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Conserved domains on  [gi|495186058|ref|WP_007910848|]
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MULTISPECIES: alpha/beta fold hydrolase [unclassified Pseudomonas]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2-272 6.79e-63

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 197.15  E-value: 6.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   2 STFTTQDGTEIYYKDWG-SGKPVLFSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQL 80
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  81 INHLDLRDVTLVGFSMGGGdVSRYIARHGSERVAGLVLLGAVtplfgkkadfpqgvdtsvfdgikagllqdRAQFIADFA 160
Cdd:COG0596   83 LDALGLERVVLVGHSMGGM-VALELAARHPERVAGLVLVDEV-----------------------------LAALAEPLR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 161 APFYGtnqgqkvsagvltqtlnvallasLKGTVDCVTAFSETDFRPDMAKIDVPTLVIHGDGDQIVPFEtTGKQAAAQIK 240
Cdd:COG0596  133 RPGLA-----------------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPA-LARRLAELLP 188
                        250       260       270
                 ....*....|....*....|....*....|..
gi 495186058 241 GAELKVYAGAPHGFAVTHAQALNEDLLAFLKR 272
Cdd:COG0596  189 NAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2-272 6.79e-63

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 197.15  E-value: 6.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   2 STFTTQDGTEIYYKDWG-SGKPVLFSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQL 80
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  81 INHLDLRDVTLVGFSMGGGdVSRYIARHGSERVAGLVLLGAVtplfgkkadfpqgvdtsvfdgikagllqdRAQFIADFA 160
Cdd:COG0596   83 LDALGLERVVLVGHSMGGM-VALELAARHPERVAGLVLVDEV-----------------------------LAALAEPLR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 161 APFYGtnqgqkvsagvltqtlnvallasLKGTVDCVTAFSETDFRPDMAKIDVPTLVIHGDGDQIVPFEtTGKQAAAQIK 240
Cdd:COG0596  133 RPGLA-----------------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPA-LARRLAELLP 188
                        250       260       270
                 ....*....|....*....|....*....|..
gi 495186058 241 GAELKVYAGAPHGFAVTHAQALNEDLLAFLKR 272
Cdd:COG0596  189 NAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
21-252 3.08e-37

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 131.86  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   21 KPVLFSHGWPLDADMWEYQMEYLSSRGYRTIAFDRRGFGRSDQPWTGYDY--DTFADDIAQLINHLDLRDVTLVGFSMGG 98
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   99 GDVSRYIARHgSERVAGLVLLGAVTP--LFGKKADFPQGVDTSVFDGIKAGLLQDR-AQFIADFAAPFYGTNQGQKVSAG 175
Cdd:pfam00561  81 LIALAYAAKY-PDRVKALVLLGALDPphELDEADRFILALFPGFFDGFVADFAPNPlGRLVAKLLALLLLRLRLLKALPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  176 VLTQTLNV-ALLASLKGT--VDCVTAFSETDFRPDMAKIDVPTLVIHGDGDQIVPfETTGKQAAAQIKGAELKVYAGAPH 252
Cdd:pfam00561 160 LNKRFPSGdYALAKSLVTgaLLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVP-PQALEKLAQLFPNARLVVIPDAGH 238
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
11-271 2.07e-27

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 106.29  E-value: 2.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   11 EIYYKDWG--SGKPVL-FSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQLINHLDLR 87
Cdd:TIGR02427   1 RLHYRLDGaaDGAPVLvFINSLGTDLRMWDPVLPALT-PDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   88 DVTLVGFSMGGGdVSRYIARHGSERVAGLVLLGAvTPLFGKKADFPQGVDTSVFDGIKAglLQDRAQ---FIADFAAPfy 164
Cdd:TIGR02427  80 RAVFCGLSLGGL-IAQGLAARRPDRVRALVLSNT-AAKIGTPESWNARIAAVRAEGLAA--LADAVLerwFTPGFREA-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  165 gTNQGQKVSAGVLTQTlnvallaSLKGTVDCVTAFSETDFRPDMAKIDVPTLVIHGDGDQIVPFEtTGKQAAAQIKGAEL 244
Cdd:TIGR02427 154 -HPARLDLYRNMLVRQ-------PPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPE-LVREIADLVPGARF 224
                         250       260
                  ....*....|....*....|....*..
gi 495186058  245 KVYAGAPHGFAVTHAQALNEDLLAFLK 271
Cdd:TIGR02427 225 AEIRGAGHIPCVEQPEAFNAALRDFLR 251
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
9-136 7.70e-19

