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Conserved domains on  [gi|2184988178|ref|WP_236502496|]
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alpha/beta fold hydrolase [Pseudomonas tremae]

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, ...
6-269 3.04e-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: 151.69  E-value: 3.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   6 IDGKALHYSDQG-TGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGfPEGTRNLDDLTRHALALLDHLN 84
Cdd:COG0596     9 VDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDALG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  85 IERCSIVGLSVGGMWGAIAALLAPERITGLVLMDtylgketeatkayyfslinkleetgafpaPLLDIVVPIFFRPGIDP 164
Cdd:COG0596    88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAP 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 165 QSpLYQAFRAALAGMNAEQLRQTIAPlgrmifgrddrlglieqlnadtTLVMCGDADIPRPPEETREMAGLI-GCPYVLV 243
Cdd:COG0596   139 EA-LAALLRALARTDLRERLARITVP----------------------TLVIWGEKDPIVPPALARRLAELLpNAELVVL 195
                         250       260
                  ....*....|....*....|....*.
gi 2184988178 244 PEAGHIANLENPDFVSGALMTFLARV 269
Cdd:COG0596   196 PGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
6-269 3.04e-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: 151.69  E-value: 3.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   6 IDGKALHYSDQG-TGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGfPEGTRNLDDLTRHALALLDHLN 84
Cdd:COG0596     9 VDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDALG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  85 IERCSIVGLSVGGMWGAIAALLAPERITGLVLMDtylgketeatkayyfslinkleetgafpaPLLDIVVPIFFRPGIDP 164
Cdd:COG0596    88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAP 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 165 QSpLYQAFRAALAGMNAEQLRQTIAPlgrmifgrddrlglieqlnadtTLVMCGDADIPRPPEETREMAGLI-GCPYVLV 243
Cdd:COG0596   139 EA-LAALLRALARTDLRERLARITVP----------------------TLVIWGEKDPIVPPALARRLAELLpNAELVVL 195
                         250       260
                  ....*....|....*....|....*.
gi 2184988178 244 PEAGHIANLENPDFVSGALMTFLARV 269
Cdd:COG0596   196 PGAGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
11-267 3.67e-38

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


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 134.41  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  11 LHYSDQGTG---PVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDgFPEGTRNLDDLTRHALALLDHLNIER 87
Cdd:TIGR02427   2 LHYRLDGAAdgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSD-APEGPYSIEDLADDVLALLDHLGIER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  88 CSIVGLSVGGMWGAIAALLAPERITGLVLMDT---YLGKETEATKayyfslINKLEETGAfpAPLLDIVVPIFFRPGI-D 163
Cdd:TIGR02427  81 AVFCGLSLGGLIAQGLAARRPDRVRALVLSNTaakIGTPESWNAR------IAAVRAEGL--AALADAVLERWFTPGFrE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 164 PQSPLYQAFRAALAGMNAEQLRQTIAPLGRMIFgrDDRLGLIeqlnADTTLVMCGDADIPRPPEETREMAGLI-GCPYVL 242
Cdd:TIGR02427 153 AHPARLDLYRNMLVRQPPDGYAGCCAAIRDADF--RDRLGAI----AVPTLCIAGDQDGSTPPELVREIADLVpGARFAE 226
                         250       260
                  ....*....|....*....|....*
gi 2184988178 243 VPEAGHIANLENPDFVSGALMTFLA 267
Cdd:TIGR02427 227 IRGAGHIPCVEQPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
20-255 4.92e-18

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: 81.01  E-value: 4.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  20 PVVLLGHSYLWDKGMWSAQLDTLA-SQYRVIVPDLWGHGESDGFPEGTR-NLDDLTRHALALLDHLNIERCSIVGLSVGG 97
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  98 MWGAIAALLAPERITGLVLMDTyLGKETEATKAYYFSLINKLEETGAFPAPLL---------DIVVPIFFRpgIDPQSPL 168
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFPGFFDGFVADFApnplgrlvaKLLALLLLR--LRLLKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 169 YQAFRAALAGM-NAEQLRQTIAPLGRMIFGRDDRLGLIEQLNADtTLVMCGDADIPRPPEETREMAGLIGCPYVLV-PEA 246
Cdd:pfam00561 158 PLLNKRFPSGDyALAKSLVTGALLFIETWSTELRAKFLGRLDEP-TLIIWGDQDPLVPPQALEKLAQLFPNARLVViPDA 236

