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Conserved domains on  [gi|1845781375|gb|QKC75996|]
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alpha/beta hydrolase [Mesorhizobium erdmanii]

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, ...
 14-278 7.33e-50

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: 164.02  E-value: 7.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  14 SHRVDTGRITLNVRETGN-GPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLI 92
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPdGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  93 RTLDRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAIDftpyievEVLDALEARVNagnqlfenveaveaylagrypnip 172
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-------EVLAALAEPLR------------------------ 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 173 apaikiraesgyqpvdgglRPLASPSAMAQTAKGL-RSDLVPTYRDVTKPVLIVRGETSKLVSAAALAKTSRLRPDLPVV 251
Cdd:COG0596   133 -------------------RPGLAPEALAALLRALaRTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELV 193

                         250       260
                  ....*....|....*....|....*..
gi 1845781375 252 VVPGADHYVNEVSPEITLKAITNFIDA 278
Cdd:COG0596   194 VLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 14-278 7.33e-50

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: 164.02  E-value: 7.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  14 SHRVDTGRITLNVRETGN-GPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLI 92
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPdGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  93 RTLDRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAIDftpyievEVLDALEARVNagnqlfenveaveaylagrypnip 172
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-------EVLAALAEPLR------------------------ 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 173 apaikiraesgyqpvdgglRPLASPSAMAQTAKGL-RSDLVPTYRDVTKPVLIVRGETSKLVSAAALAKTSRLRPDLPVV 251
Cdd:COG0596   133 -------------------RPGLAPEALAALLRALaRTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELV 193

                         250       260
                  ....*....|....*....|....*..
gi 1845781375 252 VVPGADHYVNEVSPEITLKAITNFIDA 278
Cdd:COG0596   194 VLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-265 9.85e-28

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: 107.21  E-value: 9.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  33 PLMLLFHGITSNSAVFAPLMTRLS-DRFRTIAVDQRGHGRSDKPEA--GYEANDYADDIAGLIRTLDRGPAILVGHSLGA 109
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 110 RNSVTAAAKYPDLVRSVVAIDftpyIEVEVLDALEARVNAGNQLFE----NVEAVEAYLAGRYPNIPA--------PAIK 177
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLG----ALDPPHELDEADRFILALFPGffdgFVADFAPNPLGRLVAKLLallllrlrLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 178 IRAESGYQPVDGglrpLASPSAMAQTAKGLRS-----DLVPTYRDVTKPVLIVRGETSKLVSAAALAKTSRLRPDLPVVV 252
Cdd:pfam00561 157 LPLLNKRFPSGD----YALAKSLVTGALLFIEtwsteLRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVV 232

                         250
                  ....*....|...
gi 1845781375 253 VPGADHYVNEVSP 265
Cdd:pfam00561 233 IPDAGHFAFLEGP 245
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 12-273 5.17e-16

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 76.05  E-value: 5.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  12 FVSHRVDTGRITLNVRETGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEA-GYEANDYADDIAG 90
Cdd:PRK03204   14 FESRWFDSSRGRIHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGfGYQIDEHARVIGE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  91 LIRTLDRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAID--FTPY--IEVEVLDALEARVNAGNQLFENVEAVEAYLAG 166
Cdd:PRK03204   94 FVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNtwFWPAdtLAMKAFSRVMSSPPVQYAILRRNFFVERLIPA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 167 RYPNIPAPAIkIRAESGYQPVDGGLRPLAspsAMAQTAKGLRSDLVPTYRDV-----TKPVLIVRGETSKLVS-AAALAK 240
Cdd:PRK03204  174 GTEHRPSSAV-MAHYRAVQPNAAARRGVA---EMPKQILAARPLLARLAREVpatlgTKPTLLVWGMKDVAFRpKTILPR 249

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1845781375 241 TSRLRPDLPVVVVPGADHYVNEVSPEITLKAIT 273
Cdd:PRK03204  250 LRATFPDHVLVELPNAKHFIQEDAPDRIAAAII 282
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 95-129 6.96e-06

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 46.47  E-value: 6.96e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1845781375  95 LDR-GPAILVGHSLGARNSVTAAAKYPDLVRSVVAI 129
Cdd:cd12808   184 LDRvGPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 14-278 7.33e-50