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 83.89  E-value: 7.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   9 GTEIYYKDWGSGKPVLFSHGWPLDADMWEYQMEYLSSRGyRTIAFDRRGFGRSDQPWTGYdydTFADDIAQL---INHLD 85
Cdd:PRK03592  16 GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIDY---TFADHARYLdawFDALG 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495186058  86 LRDVTLVGFSMGGGDVSRYIARHgSERVAGLVLL-GAVTPLFGkkADFPQGV 136
Cdd:PRK03592  92 LDDVVLVGHDWGSALGFDWAARH-PDRVRGIAFMeAIVRPMTW--DDFPPAV 140
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2-272 6.79e-63

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 197.15  E-value: 6.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   2 STFTTQDGTEIYYKDWG-SGKPVLFSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQL 80
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  81 INHLDLRDVTLVGFSMGGGdVSRYIARHGSERVAGLVLLGAVtplfgkkadfpqgvdtsvfdgikagllqdRAQFIADFA 160
Cdd:COG0596   83 LDALGLERVVLVGHSMGGM-VALELAARHPERVAGLVLVDEV-----------------------------LAALAEPLR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 161 APFYGtnqgqkvsagvltqtlnvallasLKGTVDCVTAFSETDFRPDMAKIDVPTLVIHGDGDQIVPFEtTGKQAAAQIK 240
Cdd:COG0596  133 RPGLA-----------------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPA-LARRLAELLP 188
                        250       260       270
                 ....*....|....*....|....*....|..
gi 495186058 241 GAELKVYAGAPHGFAVTHAQALNEDLLAFLKR 272
Cdd:COG0596  189 NAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
21-252 3.08e-37

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 131.86  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   21 KPVLFSHGWPLDADMWEYQMEYLSSRGYRTIAFDRRGFGRSDQPWTGYDY--DTFADDIAQLINHLDLRDVTLVGFSMGG 98
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   99 GDVSRYIARHgSERVAGLVLLGAVTP--LFGKKADFPQGVDTSVFDGIKAGLLQDR-AQFIADFAAPFYGTNQGQKVSAG 175
Cdd:pfam00561  81 LIALAYAAKY-PDRVKALVLLGALDPphELDEADRFILALFPGFFDGFVADFAPNPlGRLVAKLLALLLLRLRLLKALPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  176 VLTQTLNV-ALLASLKGT--VDCVTAFSETDFRPDMAKIDVPTLVIHGDGDQIVPfETTGKQAAAQIKGAELKVYAGAPH 252
Cdd:pfam00561 160 LNKRFPSGdYALAKSLVTgaLLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVP-PQALEKLAQLFPNARLVVIPDAGH 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
3-272 1.23e-34

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 124.34  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   3 TFTTQDGTEIYYKDW----GSGKPVLFSHGWPLDADMWEYQMEYLSSRGYRTIAFDRRGFGRSDQPwTGY--DYDTFADD 76
Cdd:COG2267    7 TLPTRDGLRLRGRRWrpagSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGP-RGHvdSFDDYVDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  77 IAQLINHLDLR---DVTLVGFSMGGGDVSRYIARHGsERVAGLVLLgavtplfgkkadfpqgvdtsvfdgikagllqdra 153
Cdd:COG2267   86 LRAALDALRARpglPVVLLGHSMGGLIALLYAARYP-DRVAGLVLL---------------------------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 154 qfiadfaAPFYGTNQGQKVSAGVLtqtlnvallaslkgtvdcvtafSETDFRPDMAKIDVPTLVIHGDGDQIVPFETTGK 233
Cdd:COG2267  131 -------APAYRADPLLGPSARWL----------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARR 181
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 495186058 234 QAAAQIKGAELKVYAGAPHGFAV-THAQALNEDLLAFLKR 272
Cdd:COG2267  182 LAARLSPDVELVLLPGARHELLNePAREEVLAAILAWLER 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
11-271 2.07e-27

