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Conserved domains on  [gi|116096349|gb|ABJ61500|]
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Alpha/beta superfamily hydrolase [Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293]

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, ...
 1-236 6.77e-43

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: 144.76  E-value: 6.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   1 MKTVTKVMSDGTKIVYDEYGNDQlKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNTKKSIDMADVIRDI 80
Cdd:COG0596    1 MSTPRFVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  81 DELRRELSIDKIIIVGYSDGANIALKYAVENQNHVSRMVLNapnvtadgvyrilwwGDAIARFgTELFSPISQKARRRHM 160
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV---------------DEVLAAL-AEPLRRPGLAPEALAA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116096349 161 QLHVMSEPlDItRAQLKVLTIPILFVIGQFD-IVKRQHIESISKIMPVAKVMILRGHGHFVTYTNPRKFAQLITPFL 236
Cdd:COG0596  144 LLRALART-DL-RERLARITVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-236 6.77e-43

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: 144.76  E-value: 6.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   1 MKTVTKVMSDGTKIVYDEYGNDQlKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNTKKSIDMADVIRDI 80
Cdd:COG0596    1 MSTPRFVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  81 DELRRELSIDKIIIVGYSDGANIALKYAVENQNHVSRMVLNapnvtadgvyrilwwGDAIARFgTELFSPISQKARRRHM 160
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV---------------DEVLAAL-AEPLRRPGLAPEALAA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116096349 161 QLHVMSEPlDItRAQLKVLTIPILFVIGQFD-IVKRQHIESISKIMPVAKVMILRGHGHFVTYTNPRKFAQLITPFL 236
Cdd:COG0596  144 LLRALART-DL-RERLARITVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 25-225 1.54e-20

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: 87.17  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   25 KTVFLLHGNGSSAHYFKRQLPS-YTAYFHVIAIDSRGHGRSTNTKKSIDM--ADVIRDIDELRRELSIDKIIIVGYSDGA 101
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  102 NIALKYAVENQNHVSRMVLNAPNVTA--------DGVYRILWWGDAIARFGTEL-FSPISQKARRRH---MQLHVMSEPL 169
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPheldeadrFILALFPGFFDGFVADFAPNpLGRLVAKLLALLllrLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  170 DITRAQLKVLT----------------------------IPILFVIGQFD-IVKRQHIESISKIMPVAKVMILRGHGHFV 220
Cdd:pfam00561 161 NKRFPSGDYALakslvtgallfietwstelrakflgrldEPTLIIWGDQDpLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ....*
gi 116096349  221 TYTNP 225
Cdd:pfam00561 241 FLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 24-236 5.19e-16

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 74.94  E-value: 5.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   24 LKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNTK--KSIDMADVIRDI-DELRRELSIDKIIIVGYSDG 100
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSdiERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  101 ANIALKYAVENQNHVSRMVLNAPN----VTADGVYRIL---WWGDAIARFGTE----------LFSpiSQK--------- 154
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLILESGSpglqTEEERAARRQndeQLAQRFEQEGLEaflddwyqqpLFA--SQKnlppeqrqa 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  155 --ARRRHMQLHVMSEPLDIT--------RAQLKVLTIPILFVIGQFDiVKRQHI-ESISKIMPVAKVMILRGHGHFVTYT 223
Cdd:TIGR03695 160 lrAERLANNPEGLAKMLRATglgkqpslWPKLQALKIPVLYLCGERD-EKFVQIaKEMQKLIPNLTLHIIPNAGHNIHLE 238

                         250
                  ....*....|...
gi 116096349  224 NPRKFAQLITPFL 236
Cdd:TIGR03695 239 NPEAFAKILLAFL 251
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 26-242 4.31e-15

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 73.79  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  26 TVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTN---TKKSIDMADV--IRDIDELRRELSIDKIIIVGYSDG 100
Cdd:PLN02894 107 TLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRpdfTCKSTEETEAwfIDSFEEWRKAKNLSNFILLGHSFG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349 101 ANIALKYAVENQNHVSRMVLNAP--------------------------------NVTADGVYRILW-WGD------AIA 141
Cdd:PLN02894 187 GYVAAKYALKHPEHVQHLILVGPagfssesddksewltkfratwkgavlnhlwesNFTPQKIIRGLGpWGPnlvrryTTA 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349 142 RFGTE-----------------LFSPISQKARRRHMQLHVMS------EPLDITRAQLKVltiPILFVIGQFDIVKRQHI 198
Cdd:PLN02894 267 RFGAHstgdilseeesklltdyVYHTLAAKASGELCLKYIFSfgafarKPLLESASEWKV---PTTFIYGRHDWMNYEGA 343