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: 164.02  E-value: 7.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  14 SHRVDTGRITLNVRETGN-GPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLI 92
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPdGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  93 RTLDRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAIDftpyievEVLDALEARVNagnqlfenveaveaylagrypnip 172
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-------EVLAALAEPLR------------------------ 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 173 apaikiraesgyqpvdgglRPLASPSAMAQTAKGL-RSDLVPTYRDVTKPVLIVRGETSKLVSAAALAKTSRLRPDLPVV 251
Cdd:COG0596   133 -------------------RPGLAPEALAALLRALaRTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELV 193

                         250       260
                  ....*....|....*....|....*..
gi 1845781375 252 VVPGADHYVNEVSPEITLKAITNFIDA 278
Cdd:COG0596   194 VLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-265 9.85e-28

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: 107.21  E-value: 9.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  33 PLMLLFHGITSNSAVFAPLMTRLS-DRFRTIAVDQRGHGRSDKPEA--GYEANDYADDIAGLIRTLDRGPAILVGHSLGA 109
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 110 RNSVTAAAKYPDLVRSVVAIDftpyIEVEVLDALEARVNAGNQLFE----NVEAVEAYLAGRYPNIPA--------PAIK 177
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLG----ALDPPHELDEADRFILALFPGffdgFVADFAPNPLGRLVAKLLallllrlrLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 178 IRAESGYQPVDGglrpLASPSAMAQTAKGLRS-----DLVPTYRDVTKPVLIVRGETSKLVSAAALAKTSRLRPDLPVVV 252
Cdd:pfam00561 157 LPLLNKRFPSGD----YALAKSLVTGALLFIEtwsteLRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVV 232

                         250
                  ....*....|...
gi 1845781375 253 VPGADHYVNEVSP 265
Cdd:pfam00561 233 IPDAGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
32-278 2.25e-22

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 91.99  E-value: 2.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  32 GPLMLLFHGITSNSAVFAPLMTRLSDR-FRTIAVDQRGHGRSDKPEAGYE-ANDYADDIAGLIRTLDR---GPAILVGHS 106
Cdd:COG2267    28 RGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDsFDDYVDDLRAALDALRArpgLPVVLLGHS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 107 LGARNSVTAAAKYPDLVRSVVAIdftpyievevldalearvnagnqlfenveaveaylagrypnipAPAIKiraesgyqp 186
Cdd:COG2267   108 MGGLIALLYAARYPDRVAGLVLL-------------------------------------------APAYR--------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 187 vdggLRPLASPSAMAQTAKGLRSDLvptyRDVTKPVLIVRGETSKLVSAAALAKT-SRLRPDLPVVVVPGADHYV-NEVS 264
Cdd:COG2267   136 ----ADPLLGPSARWLRALRLAEAL----ARIDVPVLVLHGGADRVVPPEAARRLaARLSPDVELVLLPGARHELlNEPA 207

                         250
                  ....*....|....
gi 1845781375 265 PEITLKAITNFIDA 278
Cdd:COG2267   208 REEVLAAILAWLER 221
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 12-273 5.17e-16

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 76.05  E-value: 5.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  12 FVSHRVDTGRITLNVRETGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEA-GYEANDYADDIAG 90
Cdd:PRK03204   14 FESRWFDSSRGRIHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGfGYQIDEHARVIGE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  91 LIRTLDRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAID--FTPY--IEVEVLDALEARVNAGNQLFENVEAVEAYLAG 166
Cdd:PRK03204   94 FVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNtwFWPAdtLAMKAFSRVMSSPPVQYAILRRNFFVERLIPA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 167 RYPNIPAPAIkIRAESGYQPVDGGLRPLAspsAMAQTAKGLRSDLVPTYRDV-----TKPVLIVRGETSKLVS-AAALAK 240
Cdd:PRK03204  174 GTEHRPSSAV-MAHYRAVQPNAAARRGVA---EMPKQILAARPLLARLAREVpatlgTKPTLLVWGMKDVAFRpKTILPR 249

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1845781375 241 TSRLRPDLPVVVVPGADHYVNEVSPEITLKAIT 273
Cdd:PRK03204  250 LRATFPDHVLVELPNAKHFIQEDAPDRIAAAII 282
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 34-237 1.34e-14

