alginate O-acetyltransferase [Hahella ganghwensis]
Protein Classification
alginate O-acetyltransferase( domain architecture ID 10199203)
alginate O-acetyltransferase such alginate biosynthesis protein AlgX that plays two roles in the biosynthesis of the exopolysaccharide alginate: protects alginate from degradation as the polymer traverses the periplasm, and plays a role in its O-acetylation
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| AlgX_N | cd14441 | N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ... |
35-350 | 2.43e-155 | |||||
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains. : Pssm-ID: 270207 Cd Length: 310 Bit Score: 443.29 E-value: 2.43e-155
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| CBM6-CBM35-CBM36_like super family | cl14880 | Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ... |
349-472 | 2.75e-41 | |||||
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality. The actual alignment was detected with superfamily member pfam16824: Pssm-ID: 449372 Cd Length: 125 Bit Score: 143.47 E-value: 2.75e-41
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| Name | Accession | Description | Interval | E-value | |||||
| AlgX_N | cd14441 | N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ... |
35-350 | 2.43e-155 | |||||
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains. Pssm-ID: 270207 Cd Length: 310 Bit Score: 443.29 E-value: 2.43e-155
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| ALGX | pfam16822 | SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ... |
58-328 | 2.77e-83 | |||||
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction. Pssm-ID: 435599 Cd Length: 267 Bit Score: 258.04 E-value: 2.77e-83
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| CBM_26 | pfam16824 | C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding ... |
349-472 | 2.75e-41 | |||||
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding modules frequently found at the C-terminus of enzymes. The combination is not unusual as the CBMs function to bring the relevant polysaccharide into close proximity to the active site. Pssm-ID: 435600 Cd Length: 125 Bit Score: 143.47 E-value: 2.75e-41
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| AlgX_C | cd14487 | C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate ... |
340-465 | 4.23e-40 | |||||
C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains. Pssm-ID: 271153 Cd Length: 128 Bit Score: 140.56 E-value: 4.23e-40
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| Name | Accession | Description | Interval | E-value | |||||
| AlgX_N | cd14441 | N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ... |
35-350 | 2.43e-155 | |||||
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains. Pssm-ID: 270207 Cd Length: 310 Bit Score: 443.29 E-value: 2.43e-155
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| ALGX | pfam16822 | SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ... |
58-328 | 2.77e-83 | |||||
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction. Pssm-ID: 435599 Cd Length: 267 Bit Score: 258.04 E-value: 2.77e-83
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| AlgJ_like | cd14442 | putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate ... |
61-331 | 7.97e-46 | |||||
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this family have been annotated as AlgJ or AlgV, and they closely resemble AlgX in sequence and function, although they lack the C-terminal carbohydrate binding domain of AlgX. Pssm-ID: 270208 Cd Length: 321 Bit Score: 162.09 E-value: 7.97e-46
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| AlgX_N_like | cd14439 | N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ... |
54-343 | 1.95e-43 | |||||
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. This wider family includes AlgX, AlgJ, AlgV, and a number of uncharacterized families, some of which may have been mis-annotated in sequence databases. Pssm-ID: 270205 [Multi-domain] Cd Length: 316 Bit Score: 155.69 E-value: 1.95e-43
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| CBM_26 | pfam16824 | C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding ... |
349-472 | 2.75e-41 | |||||
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding modules frequently found at the C-terminus of enzymes. The combination is not unusual as the CBMs function to bring the relevant polysaccharide into close proximity to the active site. Pssm-ID: 435600 Cd Length: 125 Bit Score: 143.47 E-value: 2.75e-41
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| AlgX_C | cd14487 | C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate ... |
340-465 | 4.23e-40 | |||||
C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains. Pssm-ID: 271153 Cd Length: 128 Bit Score: 140.56 E-value: 4.23e-40
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| AlgX_N_like_1 | cd14444 | Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate ... |
60-328 | 3.68e-35 | |||||
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such those as by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized family similar to AlgX_N have been annotated as cell division proteins FtsQ, although they share little or no similarity with experimentally characterized members of the FtsQ family. Pssm-ID: 270210 Cd Length: 298 Bit Score: 132.82 E-value: 3.68e-35
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| AlgX_N_like_2 | cd14443 | Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate ... |
59-326 | 3.58e-10 | |||||
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Some members of this uncharacterized family, which resembles AlgX_N, have been annotated as twin-arginine translocation signal, although they share little or no similarity with experimentally characterized proteins that bear the same name. Pssm-ID: 270209 Cd Length: 313 Bit Score: 60.89 E-value: 3.58e-10
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| AlgX_N_like_3 | cd14440 | Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ... |
54-177 | 1.21e-05 | |||||
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized protein family resemble AlgX_N. Pssm-ID: 270206 [Multi-domain] Cd Length: 315 Bit Score: 46.97 E-value: 1.21e-05
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