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Conserved domains on  [gi|489192193|ref|WP_003101542|]
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MULTISPECIES: alpha/beta fold hydrolase [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, ...
 1-276 2.63e-45

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: 152.08  E-value: 2.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   1 MGYVTTkDGVELFYKDWGPrDAQVIYFHHGWPLSSDDWDAQMlFFLAEGFRVVAHDRRGHGRSSQVWDGHDMDHYADDVA 80
Cdd:COG0596    4 PRFVTV-DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLI-PALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  81 AVVERLGVRGAIHVGHSTGGGEVVHYIARYPDdpvpkaAIISAVpplmvktegnpgglpksVFDDLQAQLAANRAQFYQD 160
Cdd:COG0596   81 ALLDALGLERVVLVGHSMGGMVALELAARHPE------RVAGLV-----------------LVDEVLAALAEPLRRPGLA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 161 ipagpfygynrpgaqpsegivrnwwrqgmmggAKAHYDGIVAFSQTDFSDDLKRIDIPVLVMHGDDDQIVPYENSGVLsA 240
Cdd:COG0596  138 --------------------------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRL-A 184

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489192193 241 KLLRNGTLKTYPGFPHGMPTTQAEVINADLLAFIRG 276
Cdd:COG0596  185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-276 2.63e-45

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: 152.08  E-value: 2.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   1 MGYVTTkDGVELFYKDWGPrDAQVIYFHHGWPLSSDDWDAQMlFFLAEGFRVVAHDRRGHGRSSQVWDGHDMDHYADDVA 80
Cdd:COG0596    4 PRFVTV-DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLI-PALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  81 AVVERLGVRGAIHVGHSTGGGEVVHYIARYPDdpvpkaAIISAVpplmvktegnpgglpksVFDDLQAQLAANRAQFYQD 160
Cdd:COG0596   81 ALLDALGLERVVLVGHSMGGMVALELAARHPE------RVAGLV-----------------LVDEVLAALAEPLRRPGLA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 161 ipagpfygynrpgaqpsegivrnwwrqgmmggAKAHYDGIVAFSQTDFSDDLKRIDIPVLVMHGDDDQIVPYENSGVLsA 240
Cdd:COG0596  138 --------------------------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRL-A 184

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489192193 241 KLLRNGTLKTYPGFPHGMPTTQAEVINADLLAFIRG 276
Cdd:COG0596  185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 24-256 9.76e-29

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: 109.52  E-value: 9.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   24 VIYFHHGWPLSSDDWDAQMLFFLAEGFRVVAHDRRGHGRSSQVWDGHDM--DHYADDVAAVVERLGVRGAIHVGHSTGGG 101
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  102 EVVHYIARYPdDPVPKAAIISAVPPLMVKTEGNPGGLpKSVFDDLQAQLAA----NRAQFYQDIPAGPFYGYNRPGAQP- 176
Cdd:pfam00561  82 IALAYAAKYP-DRVKALVLLGALDPPHELDEADRFIL-ALFPGFFDGFVADfapnPLGRLVAKLLALLLLRLRLLKALPl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  177 -SEGIVRNWWRQGMMGGAKAHyDGIVAFSQTDFSDDLKRIDIPVLVMHGDDDQIVPYENSGVLsAKLLRNGTLKTYPGFP 255
Cdd:pfam00561 160 lNKRFPSGDYALAKSLVTGAL-LFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKL-AQLFPNARLVVIPDAG 237


                  .
gi 489192193  256 H 256
Cdd:pfam00561 238 H 238
PRK05855 PRK05855
SDR family oxidoreductase;
4-109 6.18e-16

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 77.33  E-value: 6.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   4 VTTKDGVELFYKDWGPRDAQVIYFHHGWPLSSDDWDaQMLFFLAEGFRVVAHDRRGHGRSSQVWDGHD--MDHYADDVAA 81
Cdd:PRK05855   7 VVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWD-GVAPLLADRFRVVAYDVRGAGRSSAPKRTAAytLARLADDFAA 85

                         90       100
                 ....*....|....*....|....*....
gi 489192193  82 VVERLGVRGAIHV-GHSTGGGEVVHYIAR 109
Cdd:PRK05855  86 VIDAVSPDRPVHLlAHDWGSIQGWEAVTR 114
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-276 2.63e-45