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 106.29  E-value: 2.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   11 EIYYKDWG--SGKPVL-FSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQLINHLDLR 87
Cdd:TIGR02427   1 RLHYRLDGaaDGAPVLvFINSLGTDLRMWDPVLPALT-PDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   88 DVTLVGFSMGGGdVSRYIARHGSERVAGLVLLGAvTPLFGKKADFPQGVDTSVFDGIKAglLQDRAQ---FIADFAAPfy 164
Cdd:TIGR02427  80 RAVFCGLSLGGL-IAQGLAARRPDRVRALVLSNT-AAKIGTPESWNARIAAVRAEGLAA--LADAVLerwFTPGFREA-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  165 gTNQGQKVSAGVLTQTlnvallaSLKGTVDCVTAFSETDFRPDMAKIDVPTLVIHGDGDQIVPFEtTGKQAAAQIKGAEL 244
Cdd:TIGR02427 154 -HPARLDLYRNMLVRQ-------PPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPE-LVREIADLVPGARF 224
                         250       260
                  ....*....|....*....|....*..
gi 495186058  245 KVYAGAPHGFAVTHAQALNEDLLAFLK 271
Cdd:TIGR02427 225 AEIRGAGHIPCVEQPEAFNAALRDFLR 251
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
3-272 4.89e-27

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 104.71  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   3 TFTTQDGTEIY---YKDWGSGKP--VLFSHGWPLDAD-MWEYQMEYLSSRGYRTIAFDRRGFGRSDQPWTGYDYDTFADD 76
Cdd:COG1506    1 TFKSADGTTLPgwlYLPADGKKYpvVVYVHGGPGSRDdSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  77 IAQLINH--LDLRDVTLVGFSMGGGDVSRYIARHgSERVAGLVLLGAVTPLFGkkadfpQGVDTSVFDGIKAGLLQDRAQ 154
Cdd:COG1506   81 IDYLAARpyVDPDRIGIYGHSYGGYMALLAAARH-PDRFKAAVALAGVSDLRS------YYGTTREYTERLMGGPWEDPE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 155 FIADFAAPFYgtnqgqkvsagvltqtlnvallaslkgtvdcvtafsetdfrpdMAKIDVPTLVIHGDGDQIVPFETTGK- 233
Cdd:COG1506  154 AYAARSPLAY-------------------------------------------ADKLKTPLLLIHGEADDRVPPEQAERl 190
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 495186058 234 QAAAQIKG--AELKVYAGAPHGFAVTHAQALNEDLLAFLKR 272
Cdd:COG1506  191 YEALKKAGkpVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
41-252 2.50e-22

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 92.28  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   41 EYLSSRGYRTIAFDRRGFGRSDQPwTGY--DYDTFADDIAQLINHLDLR----DVTLVGFSMGGGDVSRYIARHgSERVA 114
Cdd:pfam12146  25 DALAAQGFAVYAYDHRGHGRSDGK-RGHvpSFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRY-PDKVD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  115 GLVLLGavtPLFGKKADFPQGV-------------DTSVFDGIKAGLLQDRAQFIADFAA-PFYGTnqgqKVSAGvltqt 180
Cdd:pfam12146 103 GLILSA---PALKIKPYLAPPIlkllakllgklfpRLRVPNNLLPDSLSRDPEVVAAYAAdPLVHG----GISAR----- 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495186058  181 lnvALLASLKGTVDCVtafsetdfrPDMAKIDVPTLVIHGDGDQIVPFETTGK-QAAAQIKGAELKVYAGAPH 252
Cdd:pfam12146 171 ---TLYELLDAGERLL---------RRAAAITVPLLLLHGGADRVVDPAGSREfYERAGSTDKTLKLYPGLYH 231
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
9-136 7.70e-19