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 116096349 199 ESISKIMPV-AKVMILRGHGHFVTYTNPRKFAQLIT----PFLLGGKHE 242
Cdd:PLN02894 344 VEARKRMKVpCEIIRVPQGGHFVFLDNPSGFHSAVLyacrKYLSPDREE 392
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-236 6.77e-43

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: 144.76  E-value: 6.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   1 MKTVTKVMSDGTKIVYDEYGNDQlKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNTKKSIDMADVIRDI 80
Cdd:COG0596    1 MSTPRFVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  81 DELRRELSIDKIIIVGYSDGANIALKYAVENQNHVSRMVLNapnvtadgvyrilwwGDAIARFgTELFSPISQKARRRHM 160
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV---------------DEVLAAL-AEPLRRPGLAPEALAA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116096349 161 QLHVMSEPlDItRAQLKVLTIPILFVIGQFD-IVKRQHIESISKIMPVAKVMILRGHGHFVTYTNPRKFAQLITPFL 236
Cdd:COG0596  144 LLRALART-DL-RERLARITVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
8-236 5.87e-23

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 92.76  E-value: 5.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   8 MSDGTKIVYDEYGNDQL--KTVFLLHGNGSSAHYFKRQLPSYTAY-FHVIAIDSRGHGRSTNTKKSI-DMADVIRDIDEL 83
Cdd:COG2267   10 TRDGLRLRGRRWRPAGSprGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  84 RRELSID---KIIIVGYSDGANIALKYAVENQNHVSRMVLNAPNVTADGVYRILwwgdaiARFGTELFspisqkarrrhm 160
Cdd:COG2267   90 LDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPS------ARWLRALR------------ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116096349 161 qlhvmsepldiTRAQLKVLTIPILFVIGQFD-IVKRQHIESI-SKIMPVAKVMILRGHGHFVTY-TNPRKFAQLITPFL 236
Cdd:COG2267  152 -----------LAEALARIDVPVLVLHGGADrVVPPEAARRLaARLSPDVELVLLPGARHELLNePAREEVLAAILAWL 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 25-225 1.54e-20

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: 87.17  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   25 KTVFLLHGNGSSAHYFKRQLPS-YTAYFHVIAIDSRGHGRSTNTKKSIDM--ADVIRDIDELRRELSIDKIIIVGYSDGA 101
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  102 NIALKYAVENQNHVSRMVLNAPNVTA--------DGVYRILWWGDAIARFGTEL-FSPISQKARRRH---MQLHVMSEPL 169
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPheldeadrFILALFPGFFDGFVADFAPNpLGRLVAKLLALLllrLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  170 DITRAQLKVLT----------------------------IPILFVIGQFD-IVKRQHIESISKIMPVAKVMILRGHGHFV 220
Cdd:pfam00561 161 NKRFPSGDYALakslvtgallfietwstelrakflgrldEPTLIIWGDQDpLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ....*
gi 116096349  221 TYTNP 225
Cdd:pfam00561 241 FLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 24-236 5.19e-16

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 74.94  E-value: 5.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   24 LKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNTK--KSIDMADVIRDI-DELRRELSIDKIIIVGYSDG 100
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSdiERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  101 ANIALKYAVENQNHVSRMVLNAPN----VTADGVYRIL---WWGDAIARFGTE----------LFSpiSQK--------- 154
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLILESGSpglqTEEERAARRQndeQLAQRFEQEGLEaflddwyqqpLFA--SQKnlppeqrqa 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  155 --ARRRHMQLHVMSEPLDIT--------RAQLKVLTIPILFVIGQFDiVKRQHI-ESISKIMPVAKVMILRGHGHFVTYT 223
Cdd:TIGR03695 160 lrAERLANNPEGLAKMLRATglgkqpslWPKLQALKIPVLYLCGERD-EKFVQIaKEMQKLIPNLTLHIIPNAGHNIHLE 238

                         250
                  ....*....|...
gi 116096349  224 NPRKFAQLITPFL 236
Cdd:TIGR03695 239 NPEAFAKILLAFL 251
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 26-242 4.31e-15

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 73.79  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  26 TVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTN---TKKSIDMADV--IRDIDELRRELSIDKIIIVGYSDG 100
Cdd:PLN02894 107 TLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRpdfTCKSTEETEAwfIDSFEEWRKAKNLSNFILLGHSFG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349 101 ANIALKYAVENQNHVSRMVLNAP--------------------------------NVTADGVYRILW-WGD------AIA 141
Cdd:PLN02894 187 GYVAAKYALKHPEHVQHLILVGPagfssesddksewltkfratwkgavlnhlwesNFTPQKIIRGLGpWGPnlvrryTTA 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349 142 RFGTE-----------------LFSPISQKARRRHMQLHVMS------EPLDITRAQLKVltiPILFVIGQFDIVKRQHI 198
Cdd:PLN02894 267 RFGAHstgdilseeesklltdyVYHTLAAKASGELCLKYIFSfgafarKPLLESASEWKV---PTTFIYGRHDWMNYEGA 343