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: 152.08  E-value: 2.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   1 MGYVTTkDGVELFYKDWGPrDAQVIYFHHGWPLSSDDWDAQMlFFLAEGFRVVAHDRRGHGRSSQVWDGHDMDHYADDVA 80
Cdd:COG0596    4 PRFVTV-DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLI-PALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  81 AVVERLGVRGAIHVGHSTGGGEVVHYIARYPDdpvpkaAIISAVpplmvktegnpgglpksVFDDLQAQLAANRAQFYQD 160
Cdd:COG0596   81 ALLDALGLERVVLVGHSMGGMVALELAARHPE------RVAGLV-----------------LVDEVLAALAEPLRRPGLA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 161 ipagpfygynrpgaqpsegivrnwwrqgmmggAKAHYDGIVAFSQTDFSDDLKRIDIPVLVMHGDDDQIVPYENSGVLsA 240
Cdd:COG0596  138 --------------------------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRL-A 184

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489192193 241 KLLRNGTLKTYPGFPHGMPTTQAEVINADLLAFIRG 276
Cdd:COG0596  185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
2-275 8.24e-31

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 114.33  E-value: 8.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   2 GYVTTKDGVELFYKDWGPRDAQ--VIYFHHGWPLSSDDWDAQMLFFLAEGFRVVAHDRRGHGRSS-QVWDGHDMDHYADD 78
Cdd:COG2267    6 VTLPTRDGLRLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDgPRGHVDSFDDYVDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  79 VAAVVERLGVRGAIHV---GHSTGGGEVVHYIARYPDDpvPKAAIISAvpplmvktegnpgglpksvfddlqaqlaanra 155
Cdd:COG2267   86 LRAALDALRARPGLPVvllGHSMGGLIALLYAARYPDR--VAGLVLLA-------------------------------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 156 qfyqdipagPFYgynrpGAQPSEGIVRNWWRQGMMggakahydgivafsqtdfSDDLKRIDIPVLVMHGDDDQIVPYENS 235
Cdd:COG2267  132 ---------PAY-----RADPLLGPSARWLRALRL------------------AEALARIDVPVLVLHGGADRVVPPEAA 179

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489192193 236 GVLSAKLLRNGTLKTYPGFPHGMP--TTQAEVInADLLAFIR 275
Cdd:COG2267  180 RRLAARLSPDVELVLLPGARHELLnePAREEVL-AAILAWLE 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 24-256 9.76e-29

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: 109.52  E-value: 9.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   24 VIYFHHGWPLSSDDWDAQMLFFLAEGFRVVAHDRRGHGRSSQVWDGHDM--DHYADDVAAVVERLGVRGAIHVGHSTGGG 101
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  102 EVVHYIARYPdDPVPKAAIISAVPPLMVKTEGNPGGLpKSVFDDLQAQLAA----NRAQFYQDIPAGPFYGYNRPGAQP- 176
Cdd:pfam00561  82 IALAYAAKYP-DRVKALVLLGALDPPHELDEADRFIL-ALFPGFFDGFVADfapnPLGRLVAKLLALLLLRLRLLKALPl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  177 -SEGIVRNWWRQGMMGGAKAHyDGIVAFSQTDFSDDLKRIDIPVLVMHGDDDQIVPYENSGVLsAKLLRNGTLKTYPGFP 255
Cdd:pfam00561 160 lNKRFPSGDYALAKSLVTGAL-LFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKL-AQLFPNARLVVIPDAG 237


                  .
gi 489192193  256 H 256
Cdd:pfam00561 238 H 238
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 45-258 4.76e-21

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: 88.81  E-value: 4.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   45 FLAEGFRVVAHDRRGHGRSsqvwDGH-----DMDHYADDVAAVVERLGVRGA----IHVGHSTGGGEVVHYIARYPDDPv 115
Cdd:pfam12146  27 LAAQGFAVYAYDHRGHGRS----DGKrghvpSFDDYVDDLDTFVDKIREEHPglplFLLGHSMGGLIAALYALRYPDKV- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  116 pKAAIISA---------VPPLMVKTEG-----------NPGGLPKSVFDDlqaqlAANRAQFYQDipagPFYGynrpgaq 175
Cdd:pfam12146 102 -DGLILSApalkikpylAPPILKLLAKllgklfprlrvPNNLLPDSLSRD-----PEVVAAYAAD----PLVH------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  176 psEGIVRNWWRQGMMGGAKAHydgivafsqtdfsDDLKRIDIPVLVMHGDDDQIVPYENSGVLSAKL-LRNGTLKTYPGF 254
Cdd:pfam12146 165 --GGISARTLYELLDAGERLL-------------RRAAAITVPLLLLHGGADRVVDPAGSREFYERAgSTDKTLKLYPGL 229


                  ....
gi 489192193  255 PHGM 258
Cdd:pfam12146 230 YHEL 233
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
4-275 1.52e-19

