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Conserved domains on  [gi|1239680976|gb|ASW74531|]
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alpha/beta hydrolase [Chryseobacterium piperi]

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
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 68-297 1.15e-76

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: 234.38  E-value: 1.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  68 LDIYSPKGNSIeKFPVLIYIHGGGWVEGDKIIRANnYVESTILKLVEQQYAVISINYTLvSKDVHFPLPVQDTKDAIRWV 147
Cdd:pfam20434   1 LDIYLPKNAKG-PYPVVIWIHGGGWNSGDKEADMG-FMTNTVKALLKAGYAVASINYRL-STDAKFPAQIQDVKAAIRFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 148 RKNAEKYHFDTNNIGLFGTSAGAHLSLLSAYTQDN-EFIGD-----PELSSYSAKVNYVVNNFGPTDLNKLLKTRVGkvg 221
Cdd:pfam20434  78 RANAAKYGIDTNKIALMGFSAGGHLALLAGLSNNNkEFEGNvgdytPESSKESFKVNAVVDFYGPTDLLDMDSCGTH--- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239680976 222 afivslfskKIVDLREKLILGisgydinKDKRKIIEYFETISPVSYV-GSATPTLILQGNRDKIVPLHQSKILHHKL 297
Cdd:pfam20434 155 ---------NDAKSPETLLLG-------APPLENPDLAKSASPITYVdKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Abhydrolase_11 super family cl48564
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 272-335 1.29e-05

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


The actual alignment was detected with superfamily member pfam20408:

Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 45.27  E-value: 1.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 272 TPTLILQGNRDKIVPLHQskILHHKLiNEGVknTLTIVDGGDHGFRT------TNQAYLDQLVDEMVRFI 335
Cdd:pfam20408 128 CPTLILQGERDPFGNREE--VAAYPL-PDNV--SLHWLEDGDHDFKPrkrsglTHEQNLQEAADAIAAFI 192
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 68-297 1.15e-76

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: 234.38  E-value: 1.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  68 LDIYSPKGNSIeKFPVLIYIHGGGWVEGDKIIRANnYVESTILKLVEQQYAVISINYTLvSKDVHFPLPVQDTKDAIRWV 147
Cdd:pfam20434   1 LDIYLPKNAKG-PYPVVIWIHGGGWNSGDKEADMG-FMTNTVKALLKAGYAVASINYRL-STDAKFPAQIQDVKAAIRFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 148 RKNAEKYHFDTNNIGLFGTSAGAHLSLLSAYTQDN-EFIGD-----PELSSYSAKVNYVVNNFGPTDLNKLLKTRVGkvg 221
Cdd:pfam20434  78 RANAAKYGIDTNKIALMGFSAGGHLALLAGLSNNNkEFEGNvgdytPESSKESFKVNAVVDFYGPTDLLDMDSCGTH--- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239680976 222 afivslfskKIVDLREKLILGisgydinKDKRKIIEYFETISPVSYV-GSATPTLILQGNRDKIVPLHQSKILHHKL 297
Cdd:pfam20434 155 ---------NDAKSPETLLLG-------APPLENPDLAKSASPITYVdKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
69-335 1.32e-41

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 143.86  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  69 DIYSPKGNSiEKFPVLIYIHGGGWVEGDKiiranNYVESTILKLVEQQ-YAVISINYTLVSkDVHFPLPVQDTKDAIRWV 147
Cdd:COG0657     2 DVYRPAGAK-GPLPVVVYFHGGGWVSGSK-----DTHDPLARRLAARAgAAVVSVDYRLAP-EHPFPAALEDAYAALRWL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 148 RKNAEKYHFDTNNIGLFGTSAGAHLSLLSAYTQDNEfiGDPelssysaKVNYVVNNFGPTDLnkllktrvgkvgafivsl 227
Cdd:COG0657    75 RANAAELGIDPDRIAVAGDSAGGHLAAALALRARDR--GGP-------RPAAQVLIYPVLDL------------------ 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 228 fskkivdlreklilgisgydinkdkrkiieyfeTISPVSY-VGSATPTLILQGNRDKIVPlhQSKILHHKLINEGVKNTL 306
Cdd:COG0657   128 ---------------------------------TASPLRAdLAGLPPTLIVTGEADPLVD--ESEALAAALRAAGVPVEL 172

