  HWDREWYFST  EESRILLVNN  MEEIMNRLET  DPDYPYYVLD  GQTSILEDYF60
AVKPENKERV  KKLVQDGKLI  IGPWYTQTDE  MVVGGESIVR  NLQYGIKDSK  EFGSPMMIGY120
LPDSFGQSAQ  MPQILNGFDI  KYTIFWRGTS  ERHGTDKTEF  YWESDDGSKV  LVQLLPLGYA180
IGKYLPEEDG  ALKERMEKYF  PVLDRGTTTN  HLLLPNGHDQ  MPIQKNIFQV  IEKLKQLYPN240
RDFFLSKYEH  VFAEIEKQND  LATLNGEFLD  GKYMRVHRSI  YSTRMDIKAA  NTRVENKLTN300
VLEPLASMAY  DLGFEYHHGL  IELIWKEIMK  NHAHDSIGCC  CSDKVHQEIA  NRLFIAEEKT360
DRLIDFYKRQ  IVDAIDTEND  ADRLTLFNFL  PYKRKEAVTA  ELITKYGSFK  LIDENGSEVP420
FEVLEAEEID  PGLIDRQIVH  YGNYDPFIKY  QIQLKAELPA  TGYRTLFVEQ  VSENTFNHAK480
QTKEIDNDFY  RITVNGNGTV  DIFDKRLDQT  FEQVLLLENG  GDDGDEYDYS  PIEGETLLYS540
DKVEADISLT  QNAYAGEIDI  RYTLEVPADL  ESRKEGKINS  YVDVHFNLHI  PNHKPLIEVN600
CELDNQARDH  RLRALIPTGL  ASSLSIADNQ  FGFIKRGVYD  SAMDVWEKEN  WSERPDAIYP660
MLNFVGLSDQ  DYGVSVLTNS  TREYEIVGQN  YDTIALTLFR  SIGYLGKAEM  VRRPGRPSGI720
KLPTPDSQMI  GKLSLDFALF  IHEGTTLHAN  VGQMAKEYLT  PVHTYNKIPH  NAMKLNPSAN780
KTPLSYQLLE  ETEKEVVLST  LKKAEHEDAL  VIRMYNPTER  DVEASYRLCS  DFDEAYEANL840
NEVPQGKSEV  EGKEIQTSIH  SNQVKTIIIK  R871

Enzyme Prediction      help

No EC number prediction in MGYG000001508_00641.

CAZyme Signature Domains help

Created with Snap43871301742172613043483914354795225666096536967407838273260GH38
Family Start End Evalue family coverage
GH38 3 260 1.1e-77 0.9442379182156134

CDD Domains      download full data without filtering help

Created with Snap43871301742172613043483914354795225666096536967407838272870PRK098193272GH38N_AMII_EcMngB_like1857AMS14272GH38N_AMII_13272GH38N_AMII_SpGH38_like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09819 PRK09819 0.0 2 870 4 875
mannosylglycerate hydrolase.
cd10815 GH38N_AMII_EcMngB_like 2.33e-168 3 272 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.
COG0383 AMS1 2.66e-157 1 857 3 936
Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10790 GH38N_AMII_1 9.99e-111 4 272 2 273
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 2.61e-100 3 272 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      help

Created with Snap43871301742172613043483914354795225666096536967407838272870ARI79120.1|GH381871ASN04311.1|GH382871QAS54672.1|GH381870BBU38225.1|GH381868QIZ05520.1|GH38
Hit ID E-Value Query Start Query End Hit Start Hit End
ARI79120.1 0.0 2 870 12 880
ASN04311.1 0.0 1 871 1 871
QAS54672.1 0.0 2 871 6 875
BBU38225.1 0.0 1 870 1 871
QIZ05520.1 0.0 1 868 1 868

PDB Hits      download full data without filtering help

Created with Snap438713017421726130434839143547952256660965369674078382728162WYH_A28225KBP_A28223LVT_A48156LZ1_A48157DD9_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WYH_A 1.43e-114 2 816 26 874
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 3.29e-113 2 822 7 855
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 5.04e-109 2 822 7 855
TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
6LZ1_A 4.88e-20 4 815 283 1016
Structureof S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_B Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_C Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_D Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-]
7DD9_A 5.67e-20 4 815 283 1016
ChainA, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_C Chain C, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_E Chain E, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_G Chain G, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct]

Swiss-Prot Hits      download full data without filtering help

Created with Snap43871301742172613043483914354795225666096536967407838271819sp|P54746|MNGB_ECOLI2856sp|Q9KER1|MNGB_ALKHC4815sp|Q9UT61|MAN1_SCHPO4398sp|Q9NTJ4|MA2C1_HUMAN4398sp|Q91W89|MA2C1_MOUSE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54746 0.0 1 819 4 824
Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1 5.42e-101 2 856 3 884
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
Q9UT61 2.60e-19 4 815 283 1016
Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q9NTJ4 2.27e-18 4 398 253 638
Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q91W89 2.99e-18 4 398 252 637
Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000040 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001508_00641.