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Conserved domains on  [gi|486835130|gb|EOH68928|]
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hypothetical protein UAG_01206 [Enterococcus faecium ATCC 8459 = NRRL B-2354]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
80-188 9.25e-26

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 98.41  E-value: 9.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130  80 MDIYTPKVEKKKSPILFWMHGGAYVGGDKNDCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPVIQLNEAIQAAKKEIKD 159
Cdd:COG0657    1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAE 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 486835130 160 -QADWSNISIGGDSAGAQISGEYLLALQNE 188
Cdd:COG0657   81 lGIDPDRIAVAGDSAGGHLAAALALRARDR 110
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
80-188 9.25e-26

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 98.41  E-value: 9.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130  80 MDIYTPKVEKKKSPILFWMHGGAYVGGDKNDCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPVIQLNEAIQAAKKEIKD 159
Cdd:COG0657    1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAE 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 486835130 160 -QADWSNISIGGDSAGAQISGEYLLALQNE 188
Cdd:COG0657   81 lGIDPDRIAVAGDSAGGHLAAALALRARDR 110
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 80-175 6.09e-15

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 69.90  E-value: 6.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130   80 MDIYTPKVEKKKSPILFWMHGGAYVGGDKNDCRDYLEYLCS---DTQQIIVNIDYERSPEAKHPTPVIQLNEAI-----Q 151
Cdd:pfam20434   1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKallKAGYAVASINYRLSTDAKFPAQIQDVKAAIrflraN 80

                          90       100
                  ....*....|....*....|....
gi 486835130  152 AAKKEIkdqaDWSNISIGGDSAGA 175
Cdd:pfam20434  81 AAKYGI----DTNKIALMGFSAGG 100
PRK10162 PRK10162
acetyl esterase;
66-190 1.72e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 58.58  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130  66 KKEISYPSKYKNNNMDIYTPKveKKKSPILFWMHGGAYVGGDKNDCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPViq 145
Cdd:PRK10162  57 TRAYMVPTPYGQVETRLYYPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAI-- 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 486835130 146 lnEAIQAAKKEIKDQAD-----WSNISIGGDSAGAQISGEYLLALQNEEI 190
Cdd:PRK10162 133 --EEIVAVCCYFHQHAEdyginMSRIGFAGDSAGAMLALASALWLRDKQI 180
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 81-175 2.71e-03

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 37.70  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130  81 DIYTPKVEKKKS--PILFWMHGGAYVGGDKNdCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPVIQLNEA-----IQAA 153
Cdd:cd00312   82 NVYTPKNTKPGNslPVMVWIHGGGFMFGSGS-LYPGDGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNyglkdQRLA 160

                         90       100
                 ....*....|....*....|....*..
gi 486835130 154 KKEIKDQA-----DWSNISIGGDSAGA 175
Cdd:cd00312  161 LKWVQDNIaafggDPDSVTIFGESAGG 187
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
80-188 9.25e-26

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 98.41  E-value: 9.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130  80 MDIYTPKVEKKKSPILFWMHGGAYVGGDKNDCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPVIQLNEAIQAAKKEIKD 159
Cdd:COG0657    1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAE 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 486835130 160 -QADWSNISIGGDSAGAQISGEYLLALQNE 188
Cdd:COG0657   81 lGIDPDRIAVAGDSAGGHLAAALALRARDR 110
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 80-175 6.09e-15

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 69.90  E-value: 6.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130   80 MDIYTPKVEKKKSPILFWMHGGAYVGGDKNDCRDYLEYLCS---DTQQIIVNIDYERSPEAKHPTPVIQLNEAI-----Q 151
Cdd:pfam20434   1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKallKAGYAVASINYRLSTDAKFPAQIQDVKAAIrflraN 80

                          90       100
                  ....*....|....*....|....
gi 486835130  152 AAKKEIkdqaDWSNISIGGDSAGA 175
Cdd:pfam20434  81 AAKYGI----DTNKIALMGFSAGG 100
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 95-192 1.87e-14

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 68.39  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130   95 LFWMHGGAYVGGDKNDCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPVIQLNEAIQAAKKEI-KDQADWSNISIGGDSA 173
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAaELGADPSRIAVAGDSA 80

                          90
                  ....*....|....*....
gi 486835130  174 GAQISGEYLLALQNEEIKK 192
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPK 99
PRK10162 PRK10162
acetyl esterase;
66-190 1.72e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 58.58  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130  66 KKEISYPSKYKNNNMDIYTPKveKKKSPILFWMHGGAYVGGDKNDCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPViq 145
Cdd:PRK10162  57 TRAYMVPTPYGQVETRLYYPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAI-- 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 486835130 146 lnEAIQAAKKEIKDQAD-----WSNISIGGDSAGAQISGEYLLALQNEEI 190
Cdd:PRK10162 133 --EEIVAVCCYFHQHAEdyginMSRIGFAGDSAGAMLALASALWLRDKQI 180
COesterase pfam00135
Carboxylesterase family;
80-131 6.36e-04

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 39.60  E-value: 6.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 486835130   80 MDIYTPKV---EKKKSPILFWMHGGAYVGGDKNDCRDylEYLCSDTQQIIVNIDY 131
Cdd:pfam00135  88 LNVYTPKElkeNKNKLPVMVWIHGGGFMFGSGSLYDG--SYLAAEGDVIVVTINY 140
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 81-175 2.71e-03

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 37.70  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486835130  81 DIYTPKVEKKKS--PILFWMHGGAYVGGDKNdCRDYLEYLCSDTQQIIVNIDYERSPEAKHPTPVIQLNEA-----IQAA 153
Cdd:cd00312   82 NVYTPKNTKPGNslPVMVWIHGGGFMFGSGS-LYPGDGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNyglkdQRLA 160

                         90       100
                 ....*....|....*....|....*..
gi 486835130 154 KKEIKDQA-----DWSNISIGGDSAGA 175
Cdd:cd00312  161 LKWVQDNIaafggDPDSVTIFGESAGG 187
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
79-107 6.91e-03

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 36.40  E-value: 6.91e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 486835130  79 NMDIYTPKV-EKKKSPILFWMHGGAYVGGD 107
Cdd:COG2272   91 YLNVWTPALaAGAKLPVMVWIHGGGFVSGS 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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