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1239680976 307 TIVDGGDHGF---RTTNQAylDQLVDEMVRFI 335
Cdd:COG0657   173 HVYPGGGHGFgllAGLPEA--RAALAEIAAFL 202
PRK10162 PRK10162
acetyl esterase;
65-181 7.24e-15

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 73.98  E-value: 7.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  65 SVALDIYSPKGNSIEkfpVLIYIHGGGWVEG-----DKIIRannyvestiLKLVEQQYAVISINYTLvSKDVHFPLPVQD 139
Cdd:PRK10162   68 QVETRLYYPQPDSQA---TLFYLHGGGFILGnldthDRIMR---------LLASYSGCTVIGIDYTL-SPEARFPQAIEE 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1239680976 140 TKDAIRWVRKNAEKYHFDTNNIGLFGTSAGAHLSLLSA-YTQD 181
Cdd:PRK10162  135 IVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLALASAlWLRD 177
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 68-181 1.08e-11

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: 65.43  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  68 LDIYSPKGNSI-EKFPVLIYIHGGGWVEG-------DKIIRANNYVestilklveqqyAVISINYTL-----VSKDvHFP 134
Cdd:cd00312    81 LNVYTPKNTKPgNSLPVMVWIHGGGFMFGsgslypgDGLAREGDNV------------IVVSINYRLgvlgfLSTG-DIE 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239680976 135 LP----VQDTKDAIRWVRKNAEkyHF--DTNNIGLFGTSAGA---HLSLLSAYTQD 181
Cdd:cd00312   148 LPgnygLKDQRLALKWVQDNIA--AFggDPDSVTIFGESAGGasvSLLLLSPDSKG 201
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 272-335 1.29e-05

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 45.27  E-value: 1.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 272 TPTLILQGNRDKIVPLHQskILHHKLiNEGVknTLTIVDGGDHGFRT------TNQAYLDQLVDEMVRFI 335
Cdd:pfam20408 128 CPTLILQGERDPFGNREE--VAAYPL-PDNV--SLHWLEDGDHDFKPrkrsglTHEQNLQEAADAIAAFI 192
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
271-335 3.10e-05

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 44.10  E-value: 3.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239680976 271 ATPTLILQGNRDkivPLHQSKILHHKLINEGVknTLTIVDGGDHGFRT------TNQAYLDQLVDEMVRFI 335
Cdd:COG3571   132 TVPTLIVQGERD---PFGTPEEVAGYPLPPAI--ELVWLPGGDHDLKPrkrsgrTQEDHLAAAADAVAAWL 197
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 68-297 1.15e-76

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: 234.38  E-value: 1.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  68 LDIYSPKGNSIeKFPVLIYIHGGGWVEGDKIIRANnYVESTILKLVEQQYAVISINYTLvSKDVHFPLPVQDTKDAIRWV 147
Cdd:pfam20434   1 LDIYLPKNAKG-PYPVVIWIHGGGWNSGDKEADMG-FMTNTVKALLKAGYAVASINYRL-STDAKFPAQIQDVKAAIRFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 148 RKNAEKYHFDTNNIGLFGTSAGAHLSLLSAYTQDN-EFIGD-----PELSSYSAKVNYVVNNFGPTDLNKLLKTRVGkvg 221
Cdd:pfam20434  78 RANAAKYGIDTNKIALMGFSAGGHLALLAGLSNNNkEFEGNvgdytPESSKESFKVNAVVDFYGPTDLLDMDSCGTH--- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239680976 222 afivslfskKIVDLREKLILGisgydinKDKRKIIEYFETISPVSYV-GSATPTLILQGNRDKIVPLHQSKILHHKL 297
Cdd:pfam20434 155 ---------NDAKSPETLLLG-------APPLENPDLAKSASPITYVdKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
69-335 1.32e-41