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 84.68  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   4 VTTKDGVEL---FYKDWGPRDAQVIYFHHGWPLSSDD-WDAQMLFFLAEGFRVVAHDRRGHGRSSQVWDGHDMdhyaDDV 79
Cdd:COG1506    2 FKSADGTTLpgwLYLPADGKKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEV----DDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  80 AAVVERLGVRGAIH------VGHSTGGGEVVHYIARYPDDPvpkAAIISAVPPlmvktegnpgglpksvfddlqaqlaAN 153
Cdd:COG1506   78 LAAIDYLAARPYVDpdrigiYGHSYGGYMALLAAARHPDRF---KAAVALAGV-------------------------SD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 154 RAQFYQDIpagpfygynrpgaqpsegivrNWWRQGMMGGAKAHYDGIVAFSQTDFsddLKRIDIPVLVMHGDDDQIVPYE 233
Cdd:COG1506  130 LRSYYGTT---------------------REYTERLMGGPWEDPEAYAARSPLAY---ADKLKTPLLLIHGEADDRVPPE 185

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489192193 234 NSGVLSAKLLRNG---TLKTYPGFPHGMPTTQAEVINADLLAFIR 275
Cdd:COG1506  186 QAERLYEALKKAGkpvELLVYPGEGHGFSGAGAPDYLERILDFLD 230
PRK05855 PRK05855
SDR family oxidoreductase;
4-109 6.18e-16

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 77.33  E-value: 6.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   4 VTTKDGVELFYKDWGPRDAQVIYFHHGWPLSSDDWDaQMLFFLAEGFRVVAHDRRGHGRSSQVWDGHD--MDHYADDVAA 81
Cdd:PRK05855   7 VVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWD-GVAPLLADRFRVVAYDVRGAGRSSAPKRTAAytLARLADDFAA 85

                         90       100
                 ....*....|....*....|....*....
gi 489192193  82 VVERLGVRGAIHV-GHSTGGGEVVHYIAR 109
Cdd:PRK05855  86 VIDAVSPDRPVHLlAHDWGSIQGWEAVTR 114
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 4-275 5.81e-13

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 66.86  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   4 VTTKDGVEL-----FYKDWGPRDAQVIYFHhGWPLSSDDWDAQMLFFLAEGFRVVAHDRRGHGRSSQVWDGHDmDHYADD 78
Cdd:COG1073   15 FKSRDGIKLagdlyLPAGASKKYPAVVVAH-GNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEG-SPERRD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  79 VAAVVERLGVRGAIH------VGHSTGGGEVVHYIARypdDPVPKAAIISavpplmvktegnpgglpkSVFDDLQAQLAA 152
Cdd:COG1073   93 ARAAVDYLRTLPGVDperiglLGISLGGGYALNAAAT---DPRVKAVILD------------------SPFTSLEDLAAQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 153 NRAQFYQD-IPAGPFygynRPGAQPSEGIVRNWwrqgmmggakahydgivafsqtDFSDDLKRIDIPVLVMHGDDDQIVP 231
Cdd:COG1073  152 RAKEARGAyLPGVPY----LPNVRLASLLNDEF----------------------DPLAKIEKISRPLLFIHGEKDEAVP 205

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489192193 232 YENSGVLSAKLLRNGTLKTYPGFPHGMPTTQAEVINAD-LLAFIR 275
Cdd:COG1073  206 FYMSEDLYEAAAEPKELLIVPGAGHVDLYDRPEEEYFDkLAEFFK 250
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 8-276 2.56e-11

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 63.04  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   8 DGVELFYKDWGPRDAQVIYFHHGWPLSSDDWdaqmLFF---LAEGFRVVAHDRRGHGRSSQVWDGHDMDHYADDVAAVVE 84
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNW----LFNhaaLAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  85 RLGVRGAIHVGHSTGGGEVVHYIARYPDDpVPKAAIIS-----------------------AVPPLMVKTEGNPGGLPKS 141
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQR-VASLTLIApaglgpeingdyidgfvaaesrrELKPVLELLFADPALVTRQ 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 142 VFDDLQAQLAANRAQ-FYQDIPAGPFygynRPGAQpsegivrnwwrqgmmggakahydgivafsQTDFSDDLKRIDIPVL 220
Cdd:PRK14875 272 MVEDLLKYKRLDGVDdALRALADALF----AGGRQ-----------------------------RVDLRDRLASLAIPVL 318