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 116096349 199 ESISKIMPV-AKVMILRGHGHFVTYTNPRKFAQLIT----PFLLGGKHE 242
Cdd:PLN02894 344 VEARKRMKVpCEIIRVPQGGHFVFLDNPSGFHSAVLyacrKYLSPDREE 392
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 22-235 4.65e-15

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 72.16  E-value: 4.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   22 DQLKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTnTKKSIDMADVIRDIdelrRELSIDKIIIVGYSDGA 101
Cdd:TIGR01738   2 QGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR-GFGPLSLADMAEAI----AAQAPDPAIWLGWSLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  102 NIALKYAVENQNHVSRMVLNA--PNVTADGVYRILWWGDAIARFgTELFSPISQKARRRHMQLHVMSEP----------- 168
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTVAssPCFSAREDWPEGIKPDVLTGF-QQQLSDDYQRTIERFLALQTLGTPtarqdaralkq 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  169 ----------------LDI-----TRAQLKVLTIPILFVIGQFD-IVKRQHIESISKIMPVAKVMILRGHGHFVTYTNPR 226
Cdd:TIGR01738 156 tllarptpnvqvlqagLEIlatvdLRQPLQNISVPFLRLYGYLDgLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAE 235


                  ....*....
gi 116096349  227 KFAQLITPF 235
Cdd:TIGR01738 236 AFCALLVAF 244
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
25-236 1.20e-13

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 68.04  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  25 KTVFLLHGNGSS---AHYFKRQLpsYTAYFHVIAIDSRGHGRSTNtkksiDMADV-IRD-IDELRRELSI-----DKIII 94
Cdd:COG1647   16 KGVLLLHGFTGSpaeMRPLAEAL--AKAGYTVYAPRLPGHGTSPE-----DLLKTtWEDwLEDVEEAYEIlkagyDKVIV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  95 VGYSDGANIALKYAvENQNHVSRMVLNAPNVTADGVYRIL-----WWGDAIARFGTELFSPISQKARRRHM---QLHVMS 166
Cdd:COG1647   89 IGLSMGGLLALLLA-ARYPDVAGLVLLSPALKIDDPSAPLlpllkYLARSLRGIGSDIEDPEVAEYAYDRTplrALAELQ 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116096349 167 EPLDITRAQLKVLTIPILFVIGQFDIVkrQHIESISKIM-----PVAKVMILRGHGHFVTYTNPRK-FAQLITPFL 236
Cdd:COG1647  168 RLIREVRRDLPKITAPTLIIQSRKDEV--VPPESARYIYerlgsPDKELVWLEDSGHVITLDKDREeVAEEILDFL 241
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
9-236 6.41e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 65.81  E-value: 6.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   9 SDGTKI---VYDEYGNDQLKTVFLLHGNGSSA-HYFKRQLPSYTAY-FHVIAIDSRGHGRSTNTKKSIDMADVIRDIDEL 83
Cdd:COG1506    5 ADGTTLpgwLYLPADGKKYPVVVYVHGGPGSRdDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  84 RRELSID--KIIIVGYSDGANIALKYAVENQNHVSRMVLNAPNVTADGVYRILWWGDAIarfgtELFSPISQKARRRHMQ 161
Cdd:COG1506   85 AARPYVDpdRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTER-----LMGGPWEDPEAYAARS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349 162 LHvmseplditrAQLKVLTIPILFVIGQFD-IVKRQHIESISKIMPVAKV----MILRGHGHFVTYTNPRKFAQLITPFL 236
Cdd:COG1506  160 PL----------AYADKLKTPLLLIHGEADdRVPPEQAERLYEALKKAGKpvelLVYPGEGHGFSGAGAPDYLERILDFL 229
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 27-231 2.12e-12