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 143.86  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  69 DIYSPKGNSiEKFPVLIYIHGGGWVEGDKiiranNYVESTILKLVEQQ-YAVISINYTLVSkDVHFPLPVQDTKDAIRWV 147
Cdd:COG0657     2 DVYRPAGAK-GPLPVVVYFHGGGWVSGSK-----DTHDPLARRLAARAgAAVVSVDYRLAP-EHPFPAALEDAYAALRWL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 148 RKNAEKYHFDTNNIGLFGTSAGAHLSLLSAYTQDNEfiGDPelssysaKVNYVVNNFGPTDLnkllktrvgkvgafivsl 227
Cdd:COG0657    75 RANAAELGIDPDRIAVAGDSAGGHLAAALALRARDR--GGP-------RPAAQVLIYPVLDL------------------ 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 228 fskkivdlreklilgisgydinkdkrkiieyfeTISPVSY-VGSATPTLILQGNRDKIVPlhQSKILHHKLINEGVKNTL 306
Cdd:COG0657   128 ---------------------------------TASPLRAdLAGLPPTLIVTGEADPLVD--ESEALAAALRAAGVPVEL 172

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1239680976 307 TIVDGGDHGF---RTTNQAylDQLVDEMVRFI 335
Cdd:COG0657   173 HVYPGGGHGFgllAGLPEA--RAALAEIAAFL 202
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
59-335 3.35e-27

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 107.02  E-value: 3.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  59 TNGNGHSVALDIYSPKGNsiEKFPVLIYIHGGGWvegdkiIRANNYVeSTILKLVEQQYAVISINYTLVSKDVHFP--LP 136
Cdd:COG1506     3 KSADGTTLPGWLYLPADG--KKYPVVVYVHGGPG------SRDDSFL-PLAQALASRGYAVLAPDYRGYGESAGDWggDE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 137 VQDTKDAIRWVRKNAEkyhFDTNNIGLFGTSAGAHLSLLSAYTQDNEFigdpelssysaKVnyVVNNFGPTDLNKLLKTR 216
Cdd:COG1506    74 VDDVLAAIDYLAARPY---VDPDRIGIYGHSYGGYMALLAAARHPDRF-----------KA--AVALAGVSDLRSYYGTT 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 217 VGKVGAFIvslfskkivdlreklilgisgydinKDKRKIIEYFETISPVSYVGS-ATPTLILQGNRDKIVPLHQSKILHH 295
Cdd:COG1506   138 REYTERLM-------------------------GGPWEDPEAYAARSPLAYADKlKTPLLLIHGEADDRVPPEQAERLYE 192

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1239680976 296 KLINEGVKNTLTIVDGGDHGFRttnQAYLDQLVDEMVRFI 335
Cdd:COG1506   193 ALKKAGKPVELLVYPGEGHGFS---GAGAPDYLERILDFL 229
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 84-316 6.19e-19

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: 83.80  E-value: 6.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  84 LIYIHGGGWVEGDkiirANNYvESTILKLVEQ-QYAVISINYTLvSKDVHFPLPVQDTKDAIRWVRKNAEKYHFDTNNIG 162
Cdd:pfam07859   1 LVYFHGGGFVLGS----ADTH-DRLCRRLAAEaGAVVVSVDYRL-APEHPFPAAYDDAYAALRWLAEQAAELGADPSRIA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 163 LFGTSAGAHLSL-LSAYTQDNefiGDPelssysaKVNYVVNNFGPTDLNKLLKTRVGKVGAFIvSLFSKKIVDLREKLIL 241
Cdd:pfam07859  75 VAGDSAGGNLAAaVALRARDE---GLP-------KPAGQVLIYPGTDLRTESPSYLAREFADG-PLLTRAAMDWFWRLYL 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239680976 242 GISGYDinkDKRkiieyfetISPV--SYVGSATPTLILQGNRDkivPLH-QSKILHHKLINEGVKNTLTIVDGGDHGF 316
Cdd:pfam07859 144 PGADRD---DPL--------ASPLfaSDLSGLPPALVVVAEFD---PLRdEGEAYAERLRAAGVPVELIEYPGMPHGF 207
PRK10162 PRK10162
acetyl esterase;
65-181 7.24e-15