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489192193 221 VMHGDDDQIVPYENSGVLSAkllrNGTLKTYPGFPHgMP-TTQAEVINADLLAFIRG 276
Cdd:PRK14875 319 VIWGEQDRIIPAAHAQGLPD----GVAVHVLPGAGH-MPqMEAAADVNRLLAEFLGK 370
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
17-275 1.42e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 57.26  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  17 WGPRDAqVIYFHhGwpLSSDDWDAQML--FFLAEGFRVVAHDRRGHGRSSQVWDGHDMDHYADDVAAVVERLGVRGA-IH 93
Cdd:COG1647   12 EGGRKG-VLLLH-G--FTGSPAEMRPLaeALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGYDkVI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  94 V-GHSTGGGEVVHYIARYPDdpVPKAAIISavPPLMVKtegNPGGLPKSVFDDLQAQLAANRAQFyqDIPAGPFYGYNRp 172
Cdd:COG1647   88 ViGLSMGGLLALLLAARYPD--VAGLVLLS--PALKID---DPSAPLLPLLKYLARSLRGIGSDI--EDPEVAEYAYDR- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 173 gaQPSEGIVRnwwRQGMMGGAKAHydgivafsqtdfsddLKRIDIPVLVMHGDDDQIVPYENSGVLSAKL-LRNGTLKTY 251
Cdd:COG1647  158 --TPLRALAE---LQRLIREVRRD---------------LPKITAPTLIIQSRKDEVVPPESARYIYERLgSPDKELVWL 217

                        250       260
                 ....*....|....*....|....*
gi 489192193 252 PGFPHGMPT-TQAEVINADLLAFIR 275
Cdd:COG1647  218 EDSGHVITLdKDREEVAEEILDFLE 242
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 25-232 9.54e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 54.40  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   25 IYFHHGWPLSSddwdAQMLFFLAEGFRVVAHDRRGHGRSSQVWdgHDMDHYADDVAAVVERLGVRGAIHVGHSTGGgevv 104
Cdd:pfam12697   1 VVLVHGAGLSA----APLAALLAAGVAVLAPDLPGHGSSSPPP--LDLADLADLAALLDELGAARPVVLVGHSLGG---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  105 HYIARYPDDPVPKAAIISAVPPlmvktegnPGGLPKSVFDDLQAQLAANRAQFYqdipagpfygynRPGAQPSEGIVRNW 184
Cdd:pfam12697  71 AVALAAAAAALVVGVLVAPLAA--------PPGLLAALLALLARLGAALAAPAW------------LAAESLARGFLDDL 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 489192193  185 WRQGMMGGAKAHYDGIVAFSQTDFSDDLKRIDIPVLVMHGDDDQIVPY 232
Cdd:pfam12697 131 PADAEWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPEL 178
PRK10566 PRK10566
esterase; Provisional
 24-256 8.36e-07

esterase; Provisional


Pssm-ID: 182555 [Multi-domain]  Cd Length: 249  Bit Score: 48.83  E-value: 8.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  24 VIYFHHGWpLSSDDWDAQMLFFLAE-GFRVVAHDRRGHG---------RSSQVWD--GHDMDHYADDVAAVV-------E 84
Cdd:PRK10566  29 TVFFYHGF-TSSKLVYSYFAVALAQaGFRVIMPDAPMHGarfsgdearRLNHFWQilLQNMQEFPTLRAAIReegwlldD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  85 RLGVRGAihvghSTGGGEVVHYIARYPDdpvpkaaiISAVPPLMvkTEGNPGGLPKSVFDDLQAQLAANRAQFYQDIPAg 164
Cdd:PRK10566 108 RLAVGGA-----SMGGMTALGIMARHPW--------VKCVASLM--GSGYFTSLARTLFPPLIPETAAQQAEFNNIVAP- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 165 pfygynrpgaqpsegiVRNWwrqgmmggakahydgivafsqtDFSDDLKRI-DIPVLVMHGDDDQIVPYENSGVL----- 238
Cdd:PRK10566 172 ----------------LAEW----------------------EVTHQLEQLaDRPLLLWHGLADDVVPAAESLRLqqalr 213

                        250
                 ....*....|....*...
gi 489192193 239 SAKLLRNGTLKTYPGFPH 256
Cdd:PRK10566 214 ERGLDKNLTCLWEPGVRH 231
YpfH COG0400
Predicted esterase [General function prediction only];
197-275 4.65e-06

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193 197 YDGIVAFS------QTDFSDDLKRIDIPVLVMHGDDDQIVPYENSGVLSAKLLRNG---TLKTYPGfPHGMPttQAEVin 267
Cdd:COG0400  114 LAGVVALSgylpgeEALPAPEAALAGTPVFLAHGTQDPVIPVERAREAAEALEAAGadvTYREYPG-GHEIS--PEEL-- 188