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 64.03  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   27 VFLLHGNGSSAHYFKRQLpsyTAYFHVIAIDSRGHGRSTntKKSIDMADVIRDIDELRRELSIDKIIIVGYSDGANIALK 106
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALL---AAGVAVLAPDLPGHGSSS--PPPLDLADLADLAALLDELGAARPVVLVGHSLGGAVALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  107 YAveNQNHVSRMVLNAPNVTADGVYRILWWGDAIARFGT------------ELFSPISQKARRRHM---QLHVMSEPLDI 171
Cdd:pfam12697  76 AA--AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAapawlaaeslarGFLDDLPADAEWAAAlarLAALLAALALL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  172 TRAQLKVLTIPILFVIGQfDIVKRQHIESISKIMPVAKVMILRGHGHFVtYTNPRKFAQL 231
Cdd:pfam12697 154 PLAAWRDLPVPVLVLAEE-DRLVPELAQRLLAALAGARLVVLPGAGHLP-LDDPEEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 25-193 5.06e-12

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: 63.39  E-value: 5.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   25 KTVFLLHGNGSS-------AHYFKRQlpsytaYFHVIAIDSRGHGRSTNTKKSID-MADVIRD----IDELRRELSIDKI 92
Cdd:pfam12146   5 AVVVLVHGLGEHsgryahlADALAAQ------GFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDldtfVDKIREEHPGLPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   93 IIVGYSDGANIALKYAVENQNHVSRMVLNAPNVtADGVYRILWWGDAIARF-----------GTELFSPIS-----QKA- 155
Cdd:pfam12146  79 FLLGHSMGGLIAALYALRYPDKVDGLILSAPAL-KIKPYLAPPILKLLAKLlgklfprlrvpNNLLPDSLSrdpevVAAy 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116096349  156 -----RRRHMQLHVMSEPLDIT---RAQLKVLTIPILFVIGQFDIV 193
Cdd:pfam12146 158 aadplVHGGISARTLYELLDAGerlLRRAAAITVPLLLLHGGADRV 203
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 1-236 9.30e-12

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 63.01  E-value: 9.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   1 MKTVTKVMSDGTKIVYDEY----GNDQLKTVFLLHGNGS----SAHYFKRqlpsYTAY-FHVIAIDSRGHGRSTNTKKSI 71
Cdd:COG1073   10 KEDVTFKSRDGIKLAGDLYlpagASKKYPAVVVAHGNGGvkeqRALYAQR----LAELgFNVLAFDYRGYGESEGEPREE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  72 DMADvIRD----IDELRRELSID--KIIIVGYSDGANIALKYAVENQNhVSRMVLNAP--NVTADGVYRilwwgdaIARF 143
Cdd:COG1073   86 GSPE-RRDaraaVDYLRTLPGVDpeRIGLLGISLGGGYALNAAATDPR-VKAVILDSPftSLEDLAAQR-------AKEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349 144 GTELFSPISQKARRRHMQLhvMSEPLDITrAQLKVLTIPILFVIGQFD-IVKRQHIESISKIMPVAK-VMILRGHGHFVT 221
Cdd:COG1073  157 RGAYLPGVPYLPNVRLASL--LNDEFDPL-AKIEKISRPLLFIHGEKDeAVPFYMSEDLYEAAAEPKeLLIVPGAGHVDL 233

                        250
                 ....*....|....*.
gi 116096349 222 Y-TNPRKFAQLITPFL 236
Cdd:COG1073  234 YdRPEEEYFDKLAEFF 249
YpfH COG0400
Predicted esterase [General function prediction only];
26-120 9.32e-10

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 56.45  E-value: 9.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  26 TVFLLHGNGSSAHYFK---RQLPSytAYFHVIAIDSR----GHGRS----TNTKKSIDMADVIRD-------IDELRREL 87
Cdd:COG0400    7 LVVLLHGYGGDEEDLLplaPELAL--PGAAVLAPRAPvpegPGGRAwfdlSFLEGREDEEGLAAAaealaafIDELEARY 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 116096349  88 SID--KIIIVGYSDGANIALKYAVENQNHVSRMVL 120
Cdd:COG0400   85 GIDpeRIVLAGFSQGAAMALSLALRRPELLAGVVA 119
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
25-116 4.25e-09

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 55.92  E-value: 4.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  25 KTVFLLHG-NGSS-AHY---FKRQLpsYTAYFHVIAIDSRGHGRSTNTKK----SIDMADVIRDIDELRRELSIDKIIIV 95
Cdd:COG0429   62 PLVVLLHGlEGSSdSHYargLARAL--YARGWDVVRLNFRGCGGEPNLLPrlyhSGDTEDLVWVLAHLRARYPYAPLYAV 139

                         90       100
                 ....*....|....*....|.
gi 116096349  96 GYSDGANIALKYAVENQNHVS 116
Cdd:COG0429  140 GFSLGGNLLLKYLGEQGDDAP 160
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 1-128 1.93e-07