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 73.98  E-value: 7.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  65 SVALDIYSPKGNSIEkfpVLIYIHGGGWVEG-----DKIIRannyvestiLKLVEQQYAVISINYTLvSKDVHFPLPVQD 139
Cdd:PRK10162   68 QVETRLYYPQPDSQA---TLFYLHGGGFILGnldthDRIMR---------LLASYSGCTVIGIDYTL-SPEARFPQAIEE 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1239680976 140 TKDAIRWVRKNAEKYHFDTNNIGLFGTSAGAHLSLLSA-YTQD 181
Cdd:PRK10162  135 IVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLALASAlWLRD 177
COesterase pfam00135
Carboxylesterase family;
32-181 1.88e-12

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 67.72  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  32 QDPVTIQKKKSIQlfektNVSENIVYktngnghsvaLDIYSPKG--NSIEKFPVLIYIHGGGWVEGDkiirANNYVESTI 109
Cdd:pfam00135  67 QNGDLTSPGSSGL-----EGSEDCLY----------LNVYTPKElkENKNKLPVMVWIHGGGFMFGS----GSLYDGSYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 110 LK---LVeqqyaVISINYTL------VSKDVHFP--LPVQDTKDAIRWVRKNAEkyHF--DTNNIGLFGTSAGA---HLS 173
Cdd:pfam00135 128 AAegdVI-----VVTINYRLgplgflSTGDDEAPgnYGLLDQVLALRWVQENIA--SFggDPNRVTLFGESAGAasvSLL 200


                  ....*...
gi 1239680976 174 LLSAYTQD 181
Cdd:pfam00135 201 LLSPLSKG 208
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 59-329 5.94e-12

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 64.94  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  59 TNGNGHSVALDIYSPKGNSiEKFPVLIYIHGGGwveGDKIIRANnYVEstilKLVEQQYAVISINY-----------TLV 127
Cdd:COG1073    16 KSRDGIKLAGDLYLPAGAS-KKYPAVVVAHGNG---GVKEQRAL-YAQ----RLAELGFNVLAFDYrgygesegeprEEG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 128 SKDVhfplpvQDTKDAIRWVRknaEKYHFDTNNIGLFGTSAGAHLSLLSAYTqdnefigDPELSSYSAKVnyvvnnfGPT 207
Cdd:COG1073    87 SPER------RDARAAVDYLR---TLPGVDPERIGLLGISLGGGYALNAAAT-------DPRVKAVILDS-------PFT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 208 DLNKLLKTRVGKVGAFIVSLFSKKIVDLREKLILgiSGYDinkdkrkIIEYFETISpvsyvgsaTPTLILQGNRDKIVPL 287
Cdd:COG1073   144 SLEDLAAQRAKEARGAYLPGVPYLPNVRLASLLN--DEFD-------PLAKIEKIS--------RPLLFIHGEKDEAVPF 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1239680976 288 HQSKILhHKLINEgvKNTLTIVDGGDH--GFRTTNQAYLDQLVD 329
Cdd:COG1073   207 YMSEDL-YEAAAE--PKELLIVPGAGHvdLYDRPEEEYFDKLAE 247
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 68-181 1.08e-11

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: 65.43  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  68 LDIYSPKGNSI-EKFPVLIYIHGGGWVEG-------DKIIRANNYVestilklveqqyAVISINYTL-----VSKDvHFP 134
Cdd:cd00312    81 LNVYTPKNTKPgNSLPVMVWIHGGGFMFGsgslypgDGLAREGDNV------------IVVSINYRLgvlgfLSTG-DIE 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239680976 135 LP----VQDTKDAIRWVRKNAEkyHF--DTNNIGLFGTSAGA---HLSLLSAYTQD 181
Cdd:cd00312   148 LPgnygLKDQRLALKWVQDNIA--AFggDPDSVTIFGESAGGasvSLLLLSPDSKG 201
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
68-177 4.08e-07