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: 71.48  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  34 LMLLFHGITSNSAVFAPLMTRLSDR-FRTIAVDQRGHGRSDkPEAGYEA--NDYADDIAGLIRTLD----RGPAILVGHS 106
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSD-GKRGHVPsfDDYVDDLDTFVDKIReehpGLPLFLLGHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 107 LGARNSVTAAAKYPDLVRSVVAidFTPYIEVEVLDALearvnagnqlfeNVEAVEAYLAGR-YPNIPAPA-IKIRAESGY 184
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGLIL--SAPALKIKPYLAP------------PILKLLAKLLGKlFPRLRVPNnLLPDSLSRD 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1845781375 185 QPVDGGLR--PLASPSAMAQTAKGLR---SDLVPTYRDVTKPVLIVRGETSKLVSAAA 237
Cdd:pfam12146 151 PEVVAAYAadPLVHGGISARTLYELLdagERLLRRAAAITVPLLLLHGGADRVVDPAG 208
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 35-262 2.55e-14

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 70.20  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  35 MLLFHGITSNSAVFAPLmtrLSDRFRTIAVDQRGHGRSDKPEAGYEAndyADDIAGLIRTLDR-GPAILVGHSLGArnSV 113
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL---LAAGVAVLAPDLPGHGSSSPPPLDLAD---LADLAALLDELGAaRPVVLVGHSLGG--AV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 114 TAAAKYPDLVRSVvaidftpyieveVLDALEARVNAGNQLFENVEAVEAYLAGRypniPAPAIKIRAESGYQPVDGGLRP 193
Cdd:pfam12697  73 ALAAAAAALVVGV------------LVAPLAAPPGLLAALLALLARLGAALAAP----AWLAAESLARGFLDDLPADAEW 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845781375 194 LASPSAMAQTAKGLRSDLVPTYRDVTKPVLIVRGEtsKLVSAAALAKTSRLRPDLPVVVVPGADHYVNE 262
Cdd:pfam12697 137 AAALARLAALLAALALLPLAAWRDLPVPVLVLAEE--DRLVPELAQRLLAALAGARLVVLPGAGHLPLD 203
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 27-127 7.25e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 67.33  E-value: 7.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  27 RETGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLIRTLDRGPAILVGHS 106
Cdd:PRK03592   22 IETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWFDALGLDDVVLVGHD 101

                          90       100
                  ....*....|....*....|.
gi 1845781375 107 LGARNSVTAAAKYPDLVRSVV 127
Cdd:PRK03592  102 WGSALGFDWAARHPDRVRGIA 122
PRK05855 PRK05855
SDR family oxidoreductase;
15-109 1.04e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 67.70  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  15 HRVDTGRITLNVRETGN--GPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPE--AGYEANDYADDIAG 90
Cdd:PRK05855    6 TVVSSDGVRLAVYEWGDpdRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKrtAAYTLARLADDFAA 85

                          90       100
                  ....*....|....*....|.
gi 1845781375  91 LIRTL--DRgPAILVGHSLGA 109
Cdd:PRK05855   86 VIDAVspDR-PVHLLAHDWGS 105
PRK10673 PRK10673
esterase;
29-278 2.96e-12

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 65.14  E-value: 2.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  29 TGNGPLMLLfHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDK-PEAGYEAndYADDIAGLIRTLDRGPAILVGHSL 107
Cdd:PRK10673   14 HNNSPIVLV-HGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRdPVMNYPA--MAQDLLDTLDALQIEKATFIGHSM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 108 GARNSVTAAAKYPDLVRSVVAIDFTPyievevldaLEARVNAGNQLFENVEAVEAylAGRYPNIPAPAI---KIRAESGY 184
Cdd:PRK10673   91 GGKAVMALTALAPDRIDKLVAIDIAP---------VDYHVRRHDEIFAAINAVSE--AGATTRQQAAAImrqHLNEEGVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 185 Q-----PVDGGLRpLASPSAMAQTAKGLRSDLVPTYrdvTKPVLIVRGETSKLVSAAALAKTSRLRPDLPVVVVPGADHY 259
Cdd:PRK10673  160 QfllksFVDGEWR-FNVPVLWDQYPHIVGWEKIPAW---PHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHW 235