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 83.89  E-value: 7.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   9 GTEIYYKDWGSGKPVLFSHGWPLDADMWEYQMEYLSSRGyRTIAFDRRGFGRSDQPWTGYdydTFADDIAQL---INHLD 85
Cdd:PRK03592  16 GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIDY---TFADHARYLdawFDALG 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495186058  86 LRDVTLVGFSMGGGDVSRYIARHgSERVAGLVLL-GAVTPLFGkkADFPQGV 136
Cdd:PRK03592  92 LDDVVLVGHDWGSALGFDWAARH-PDRVRGIAFMeAIVRPMTW--DDFPPAV 140
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
3-272 2.81e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 81.50  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   3 TFTTQDGTEI----YYKDWGSGKP--VLFSHGWPLDADMWEYQMEYLSSRGYRTIAFDRRGFGRSDQPWTGY-DYDTFad 75
Cdd:COG1073   14 TFKSRDGIKLagdlYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEgSPERR-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  76 DIAQLINHLDLRD------VTLVGFSMGGGDVSRYIARHgsERVAGLVLLGAVTplfgkkadfpqgvdtsvfdgikagll 149
Cdd:COG1073   92 DARAAVDYLRTLPgvdperIGLLGISLGGGYALNAAATD--PRVKAVILDSPFT-------------------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 150 qDRAQFIADFAAPFYGTNQGqkvsagvltqtlNVALLASLKgtvdcVTAFSETDFRP--DMAKIDVPTLVIHGDGDQIVP 227
Cdd:COG1073  144 -SLEDLAAQRAKEARGAYLP------------GVPYLPNVR-----LASLLNDEFDPlaKIEKISRPLLFIHGEKDEAVP 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 495186058 228 FEtTGKQAAAQIKGA-ELKVYAGAPH--GFAVTHAQALnEDLLAFLKR 272
Cdd:COG1073  206 FY-MSEDLYEAAAEPkELLIVPGAGHvdLYDRPEEEYF-DKLAEFFKK 251
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
8-272 9.11e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 78.83  E-value: 9.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   8 DGTEIYYKDWG--SGKPVLFSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQLINHLD 85
Cdd:PRK14875 117 GGRTVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALG 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  86 LRDVTLVGFSMGGGdVSRYIARHGSERVAGLVLLGAvtplfgkkadfpqgvdtsvfdgikAGLLQD-RAQFIADFAApfy 164
Cdd:PRK14875 196 IERAHLVGHSMGGA-VALRLAARAPQRVASLTLIAP------------------------AGLGPEiNGDYIDGFVA--- 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 165 GTNQGQKVS--------AGVLTQTLNVALLAS--LKGTVDCVTAFSET---------DFRPDMAKIDVPTLVIHGDGDQI 225
Cdd:PRK14875 248 AESRRELKPvlellfadPALVTRQMVEDLLKYkrLDGVDDALRALADAlfaggrqrvDLRDRLASLAIPVLVIWGEQDRI 327
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 495186058 226 VPFettgKQAAAQIKGAELKVYAGAPHGFAVTHAQALNEDLLAFLKR 272
Cdd:PRK14875 328 IPA----AHAQGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
17-272 2.32e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 70.74  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  17 WGSGKPVLFSHGW---PLDADMWeyqMEYLSSRGYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQLINHLDLR--DVTL 91
Cdd:COG1647   12 EGGRKGVLLLHGFtgsPAEMRPL---AEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  92 VGFSMGGGdVSRYIARHGSErVAGLVLLGAvtPLFgkkadfpqgvdtsvFDGIKAgLLQDRAQFIADFAAPFYGTNQGQK 171
Cdd:COG1647   89 IGLSMGGL-LALLLAARYPD-VAGLVLLSP--ALK--------------IDDPSA-PLLPLLKYLARSLRGIGSDIEDPE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 172 VSAGVLTQTlNVALLASLKGTVDcvtafsetDFRPDMAKIDVPTLVIHGDGDQIVPFETTgKQAAAQIKGA--ELKVYAG 249
Cdd:COG1647  150 VAEYAYDRT-PLRALAELQRLIR--------EVRRDLPKITAPTLIIQSRKDEVVPPESA-RYIYERLGSPdkELVWLED 219
                        250       260
                 ....*....|....*....|....
gi 495186058 250 APHGFAV-THAQALNEDLLAFLKR 272
Cdd:COG1647  220 SGHVITLdKDREEVAEEILDFLER 243
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
23-264 5.55e-13