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 51.03  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   1 MKTVTKVMSDGTKIVYDEYGNDQLKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNTKK----SIDMADV 76
Cdd:PLN03084 104 MGAQSQASSDLFRWFCVESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPgygfNYTLDEY 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116096349  77 IRDIDELRRELSIDKIIIVGYSDGANIALKYAVENQNHVSRMVLNAPNVTAD 128
Cdd:PLN03084 184 VSSLESLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNPPLTKE 235
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 27-113 2.47e-06

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 47.14  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  27 VFLlHG-NGSSAHYfkRQLPSYTAYFHVIAIDSRGHGRSTNTKkSIDMADVIRDIDELRRELSIDKIIIVGYSDGANIAL 105
Cdd:PRK11126   6 VFL-HGlLGSGQDW--QPVGEALPDYPRLYIDLPGHGGSAAIS-VDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAM 81


                 ....*...
gi 116096349 106 KYAVENQN 113
Cdd:PRK11126  82 YYACQGLA 89
PRK05855 PRK05855
SDR family oxidoreductase;
5-68 2.88e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 47.67  E-value: 2.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116096349   5 TKVMSDGTKIVYDEYGNDQLKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNTK 68
Cdd:PRK05855   6 TVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPK 69
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-123 3.79e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 47.25  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  10 DGTKIVYDEYGNDQLKTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRSTNT--KKSID-MAD-VIRDIDelrr 85
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAvgAGSLDeLAAaVLAFLD---- 192

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 116096349  86 ELSIDKIIIVGYSDGANIALKYAVENQNHVSRMVLNAP 123
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 26-104 4.47e-06

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: 46.23  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   26 TVFLLHGNGSSAHYFK---RQLPSYTAyfhVIAIDSRGHGRSTNTKKSID-MADVIrdIDELRRELSIDKIIIVGYSDGA 101
Cdd:pfam00975   2 PLFCFPPAGGSASSFRslaRRLPPPAE---VLAVQYPGRGRGEPPLNSIEaLADEY--AEALRQIQPEGPYALFGHSMGG 76


                  ...
gi 116096349  102 NIA 104
Cdd:pfam00975  77 MLA 79
PLN02578 PLN02578
hydrolase
 11-120 1.51e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.22  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  11 GTKIVYDEYGNDQlkTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRStnTKKSIDM-ADVIRD-IDELRRELS 88
Cdd:PLN02578  75 GHKIHYVVQGEGL--PIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWS--DKALIEYdAMVWRDqVADFVKEVV 150

                         90       100       110
                 ....*....|....*....|....*....|..
gi 116096349  89 IDKIIIVGYSDGANIALKYAVENQNHVSRMVL 120
Cdd:PLN02578 151 KEPAVLVGNSLGGFTALSTAVGYPELVAGVAL 182
PHA02857 PHA02857
monoglyceride lipase; Provisional
 27-132 1.18e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 42.18  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349  27 VFLLHGNGSSAHYFKRQLPSYTAY-FHVIAIDSRGHGRSTNTKKSID-----MADVIRDIDELRRELSIDKIIIVGYSDG 100
Cdd:PHA02857  28 VFISHGAGEHSGRYEELAENISSLgILVFSHDHIGHGRSNGEKMMIDdfgvyVRDVVQHVVTIKSTYPGVPVFLLGHSMG 107

                         90       100       110
                 ....*....|....*....|....*....|..
gi 116096349 101 ANIALKYAVENQNHVSRMVLNAPNVTADGVYR 132
Cdd:PHA02857 108 ATISILAAYKNPNLFTAMILMSPLVNAEAVPR 139
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 25-120 1.33e-04

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 42.92  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   25 KTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRS--------TNTKKSIDMADVIRDIDELRRELSIDKIIIVG 96
Cdd:PLN02980 1372 SVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhakeTQTEPTLSVELVADLLYKLIEHITPGKVTLVG 1451

                          90       100
                  ....*....|....*....|....
gi 116096349   97 YSDGANIALKYAVENQNHVSRMVL 120
Cdd:PLN02980 1452 YSMGARIALYMALRFSDKIEGAVI 1475
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-108 8.81e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 39.59  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116096349   1 MKTVTkvmSDGTKIVYDEYGNDQlkTVFLLHGNGSSAHYFKRQLPSYTAYFHVIAIDSRGHGRStnTKKSID--MADVIR 78
Cdd:PRK03592   9 MRRVE---VLGSRMAYIETGEGD--PIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGAS--DKPDIDytFADHAR 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 116096349  79 DIDELRRELSIDKIIIVGYSDGANIALKYA 108
Cdd:PRK03592  82 YLDAWFDALGLDDVVLVGHDWGSALGFDWA 111
 
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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