                         250
                  ....*....|....*....
gi 1845781375 260 VNEVSPEITLKAITNFIDA 278
Cdd:PRK10673  236 VHAEKPDAVLRAIRRYLND 254
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 16-260 3.60e-12

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 65.74  E-value: 3.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  16 RVDTGRITLNVRETGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLIRTL 95
Cdd:PRK14875  115 RIGGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDAL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  96 DRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAID---FTPYIEVEVLDALearVNAGN---------QLFEN------- 156
Cdd:PRK14875  195 GIERAHLVGHSMGGAVALRLAARAPQRVASLTLIApagLGPEINGDYIDGF---VAAESrrelkpvleLLFADpalvtrq 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 157 -VEAVEAYLagrypnipapaikiRAESgyqpVDGGLRPLASpSAMAQTAKglRSDLVPTYRDVTKPVLIVRGETSKLVSA 235
Cdd:PRK14875  272 mVEDLLKYK--------------RLDG----VDDALRALAD-ALFAGGRQ--RVDLRDRLASLAIPVLVIWGEQDRIIPA 330

                         250       260
                  ....*....|....*....|....*
gi 1845781375 236 aalAKTSRLRPDLPVVVVPGADHYV 260
Cdd:PRK14875  331 ---AHAQGLPDGVAVHVLPGAGHMP 352
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 33-278 6.31e-12

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 64.17  E-value: 6.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  33 PLMLLFHGITSNSAVFAPLMTRLSDR-FRTIAVDQRGHGRSD-KP-EAG-YEANDYAD--DIAGLIRTLDRGPAILVGHS 106
Cdd:COG1073    38 PAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESEgEPrEEGsPERRDARAavDYLRTLPGVDPERIGLLGIS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 107 LGARNSVTAAAKYPDlVRSVVAIdfTPYIEVEvlDALEARvnagnqlfenveaVEAYLAGRYPNIPapaikiraesgyqp 186
Cdd:COG1073   118 LGGGYALNAAATDPR-VKAVILD--SPFTSLE--DLAAQR-------------AKEARGAYLPGVP-------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 187 vdggLRPLASPSAMAqtakglrSDLVPTYRDV---TKPVLIVRGETSKLVSAAALAKTSRLRPDlP--VVVVPGADHY-V 260
Cdd:COG1073   166 ----YLPNVRLASLL-------NDEFDPLAKIekiSRPLLFIHGEKDEAVPFYMSEDLYEAAAE-PkeLLIVPGAGHVdL 233

                         250
                  ....*....|....*...
gi 1845781375 261 NEVSPEITLKAITNFIDA 278
Cdd:COG1073   234 YDRPEEEYFDKLAEFFKK 251
PLN02578 PLN02578
hydrolase
 28-278 2.10e-11

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 63.32  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  28 ETGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLIRTLDRGPAILVGHSL 107
Cdd:PLN02578   82 VQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 108 GARNSVTAAAKYPDLVRSVVAIDFTpyievevldaleARVNAGNQLFENVEAVEAYLAGRYPNIPAPAIKIRAESGY--- 184
Cdd:PLN02578  162 GGFTALSTAVGYPELVAGVALLNSA------------GQFGSESREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGFlfw 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 185 ---QP---------------------VDGGLRPLASPSA------------MAQTAKGLRSDLvptyRDVTKPVLIVRGE 228
Cdd:PLN02578  230 qakQPsriesvlksvykdksnvddylVESITEPAADPNAgevyyrlmsrflFNQSRYTLDSLL----SKLSCPLLLLWGD 305

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1845781375 229 TSKLVSAAALAKTSRLRPDLPVVVVPgADHYVNEVSPEITLKAITNFIDA 278
Cdd:PLN02578  306 LDPWVGPAKAEKIKAFYPDTTLVNLQ-AGHCPHDEVPEQVNKALLEWLSS 354
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 24-276 5.23e-11

