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CAZyme Information: MGYG000004219_01654

You are here: Home > Sequence: MGYG000004219_01654

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; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873;
CAZyme ID MGYG000004219_01654
CAZy Family GH97
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1079 MGYG000004219_35|CGC1 118475.66 4.6169
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004219 2569787 MAG United Kingdom Europe
Gene Location Start: 13894;  End: 17133  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004219_01654.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH97 24 607 1.2e-156 0.9746434231378764
CBM35 621 743 6.5e-21 0.9831932773109243
CBM32 872 981 2.9e-20 0.8306451612903226

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam10566 Glyco_hydro_97 2.79e-68 274 502 1 263
Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
pfam14508 GH97_N 5.98e-51 27 268 1 234
Glycosyl-hydrolase 97 N-terminal. This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.
pfam14509 GH97_C 2.70e-27 519 608 1 97
Glycosyl-hydrolase 97 C-terminal, oligomerization. Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.
cd04081 CBM35_galactosidase-like 5.58e-21 620 743 3 125
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.
cd04082 CBM35_pectate_lyase-like 1.24e-13 619 743 2 124
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADO69318.1 1.84e-125 27 638 30 622
ATB36826.1 6.91e-124 27 638 29 620
AEE97714.1 4.70e-122 27 610 16 593
AEC02290.1 3.59e-115 27 746 51 740
SDT24292.1 1.05e-108 17 744 37 759

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5XFM_A 1.09e-63 28 603 22 638
Crystalstructure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_B Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_C Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_D Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron]
3A24_A 4.64e-50 83 607 61 640
Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron]
5E1Q_A 4.51e-49 83 607 75 654
Mutant(D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482],5E1Q_B Mutant (D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482]
5HQ4_A 6.52e-45 27 606 5 657
AGlycoside Hydrolase Family 97 enzyme from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8],5HQA_A A Glycoside Hydrolase Family 97 enzyme in complex with Acarbose from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]
5HQC_A 6.52e-45 27 606 5 657
AGlycoside Hydrolase Family 97 enzyme R171K variant from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D7CFN7 2.68e-81 42 605 57 618
Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1
Q8A6L0 3.44e-49 83 607 82 661
Retaining alpha-galactosidase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1871 PE=1 SV=1
G8JZS4 9.81e-32 24 607 24 723
Glucan 1,4-alpha-glucosidase SusB OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=susB PE=1 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
0.023036 0.975681 0.000375 0.000321 0.000279 0.000286

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004219_01654.