                 ....*...
gi 489192193 268 ADLLAFIR 275
Cdd:COG0400  189 ADARAWLA 196
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
213-274 6.88e-05

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 42.99  E-value: 6.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489192193  213 KRIDIPVLVMHGDDDQIVPYENSGVLSAKLLRNGT---LKTYPGFPHG--MPTTQAEVInADLLAFI 274
Cdd:pfam00326 141 VKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVpflLLIFPDEGHGigKPRNKVEEY-ARELAFL 206
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-128 7.30e-05

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 43.59  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   4 VTTKDG--VELfykDWGPRDAQ----VIYFHhGWPLSSDDWDAQ--MLFFLAEGFRVVAHDRRGHGRSsqvwdghdmDHY 75
Cdd:COG0429   41 LELPDGdfVDL---DWSDPPAPskplVVLLH-GLEGSSDSHYARglARALYARGWDVVRLNFRGCGGE---------PNL 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489192193  76 A---------DDVAAVVERL---GVRGAIH-VGHSTGGGEVVHYIARYPDDPVP--KAAIISavPPLM 128
Cdd:COG0429  108 LprlyhsgdtEDLVWVLAHLrarYPYAPLYaVGFSLGGNLLLKYLGEQGDDAPPlkAAVAVS--PPLD 173
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-112 5.61e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 40.75  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193   1 MGYVTTKdGVELFYKDWGprDAQVIYFHHGWPLSSDDWdAQMLFFLAEGFRVVAHDRRGHGRSSQVWDGHDMDHYADDVA 80
Cdd:PRK03592   9 MRRVEVL-GSRMAYIETG--EGDPIVFLHGNPTSSYLW-RNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLD 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489192193  81 AVVERLGVRGAIHVGHSTGGGEVVHYIARYPD 112
Cdd:PRK03592  85 AWFDALGLDDVVLVGHDWGSALGFDWAARHPD 116
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 197-275 5.68e-04

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 40.05  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  197 YDGIVAFS-----QTDFSDDLKRI--DIPVLVMHGDDDQIVPYEnSGVLSAKLLR----NGTLKTYPGFPHGMPTTQAEv 265
Cdd:pfam02230 130 LGGIVAFSgflplPTKFPSHPNLVtkKTPIFLIHGEEDPVVPLA-LGKLAKEYLKtslnKVELKIYEGLAHSICGREMQ- 207

                          90
                  ....*....|
gi 489192193  266 inaDLLAFIR 275
Cdd:pfam02230 208 ---DIKKFLS 214
COG4099 COG4099
Predicted peptidase [General function prediction only];
216-257 1.14e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.57  E-value: 1.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 489192193 216 DIPVLVMHGDDDQIVPYENSGVLSAKLLRNG---TLKTYPGFPHG 257
Cdd:COG4099  170 KVPVWIFHGAKDDVVPVEESRAMVEALKAAGadvKYTEYPGVGHN 214
PRK10749 PRK10749
lysophospholipase L2; Provisional
 49-112 1.42e-03

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 39.60  E-value: 1.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489192193  49 GFRVVAHDRRGHGRSSQVWD----GH--DMDHYADDVAAVVERLGVRGAIH----VGHSTGGGEVVHYIARYPD 112
Cdd:PRK10749  81 GYDVLIIDHRGQGRSGRLLDdphrGHveRFNDYVDDLAAFWQQEIQPGPYRkryaLAHSMGGAILTLFLQRHPG 154
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
198-258 2.39e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.41  E-value: 2.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489192193 198 DGIVAF----SQTDFSDDLKRIDIPVLVMHGDDDQIVPYENSGVLSAKLLRNG---TLKTYPGFPHGM 258
Cdd:COG0412  134 AAAVSFygglPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGvdvELHVYPGAGHGF 201
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 216-242 3.14e-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: 37.93  E-value: 3.14e-03
                          10        20
                  ....*....|....*....|....*..
gi 489192193  216 DIPVLVMHGDDDQIVPYENSGVLSAKL 242
Cdd:pfam20434 189 DPPFLIIHGDKDPLVPYCQSVLLHEKL 215
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 21-110 5.35e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.58  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192193  21 DAQVIYFHHGWPLSSDDWDAQMLFFLAEGFRVVAHDrrghgrssQVWDGHDMDHYADDVAAVVER-LGVRGA--IH-VGH 96
Cdd:COG1075    4 TRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYALN--------YPSTNGSIEDSAEQLAAFVDAvLAATGAekVDlVGH 75

                         90
                 ....*....|....
gi 489192193  97 STGGgevvhYIARY 110
Cdd:COG1075   76 SMGG-----LVARY 84
 
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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