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 62.95  E-value: 5.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375   24 LNVRETG---NGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEAND--------YADDIAGLI 92
Cdd:PLN02980  1360 IKVHEVGqnaEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNHAKETQTeptlsvelVADLLYKLI 1439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375   93 RTLDRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAIDFTPYIEVEV-------LDALEAR--VNAGNQLFenveaVEAY 163
Cdd:PLN02980  1440 EHITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIISGSPGLKDEVarkirsaKDDSRARmlIDHGLEIF-----LENW 1514

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  164 LAGRYPNipapaiKIRAESGYQPV------DGGLRPLAspSAMAQTAKGLRSDLVPTYRDVTKPVLIVRGETSKLVSAAA 237
Cdd:PLN02980  1515 YSGELWK------SLRNHPHFNKIvasrllHKDVPSLA--KLLSDLSIGRQPSLWEDLKQCDTPLLLVVGEKDVKFKQIA 1586

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1845781375  238 ------LAKTSRLRPDLP-----VVVVPGADHYVNEVSPEITLKAITNFI 276
Cdd:PLN02980  1587 qkmyreIGKSKESGNDKGkeiieIVEIPNCGHAVHLENPLPVIRALRKFL 1636
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
27-277 1.59e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 59.65  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  27 RETGNGPLMLLFHGITSN-SAVFAPLMTRLSDR-FRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLIRT--LDRGPAIL 102
Cdd:COG1506    18 ADGKKYPVVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARpyVDPDRIGI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 103 VGHSLGARNSVTAAAKYPDLVRSVVAIdftpyievevldalearvnAGNQLFENVEAVEAYLAGRYPNIPAPAIKIRAES 182
Cdd:COG1506    98 YGHSYGGYMALLAAARHPDRFKAAVAL-------------------AGVSDLRSYYGTTREYTERLMGGPWEDPEAYAAR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 183 gyqpvdgglrplaSPSAMAqtakglrsdlvptyRDVTKPVLIVRGE---------TSKLVSAAALA-KTSRLrpdlpvVV 252
Cdd:COG1506   159 -------------SPLAYA--------------DKLKTPLLLIHGEaddrvppeqAERLYEALKKAgKPVEL------LV 205

                         250       260
                  ....*....|....*....|....*
gi 1845781375 253 VPGADHYVNEVSPEITLKAITNFID 277
Cdd:COG1506   206 YPGEGHGFSGAGAPDYLERILDFLD 230
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
30-277 3.47e-10

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 58.80  E-value: 3.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  30 GNGPLMLLFHGITSNSAVFAPLMTRLSDR-FRTIAVDQRGHGRSDKPEAGYEANDYADDIAGLIRTLDRG--PAILVGHS 106
Cdd:COG1647    13 GGRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIVIGLS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 107 LGARNSVTAAAKYPDlVRSVVAIDftPYIEVEVLDALEARVnagnqlfenVEAVEAYLAGRYPNIPAPAikiRAESGYQP 186
Cdd:COG1647    93 MGGLLALLLAARYPD-VAGLVLLS--PALKIDDPSAPLLPL---------LKYLARSLRGIGSDIEDPE---VAEYAYDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 187 VdgglrplasPSAMAQTAKGLRSDLVPTYRDVTKPVLIVRG---ETSKLVSAAALAKtsRLR-PDLPVVVVPGADHYV-N 261
Cdd:COG1647   158 T---------PLRALAELQRLIREVRRDLPKITAPTLIIQSrkdEVVPPESARYIYE--RLGsPDKELVWLEDSGHVItL 226

                         250
                  ....*....|....*.
gi 1845781375 262 EVSPEITLKAITNFID 277
Cdd:COG1647   227 DKDREEVAEEILDFLE 242
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 29-130 5.48e-07

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 50.26  E-value: 5.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  29 TGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAG----YEANDYADDIAGLIRTLDRGPAILVG 104
Cdd:PLN03084  124 SNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGygfnYTLDEYVSSLESLIDELKSDKVSLVV 203

                          90       100
                  ....*....|....*....|....*.
gi 1845781375 105 HSLGARNSVTAAAKYPDLVRSVVAID 130
Cdd:PLN03084  204 QGYFSPPVVKYASAHPDKIKKLILLN 229
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 29-127 1.45e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 48.68  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  29 TGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEA-GYEANDYADDIAGLIRTLDRGPAILVGHSL 107
Cdd:PLN02679   85 TSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGfSYTMETWAELILDFLEEVVQKPTVLIGNSV 164