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 66.34  E-value: 5.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   23 VLFSHGWPLDADmweyQMEYLSSRGYRTIAFDRRGFGRSDQPWtgYDYDTFADDIAQLINHLDLRDVTLVGFSMGGGDVS 102
Cdd:pfam12697   1 VVLVHGAGLSAA----PLAALLAAGVAVLAPDLPGHGSSSPPP--LDLADLADLAALLDELGAARPVVLVGHSLGGAVAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  103 RYIARhgsERVAGLVLLGAVTPLFGKKADFPqgvdtsvfdgikaglLQDRAQFIADFAAPFYGTNQGQKVSAGVLTQTLN 182
Cdd:pfam12697  75 AAAAA---ALVVGVLVAPLAAPPGLLAALLA---------------LLARLGAALAAPAWLAAESLARGFLDDLPADAEW 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  183 VALLASLKGTVDCVTAFSETDFRPdmakIDVPTLVIHGDgDQIVPFETtgKQAAAQIKGAELKVYAGAPHgFAVTHAQAL 262
Cdd:pfam12697 137 AAALARLAALLAALALLPLAAWRD----LPVPVLVLAEE-DRLVPELA--QRLLAALAGARLVVLPGAGH-LPLDDPEEV 208

                  ..
gi 495186058  263 NE 264
Cdd:pfam12697 209 AE 210
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
22-124 5.94e-13

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 63.70  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  22 PVLFSHGWPLDADMWEYQMEYLSSRGYRTIAFDrrgfgrsdQPWTGYDYDTFADDIAQLINHLDLRD----VTLVGFSMG 97
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRLRAAGYPVYALN--------YPSTNGSIEDSAEQLAAFVDAVLAATgaekVDLVGHSMG 78
                         90       100
                 ....*....|....*....|....*...
gi 495186058  98 GGDVSRYIARH-GSERVAGLVLLGavTP 124
Cdd:COG1075   79 GLVARYYLKRLgGAAKVARVVTLG--TP 104
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
11-272 1.27e-12

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 65.81  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  11 EIYYKDWGSGK-PVLFSHGWPLDADMWEYQMEYLSSRgYRTIAFDRRGFGRSdqpwTGYDYDTFADDIAQLINHLDLRDV 89
Cdd:PRK10349   3 NIWWQTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSH-FTLHLVDLPGFGRS----RGFGALSLADMAEAVLQQAPDKAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  90 TLvGFSMgGGDVSRYIARHGSERVAGLVLLgAVTPLFGKKADFPqGVDTSVFDGIKAGLLQDRAQFIADF-AAPFYGTNQ 168
Cdd:PRK10349  78 WL-GWSL-GGLVASQIALTHPERVQALVTV-ASSPCFSARDEWP-GIKPDVLAGFQQQLSDDFQRTVERFlALQTMGTET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 169 GQKVSagvltQTLNVALLASLKGTVDCVTAFSE----TDFRPDMAKIDVPTLVIHGDGDQIVP------FETTGKQAAAQ 238
Cdd:PRK10349 154 ARQDA-----RALKKTVLALPMPEVDVLNGGLEilktVDLRQPLQNVSMPFLRLYGYLDGLVPrkvvpmLDKLWPHSESY 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 495186058 239 IkgaelkvYAGAPHGFAVTHAQALNEDLLAFLKR 272
Cdd:PRK10349 229 I-------FAKAAHAPFISHPAEFCHLLVALKQR 255
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
4-118 5.19e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 64.49  E-value: 5.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   4 FTTQDGtEIYYKDWGSGKPVLFSHGWPLDADMWEYQMEYLSSRgYRTIAFDRRGFGRSDQPWT-GYDYDTFADDIAQLIN 82
Cdd:PRK03204  19 FDSSRG-RIHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDR-FRCVAPDYLGFGLSERPSGfGYQIDEHARVIGEFVD 96
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495186058  83 HLDLRDVTLVGFSMgGGDVSRYIARHGSERVAGLVL 118
Cdd:PRK03204  97 HLGLDRYLSMGQDW-GGPISMAVAVERADRVRGVVL 131
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
8-163 3.98e-11

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 61.91  E-value: 3.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   8 DGTEI--YYKDWGS--GKPVLFSHGWPldadMWEY----QMEYLSSRGYRTIAFDRRGFGRSDQPW--TGYDYDTFADDI 77
Cdd:PRK00870  30 DGGPLrmHYVDEGPadGPPVLLLHGEP----SWSYlyrkMIPILAAAGHRVIAPDLIGFGRSDKPTrrEDYTYARHVEWM 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  78 AQLINHLDLRDVTLVGFSMGGGDVSRYIARHGsERVAGLVLL--------GAVTPLFGKKADFPQgvDTSVFDG---IKA 146
Cdd:PRK00870 106 RSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHP-DRFARLVVAntglptgdGPMPDAFWAWRAFSQ--YSPVLPVgrlVNG 182
                        170
                 ....*....|....*...
gi 495186058 147 GLLQD-RAQFIADFAAPF 163
Cdd:PRK00870 183 GTVRDlSDAVRAAYDAPF 200
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-271 1.68e-10