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 51.43  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  68 LDIYSPKGNSIEKFPVLIYIHGGGWVEGdkiirannyveSTIL------KLVEQQYAVISINYTL----------VSKDV 131
Cdd:COG2272    92 LNVWTPALAAGAKLPVMVWIHGGGFVSG-----------SGSEplydgaALARRGVVVVTINYRLgalgflalpaLSGES 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1239680976 132 HFPLP---VQDTKDAIRWVRKNAEKyhF--DTNNIGLFGTSAGAH--LSLLSA 177
Cdd:COG2272   161 YGASGnygLLDQIAALRWVRDNIAA--FggDPDNVTIFGESAGAAsvAALLAS 211
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
141-328 1.98e-06

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 47.99  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 141 KDAIRWVRKNAEKYHFDTNNIGLFGTSAGAHLSLLSAyTQDNEFigdpelssYSAKVNYVvnnfGPTDLnkllktrvgkv 220
Cdd:pfam00326  46 DDFIAAAEYLIEQGYTDPDRLAIWGGSYGGYLTGAAL-NQRPDL--------FKAAVAHV----PVVDW----------- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 221 gafiVSLFSKKIVDLREKLIlgisGYDINKDKRKIIEYFETISPVSYVGSATPTLILQGNRDKIVPLHQSKILHHKLINE 300
Cdd:pfam00326 102 ----LAYMSDTSLPFTERYM----EWGNPWDNEEGYDYLSPYSPADNVKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRK 173

                         170       180
                  ....*....|....*....|....*....
gi 1239680976 301 GVKNTLTIVDGGDHGFRT-TNQAYLDQLV 328
Cdd:pfam00326 174 GVPFLLLIFPDEGHGIGKpRNKVEEYARE 202
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
62-335 8.11e-06

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 46.15  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  62 NGHSVALDIYSPKGNSiekFPVLIYIHGGGWvegdkiiRANNYvESTILKLVEQQYAVISINY-------TLVSKDVHFP 134
Cdd:COG2267    12 DGLRLRGRRWRPAGSP---RGTVVLVHGLGE-------HSGRY-AELAEALAAAGYAVLAFDLrghgrsdGPRGHVDSFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 135 LPVQDTKDAIRWVRKNAEKyhfdtnNIGLFGTSAGAHLSLLSAYTQDNEFIGdpelssysakvnYVVNnfGPTDLNK-LL 213
Cdd:COG2267    81 DYVDDLRAALDALRARPGL------PVVLLGHSMGGLIALLYAARYPDRVAG------------LVLL--APAYRADpLL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 214 KTRVGKVGAFIVSLFSKKIvdlreklilgisgydinkdkrkiieyfetispvsyvgsATPTLILQGNRDKIVPLHQSKIL 293
Cdd:COG2267   141 GPSARWLRALRLAEALARI--------------------------------------DVPVLVLHGGADRVVPPEAARRL 182

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1239680976 294 HHKLINEGvknTLTIVDGGDHGFrtTNQAYLDQLVDEMVRFI 335
Cdd:COG2267   183 AARLSPDV---ELVLLPGARHEL--LNEPAREEVLAAILAWL 219
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 272-335 1.29e-05

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 45.27  E-value: 1.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 272 TPTLILQGNRDKIVPLHQskILHHKLiNEGVknTLTIVDGGDHGFRT------TNQAYLDQLVDEMVRFI 335
Cdd:pfam20408 128 CPTLILQGERDPFGNREE--VAAYPL-PDNV--SLHWLEDGDHDFKPrkrsglTHEQNLQEAADAIAAFI 192
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
271-335 3.10e-05