                          90       100
                  ....*....|....*....|.
gi 1845781375 108 GARNSVTAAAKYP-DLVRSVV 127
Cdd:PLN02679  165 GSLACVIAASESTrDLVRGLV 185
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 27-130 2.58e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 47.81  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  27 RETGNGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEA--------------GYEANDYADDIAGli 92
Cdd:PLN02824   24 RAGTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPrsappnsfytfetwGEQLNDFCSDVVG-- 101

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1845781375  93 rtldrGPAILVGHSLGARNSVTAAAKYPDLVRSVVAID 130
Cdd:PLN02824  102 -----DPAFVICNSVGGVVGLQAAVDAPELVRGVMLIN 134
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 31-127 3.78e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 47.60  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  31 NGPLMLLFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPE----AGYEAND-YADDIAGLIRTLDRGPAILVGH 105
Cdd:PLN02894  104 DAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDftckSTEETEAwFIDSFEEWRKAKNLSNFILLGH 183

                          90       100
                  ....*....|....*....|..
gi 1845781375 106 SLGARNSVTAAAKYPDLVRSVV 127
Cdd:PLN02894  184 SFGGYVAAKYALKHPEHVQHLI 205
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 95-129 6.96e-06

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 46.47  E-value: 6.96e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1845781375  95 LDR-GPAILVGHSLGARNSVTAAAKYPDLVRSVVAI 129
Cdd:cd12808   184 LDRvGPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
8-129 7.68e-06

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 46.29  E-value: 7.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375   8 PSDHFVSHRVDTG-----RITLNVRETGNGPLMLLFHGIT--SNSAVFAPLMTRLSDR-FRTIAVDQRGHGRSD--KPEA 77
Cdd:COG0429    32 PALPYRRERLELPdgdfvDLDWSDPPAPSKPLVVLLHGLEgsSDSHYARGLARALYARgWDVVRLNFRGCGGEPnlLPRL 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845781375  78 gYEANDyADDIAGLIRTL-DRGPA---ILVGHSLGArNsvtAAAKY-------PDLVRSVVAI 129
Cdd:COG0429   112 -YHSGD-TEDLVWVLAHLrARYPYaplYAVGFSLGG-N---LLLKYlgeqgddAPPLKAAVAV 168
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 36-137 1.30e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 45.95  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  36 LLFHGITSNSA-----VFAPLMTRLSDRFRTIAVDQRGHGRSDKP-EAGYEANDYADDIA-GLIRTLDRGPAILVGHSLG 108
Cdd:PLN03087  205 LFIHGFISSSAfwtetLFPNFSDAAKSTYRLFAVDLLGFGRSPKPaDSLYTLREHLEMIErSVLERYKVKSFHIVAHSLG 284

                          90       100
                  ....*....|....*....|....*....
gi 1845781375 109 ARNSVTAAAKYPDLVRSVVAIDfTPYIEV 137
Cdd:PLN03087  285 CILALALAVKHPGAVKSLTLLA-PPYYPV 312
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 25-134 1.43e-05

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 45.38  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  25 NVRETGNGPLMLLFHGITSNSAVFAPL--MTRLSDRFRTIAV--DQRGHGRS---DKPEAGYEANDYAD--DIAGLIRTL 95
Cdd:COG3509    46 GYDGGAPLPLVVALHGCGGSAADFAAGtgLNALADREGFIVVypEGTGRAPGrcwNWFDGRDQRRGRDDvaFIAALVDDL 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1845781375  96 ------DRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAIDFTPY 134
Cdd:COG3509   126 aarygiDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAGLPY 170
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 37-199 1.76e-05

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 44.69  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  37 LFHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSDKPEAGYEAndYADDIAGLIR-TLDRGPAILVGHSLGARNSVTA 115
Cdd:pfam00975   5 CFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEA--LADEYAEALRqIQPEGPYALFGHSMGGMLAFEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 116 AAKYPDL---VRSVVAIDFT-PYIEV----------EVLDALeaRVNAGNQlfENVEAVEAYLAGRYPNIPAPAikiRAE 181
Cdd:pfam00975  83 ARRLERQgeaVRSLFLSDASaPHTVRyeasrapdddEVVAEF--TDEGGTP--EELLEDEELLSMLLPALRADY---RAL 155