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 59.59  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   3 TFTTQDGTEI---YYKDWGSGK--PVLFSHGWP-LDADMWEYqMEYLSSRGYRTIAFDRRGFG-------RSDQPWTGYD 69
Cdd:COG0412    7 TIPTPDGVTLpgyLARPAGGGPrpGVVVLHEIFgLNPHIRDV-ARRLAAAGYVVLAPDLYGRGgpgddpdEARALMGALD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  70 YDTFADDIAQLINHL------DLRDVTLVGFSMGGGdvsryiarhgservagLVLLGAVTplfgkkadfpqgvdtsvFDG 143
Cdd:COG0412   86 PELLAADLRAALDWLkaqpevDAGRVGVVGFCFGGG----------------LALLAAAR-----------------GPD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 144 IKAgllqdraqfiadfAAPFYGTNQGqkvsagvltqtlnvallaslkgtvdcvtafseTDFRPDMAKIDVPTLVIHGDGD 223
Cdd:COG0412  133 LAA-------------AVSFYGGLPA--------------------------------DDLLDLAARIKAPVLLLYGEKD 167
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 224 QIVPFETTgKQAAAQIKGA----ELKVYAGAPHGFAVTHAQALNED--------LLAFLK 271
Cdd:COG0412  168 PLVPPEQV-AALEAALAAAgvdvELHVYPGAGHGFTNPGRPRYDPAaaedawqrTLAFLA 226
PRK05855 PRK05855
SDR family oxidoreductase;
3-114 2.73e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 60.38  E-value: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   3 TFTTQDGTEIYYKDWG--SGKPVLFSHGWPLDADMWEYQMEYLSSRgYRTIAFDRRGFGRSDQPWT--GYDYDTFADDIA 78
Cdd:PRK05855   6 TVVSSDGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLADR-FRVVAYDVRGAGRSSAPKRtaAYTLARLADDFA 84
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495186058  79 QLINHLDL-RDVTLVGFSMGGGDVSRYIARHGSE-RVA 114
Cdd:PRK05855  85 AVIDAVSPdRPVHLLAHDWGSIQGWEAVTRPRAAgRIA 122
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
23-252 6.50e-10

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 58.58  E-value: 6.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  23 VLFSHGWPLDADMWEYQMEYLSSRGYRTIAFD------RRGFGRSDQPWTGYDYDTFAD---DIAQLINHL--------- 84
Cdd:COG4188   65 VVLSHGLGGSREGYAYLAEHLASHGYVVAAPDhpgsnaADLSAALDGLADALDPEELWErplDLSFVLDQLlalnksdpp 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  85 -----DLRDVTLVGFSMGGgdvsryiarhgserVAGLVLLGAvtplfgkKADFPQGVDTSVFDGIKAGLLQDRAQFIADF 159
Cdd:COG4188  145 lagrlDLDRIGVIGHSLGG--------------YTALALAGA-------RLDFAALRQYCGKNPDLQCRALDLPRLAYDL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 160 AAPfygtnqgqKVSAGVLtqtlnVALLASLkgtvdcvtAFSETDFrpdmAKIDVPTLVIHGDGDQIVPFETTGKQAAAQI 239
Cdd:COG4188  204 RDP--------RIKAVVA-----LAPGGSG--------LFGEEGL----AAITIPVLLVAGSADDVTPAPDEQIRPFDLL 258
                        250
                 ....*....|....*
gi 495186058 240 KGAE--LKVYAGAPH 252
Cdd:COG4188  259 PGADkyLLTLEGATH 273
PLN02578 PLN02578
hydrolase
4-121 1.27e-09