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 44.10  E-value: 3.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239680976 271 ATPTLILQGNRDkivPLHQSKILHHKLINEGVknTLTIVDGGDHGFRT------TNQAYLDQLVDEMVRFI 335
Cdd:COG3571   132 TVPTLIVQGERD---PFGTPEEVAGYPLPPAI--ELVWLPGGDHDLKPrkrsgrTQEDHLAAAADAVAAWL 197
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
63-181 3.51e-05

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 44.64  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  63 GHSVALDIYSPKGNSiEKFPVLI----YIHGGGWVEGDKIIRANnyvestiLKLVEQQYAVISinYTLVSK-------DV 131
Cdd:pfam02129   2 GVRLAADIYRPTKTG-GPVPALLtrspYGARRDGASDLALAHPE-------WEFAARGYAVVY--QDVRGTggsegvfTV 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1239680976 132 HFPLPVQDTKDAIRWVRKNAEkyhfDTNNIGLFGTSAGAHLSLLSAYTQD 181
Cdd:pfam02129  72 GGPQEAADGKDVIDWLAGQPW----CNGKVGMTGISYLGTTQLAAAATGP 117
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
 270-330 2.00e-04

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 40.01  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239680976 270 SATPTLILQGNRDKIVPLHQSKILHHKLINegvkNTLTIVDGGDHGFRTTNQAYLDQLVDE 330
Cdd:pfam08386  32 GAPPVLLVQGERDPATPYEGARELARALGG----AVLVTVQGAGHGAYIGGNACVDKAVDA 88
COG4099 COG4099
Predicted peptidase [General function prediction only];
53-340 2.01e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 42.26  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976  53 ENIVYKTNGNGHSVALDIYSPKG-NSIEKFPVLIYIHGGGWVEGD----KIIRANNYVESTILKlvEQQYAVISINYTLV 127
Cdd:COG4099    20 EARTFTDPSDGDTLPYRLYLPKGyDPGKKYPLVLFLHGAGERGTDnekqLTHGAPKFINPENQA--KFPAIVLAPQCPED 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 128 SKDVHfPLPVQDTKDAIRWVRKNaekYHFDTNNIGLFGTSAGAH--LSLLSAYtqdnefigdPELssYSAKVnyVVNNFG 205
Cdd:COG4099    98 DYWSD-TKALDAVLALLDDLIAE---YRIDPDRIYLTGLSMGGYgtWDLAARY---------PDL--FAAAV--PICGGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 206 -PTDLNKLLKtrvgkvgafivslfskkivdlreklilgisgydinkdkrkiieyfetispvsyvgsaTPTLILQGNRDKI 284
Cdd:COG4099   161 dPANAANLKK---------------------------------------------------------VPVWIFHGAKDDV 183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239680976 285 VPLHQSKILHHKLINEGVKNTLTIVDGGDHGfrTTNQAYLDQlvdEMVRFIISQKK 340
Cdd:COG4099   184 VPVEESRAMVEALKAAGADVKYTEYPGVGHN--SWDPAYANP---DLYDWLFAQKR 234
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
137-335 1.48e-03

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 39.54  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 137 VQDTKDAIRWVRKNAEKyhfdtnnIGLFGTSAGAHLSLLSAYtQDNEFIGdpeLSSYSAKVNYVVNNFGPTDLNKLLKTR 216
Cdd:COG1647    69 LEDVEEAYEILKAGYDK-------VIVIGLSMGGLLALLLAA-RYPDVAG---LVLLSPALKIDDPSAPLLPLLKYLARS 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239680976 217 VGKVGAFIVSLFSKKIVDLREKLILGISGYDINKDKRKiieYFETISpvsyvgsaTPTLILQGNRDKIVPLHQSKILHHK 296
Cdd:COG1647   138 LRGIGSDIEDPEVAEYAYDRTPLRALAELQRLIREVRR---DLPKIT--------APTLIIQSRKDEVVPPESARYIYER 206

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1239680976 297 LINEGVKntLTIVDGGDHGFRTTNQAylDQLVDEMVRFI 335
Cdd:COG1647   207 LGSPDKE--LVWLEDSGHVITLDKDR--EEVAEEILDFL 241
 
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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