                         170
                  ....*....|....*...
gi 1845781375 182 SGYQpvdggLRPLASPSA 199
Cdd:pfam00975 156 ESYS-----CPPLDAQSA 168
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 36-129 2.40e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 42.51  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  36 LLFHGITSNSAVFAPLMTRLSDR-FRTIAVDQRGHGRSdkpeagyeANDYADDIAGLIRTLDR----GPAILVGHSLG-- 108
Cdd:COG1075     9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGS--------IEDSAEQLAAFVDAVLAatgaEKVDLVGHSMGgl 80

                          90       100
                  ....*....|....*....|..
gi 1845781375 109 -ARNsVTAAAKYPDLVRSVVAI 129
Cdd:COG1075    81 vARY-YLKRLGGAAKVARVVTL 101
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 95-129 3.58e-05

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214008  Cd Length: 280  Bit Score: 44.14  E-value: 3.58e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1845781375  95 LDR-GPAILVGHSLGARNSVTAAAKYPDLVRSVVAI 129
Cdd:cd12809   167 LDIiGPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
YpfH COG0400
Predicted esterase [General function prediction only];
28-150 4.57e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 43.36  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  28 ETGNGPLMLLFHGITSNSAVFAPLMTRLS-DRFRTIAVdqrgHGRSDKPEAGY---------------EANDYADDIAGL 91
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELAlPGAAVLAP----RAPVPEGPGGRawfdlsflegredeeGLAAAAEALAAF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845781375  92 IRTL------DRGPAILVGHSLGARNSVTAAAKYPDLVRSVVAidFTPYIEVEVLDALEARVNAG 150
Cdd:COG0400    77 IDELearygiDPERIVLAGFSQGAAMALSLALRRPELLAGVVA--LSGYLPGEEALPAPEAALAG 139
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 44-278 1.35e-04

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 42.15  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  44 NSAVFAPLMTRLSDRFRTIAVD--QRGHGRSDKPEAGYEanDYADDIAGLIRTLDRGPAILVGHSLGArnsvtaaakypd 121
Cdd:COG3208    18 SASAYRPWAAALPPDIEVLAVQlpGRGDRLGEPPLTSLE--ELADDLAEELAPLLDRPFALFGHSMGA------------ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 122 lvrsVVAidftpyieVEVLDALEARvnagnqlfeNVEAVEA-YLAGRY-PNIPAPAIKIRAESGYQPVD-----GGLRP- 193
Cdd:COG3208    84 ----LLA--------FELARRLERR---------GRPLPAHlFVSGRRaPHLPRRRRPLHDLSDAELLAelrrlGGTPEe 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 194 -LASPSAMAQTAKGLRSD--LVPTYRDVTK-----PVLIVRGETSKLVSAAALAKTSRL-RPDLPVVVVPGaDH-YVNEv 263
Cdd:COG3208   143 vLADPELLELFLPILRADfrLLETYRYTPGppldcPITALGGDDDPLVSPEELAAWREHtTGPFRLRVFPG-GHfFLRD- 220

                         250
                  ....*....|....*
gi 1845781375 264 SPEITLKAITNFIDA 278
Cdd:COG3208   221 HPAELLALIRAALAA 235
Esterase_713 cd12807
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ...
 86-129 2.01e-04

Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214006  Cd Length: 315  Bit Score: 41.93  E-value: 2.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1845781375  86 DDIAGLIRTLdrGPAILVGHSLGARNSVTAAAKYPDLVRSVVAI 129
Cdd:cd12807   179 NALAALADKL--GGAVLLGHSQSGPFPLEAALLRPAGVKGIVSV 220
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
220-278 3.00e-04

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 40.92  E-value: 3.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375 220 KPVLIVRGETSKLVS-AAALAKTSRLRPDLPVVVVPGADHYVNEVSPEITlKAITNFIDA 278
Cdd:COG2945   143 APTLVIHGEQDEVVPpAEVLDWARPLSPPLPVVVVPGADHFFHGKLDELK-ELVARYLPR 201
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
36-129 4.44e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 41.02  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  36 LLFHGITSNSAVF-APLMTRLSDR-FRTIAVDQRGHGRSdKPEAGYEAN-DYAD----DIAGLIRTLDR----GPAILVG 104
Cdd:COG4757    35 VLINPATGVPQRFyRPFARYLAERgFAVLTYDYRGIGLS-RPGSLRGFDaGYRDwgelDLPAVLDALRArfpgLPLLLVG 113