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 57.93  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   4 FTTQDGTEIYYKDWGSGKPVLFSHGWPLDADMWEYQMEYLSSRgYRTIAFDRRGFGRSDQPWTGYDYDTFADDIAQLINH 83
Cdd:PLN02578  70 FWTWRGHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKE 148
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495186058  84 LDLRDVTLVGFSMGGGdVSRYIARHGSERVAGLVLLGA 121
Cdd:PLN02578 149 VVKEPAVLVGNSLGGF-TALSTAVGYPELVAGVALLNS 185
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
22-133 1.23e-08

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 54.89  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  22 PVLFSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPWTGY--DY--DTFADDIAQLINHLDLRDVTLVGFSMG 97
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLS-KNYHAIAFDWLGFGFSDKPQPGYgfNYtlDEYVSSLESLIDELKSDKVSLVVQGYF 207
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495186058  98 GGDVSRYIARHgSERVAGLVLLGAvtPLFGKKADFP 133
Cdd:PLN03084 208 SPPVVKYASAH-PDKIKKLILLNP--PLTKEHAKLP 240
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
43-272 1.50e-06

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 47.46  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  43 LSSRGYRTIAFDRRGFGRSDqpwtG-YDY-DTFADDIAQLINHL---DLRDVTLVGFSMGGgdvsrYIA-RHGSER--VA 114
Cdd:COG2945   51 LVAAGFAVLRFNFRGVGRSE----GeFDEgRGELDDAAAALDWLraqNPLPLWLAGFSFGA-----YVAlQLAMRLpeVE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058 115 GLVLLGavTPLfgKKADFPqgvdtsvfdgikagllqdraqfiadfaapfygtnqgqkvsagvltqtlnvallaslkgtvd 194
Cdd:COG2945  122 GLILVA--PPV--NRYDFS------------------------------------------------------------- 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495186058 195 cvtafsetdfrpDMAKIDVPTLVIHGDGDQIVPFETTGKQAAAQIKGAELKVYAGAPHGFaVTHAQALNEDLLAFLKR 272
Cdd:COG2945  137 ------------FLAPCPAPTLVIHGEQDEVVPPAEVLDWARPLSPPLPVVVVPGADHFF-HGKLDELKELVARYLPR 201
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
210-272 1.88e-05

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 44.53  E-value: 1.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495186058  210 KIDVPTLVIHGDGDQIVPFETTGKQAAAQI---KGAELKVYAGAPHGFA-VTHAQALNEDLLAFLKR 272
Cdd:pfam00326 142 KVYPPLLLIHGLLDDRVPPWQSLKLVAALQrkgVPFLLLIFPDEGHGIGkPRNKVEEYARELAFLLE 208
DLH pfam01738
Dienelactone hydrolase family;
185-264 5.21e-05

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 43.11  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  185 LLASLKGTVDCVTAFSETDFRPDMA---KIDVPTLVIHGDGDQIVPFE----TTGKQAAAQIKgAELKVYAGAPHGFAVT 257
Cdd:pfam01738 112 LLAAKGPLVDAAVGFYGVGPEPPLIeapDIKAPILFHFGEEDHFVPADsrelIEEALKAANVD-HQIHSYPGAGHAFAND 190

                  ....*..
gi 495186058  258 HAQALNE 264
Cdd:pfam01738 191 SRPSYNA 197
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
20-119 3.53e-04