                          90       100
                  ....*....|....*....|....*
gi 1845781375 105 HSLGARnsVTAAAKYPDLVRSVVAI 129
Cdd:COG4757   114 HSLGGQ--LLGLAPNAERVDRLVTV 136
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 18-128 4.58e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 41.11  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  18 DTGRITLNVRETG--NGPLMLLFHGITSNSAVFAPLMTRLSDR-FRTIAVDQRGHGRSDKP--EAGYEANDYADDIAGLI 92
Cdd:PRK00870   30 DGGPLRMHYVDEGpaDGPPVLLLHGEPSWSYLYRKMIPILAAAgHRVIAPDLIGFGRSDKPtrREDYTYARHVEWMRSWF 109

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1845781375  93 RTLDRGPAILVGHSLGARNSVTAAAKYPDLVRSVVA 128
Cdd:PRK00870  110 EQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVV 145
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
30-133 7.97e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.00  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  30 GNGPLMLLfHGITSNSAVFAPLMTRLSDRFRTIAVDQRGHGRSdkpeAGYEANDYADDIAGLIRtldRGP--AILVGHSL 107
Cdd:PRK10349   12 GNVHLVLL-HGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS----RGFGALSLADMAEAVLQ---QAPdkAIWLGWSL 83

                          90       100
                  ....*....|....*....|....*.
gi 1845781375 108 GARNSVTAAAKYPDLVRSVVAIDFTP 133
Cdd:PRK10349   84 GGLVASQIALTHPERVQALVTVASSP 109
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
29-129 8.50e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  29 TGNGPLMLLFHGITSNSAVFAPLMTRLSDR-FRTIAVD-QRGHGRSDKPEAGYE------ANDYADDIAGLIRTL----- 95
Cdd:COG0412    26 GGPRPGVVVLHEIFGLNPHIRDVARRLAAAgYVVLAPDlYGRGGPGDDPDEARAlmgaldPELLAADLRAALDWLkaqpe 105

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1845781375  96 -DRGPAILVGHSLGARNSVTAAAKYPDLvRSVVAI 129
Cdd:COG0412   106 vDAGRVGVVGFCFGGGLALLAAARGPDL-AAAVSF 139
PHA02857 PHA02857
monoglyceride lipase; Provisional
 34-140 1.06e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 39.87  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  34 LMLLFHGITSNSAVFAPLMTRLSDRfrTIAV---DQRGHGRSDKPEAGYEA-NDYADDIAGLIRTLDRG----PAILVGH 105
Cdd:PHA02857   27 LVFISHGAGEHSGRYEELAENISSL--GILVfshDHIGHGRSNGEKMMIDDfGVYVRDVVQHVVTIKSTypgvPVFLLGH 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1845781375 106 SLGARNSVTAAAKYPDLVRSVVAIdfTPYIEVEVL 140
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILM--SPLVNAEAV 137
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 31-110 1.42e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 39.05  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845781375  31 NGPLMLLFHGITSNSAVFAPLMTRLSDrFRTIAVDQRGHGRSdkpeAGYEANDYADDIAGLIRTLDR---GPAILVGHSL 107
Cdd:PRK11126    1 GLPWLVFLHGLLGSGQDWQPVGEALPD-YPRLYIDLPGHGGS----AAISVDGFADVSRLLSQTLQSyniLPYWLVGYSL 75


                  ...
gi 1845781375 108 GAR 110
Cdd:PRK11126   76 GGR 78
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
83-128 6.14e-03

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


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 36.75  E-value: 6.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1845781375  83 DYADDIAGLIRTLDR--GPAILVGHSLGARNSVTAAAKYPDLVRSV--VA 128
Cdd:COG3545    37 DLDDWLAALDAAVAAadGPVVLVAHSLGCLAVAHWAARLPRKVAGAllVA 86
 
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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