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 41.77  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   20 GKPVLFSHGWPLDADMWEYQMEYLSSRGyRTIAFDRRGFGRS--------DQPWTGYDYDTFADDIAQLINHLDLRDVTL 91
Cdd:PLN02980 1371 GSVVLFLHGFLGTGEDWIPIMKAISGSA-RCISIDLPGHGGSkiqnhakeTQTEPTLSVELVADLLYKLIEHITPGKVTL 1449
                          90       100
                  ....*....|....*....|....*...
gi 495186058   92 VGFSMgGGDVSRYIARHGSERVAGLVLL 119
Cdd:PLN02980 1450 VGYSM-GARIALYMALRFSDKIEGAVII 1476
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
19-119 4.00e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 41.36  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  19 SGKPVLFSHGWPLDADMWEYQMEYLSsRGYRTIAFDRRGFGRSDQPwTGYDY--DTFADDIAQLINHLDLRDVTLVGFSM 96
Cdd:PLN02679  87 SGPPVLLVHGFGASIPHWRRNIGVLA-KNYTVYAIDLLGFGASDKP-PGFSYtmETWAELILDFLEEVVQKPTVLIGNSV 164
                         90       100
                 ....*....|....*....|....*
gi 495186058  97 ggGDVSRYIARHGSER--VAGLVLL 119
Cdd:PLN02679 165 --GSLACVIAASESTRdlVRGLVLL 187
PRK10673 PRK10673
esterase;
48-119 1.11e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 39.71  E-value: 1.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495186058  48 YRTIAFDRRGFGRSdqPWT-GYDYDTFADDIAQLINHLDLRDVTLVGFSMGGGDVSRYIARhGSERVAGLVLL 119
Cdd:PRK10673  43 HDIIQVDMRNHGLS--PRDpVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTAL-APDRIDKLVAI 112
YpfH COG0400
Predicted esterase [General function prediction only];
59-141 1.20e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.12  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  59 GRSDQPWTGYDYDTFADDIAQLINH--LDLRDVTLVGFSMgGGDVSRYIARHGSERVAGLVLL-GAVTPLFGKKADFPQG 135
Cdd:COG0400   59 GREDEEGLAAAAEALAAFIDELEARygIDPERIVLAGFSQ-GAAMALSLALRRPELLAGVVALsGYLPGEEALPAPEAAL 137

                 ....*.
gi 495186058 136 VDTSVF 141
Cdd:COG0400  138 AGTPVF 143
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
9-119 3.03e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 38.18  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   9 GTEIYYKDWG-SGKPVLFSHGWPLDADMWEYQMEYLSSRGyRTIAFDRRGFGRSDQP-------WTGYDYDTFADDIAQL 80
Cdd:PLN02824  17 GYNIRYQRAGtSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPnprsappNSFYTFETWGEQLNDF 95
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495186058  81 INHLdLRDVTLVGFSMGGGDVSRYIARHGSERVAGLVLL 119
Cdd:PLN02824  96 CSDV-VGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLI 133
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
214-272 4.15e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 37.55  E-value: 4.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495186058 214 PTLVIHGDGDqivPFETTGKQAAAQIKGA----ELKVYAGAPHGFAVTH----AQALNEDLLAFLKR 272
Cdd:COG0657  141 PTLIVTGEAD---PLVDESEALAAALRAAgvpvELHVYPGGGHGFGLLAglpeARAALAEIAAFLRR 204
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-109 5.02e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 37.82  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058   4 FTTQDGTEI---YYKDWGSGKP--VLFsHGWPLDADMWeY---QMEYLSSRGYRTIAFDRRGFGRSD--QPwTGYdYDTF 73
Cdd:COG0429   41 LELPDGDFVdldWSDPPAPSKPlvVLL-HGLEGSSDSH-YargLARALYARGWDVVRLNFRGCGGEPnlLP-RLY-HSGD 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495186058  74 ADDIAQLINHL----DLRDVTLVGFSMGGGDVSRYIARHG 109
Cdd:COG0429  117 TEDLVWVLAHLraryPYAPLYAVGFSLGGNLLLKYLGEQG 156
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
205-229 5.42e-03

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: 37.16  E-value: 5.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 495186058  205 RPDMAKI----------DVPTLVIHGDGDQIVPFE 229
Cdd:pfam20434 172 NPDLAKSaspityvdknDPPFLIIHGDKDPLVPYC 206
PRK07868 PRK07868
acyl-CoA synthetase; Validated
20-158 9.14e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 37.39  E-value: 9.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495186058  20 GKPVLFSHGWPLDADMWEYQME-----YLSSRGYRTIAFDrrgFGRSDQPWTGYDyDTFADDIAQLINHLDL------RD 88
Cdd:PRK07868  67 GPPVLMVHPMMMSADMWDVTRDdgavgILHRAGLDPWVID---FGSPDKVEGGME-RNLADHVVALSEAIDTvkdvtgRD 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495186058  89 VTLVGFSMGGGDVSRYIARHGSERVAGLVLLGAvtPlfgkkadfpqgVDTS--VFDGIKAGLLQDRAQFIAD 158
Cdd:PRK07868 143 VHLVGYSQGGMFCYQAAAYRRSKDIASIVTFGS--P-----------VDTLaaLPMGIPAGLAAAAADFMAD 201
 
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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