                  ....*....
gi 2184988178 247 GHIANLENP 255
Cdd:pfam00561 237 GHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
6-269 3.27e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 77.29  E-value: 3.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   6 IDGKALHYSDQGTG---PVVLLgHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDgfPE-GTRNLDDLTRHALALLD 81
Cdd:PRK14875  116 IGGRTVRYLRLGEGdgtPVVLI-HGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS--KAvGAGSLDELAAAVLAFLD 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  82 HLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTY-LGKE----------TEATKAyyfSLINKLEETGAFPA--- 147
Cdd:PRK14875  193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAgLGPEingdyidgfvAAESRR---ELKPVLELLFADPAlvt 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 148 -PLLDIVVPIFFRPGI-DPQSPLyqAFRAALAGMNAEQLRQTIAPLG---RMIFGRDDRLglieqlnadttlvmcgdadI 222
Cdd:PRK14875  270 rQMVEDLLKYKRLDGVdDALRAL--ADALFAGGRQRVDLRDRLASLAipvLVIWGEQDRI-------------------I 328
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2184988178 223 PRPpeETREMAGLIGCpyVLVPEAGHIANLENPDFVSGALMTFLARV 269
Cdd:PRK14875  329 PAA--HAQGLPDGVAV--HVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
6-269 3.04e-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: 151.69  E-value: 3.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   6 IDGKALHYSDQG-TGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGfPEGTRNLDDLTRHALALLDHLN 84
Cdd:COG0596     9 VDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDALG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  85 IERCSIVGLSVGGMWGAIAALLAPERITGLVLMDtylgketeatkayyfslinkleetgafpaPLLDIVVPIFFRPGIDP 164
Cdd:COG0596    88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAP 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 165 QSpLYQAFRAALAGMNAEQLRQTIAPlgrmifgrddrlglieqlnadtTLVMCGDADIPRPPEETREMAGLI-GCPYVLV 243
Cdd:COG0596   139 EA-LAALLRALARTDLRERLARITVP----------------------TLVIWGEKDPIVPPALARRLAELLpNAELVVL 195
                         250       260
                  ....*....|....*....|....*.
gi 2184988178 244 PEAGHIANLENPDFVSGALMTFLARV 269
Cdd:COG0596   196 PGAGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
11-267 3.67e-38

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


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 134.41  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  11 LHYSDQGTG---PVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDgFPEGTRNLDDLTRHALALLDHLNIER 87
Cdd:TIGR02427   2 LHYRLDGAAdgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSD-APEGPYSIEDLADDVLALLDHLGIER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  88 CSIVGLSVGGMWGAIAALLAPERITGLVLMDT---YLGKETEATKayyfslINKLEETGAfpAPLLDIVVPIFFRPGI-D 163
Cdd:TIGR02427  81 AVFCGLSLGGLIAQGLAARRPDRVRALVLSNTaakIGTPESWNAR------IAAVRAEGL--AALADAVLERWFTPGFrE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 164 PQSPLYQAFRAALAGMNAEQLRQTIAPLGRMIFgrDDRLGLIeqlnADTTLVMCGDADIPRPPEETREMAGLI-GCPYVL 242
Cdd:TIGR02427 153 AHPARLDLYRNMLVRQPPDGYAGCCAAIRDADF--RDRLGAI----AVPTLCIAGDQDGSTPPELVREIADLVpGARFAE 226
                         250       260
                  ....*....|....*....|....*
gi 2184988178 243 VPEAGHIANLENPDFVSGALMTFLA 267
Cdd:TIGR02427 227 IRGAGHIPCVEQPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
20-255 4.92e-18

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: 81.01  E-value: 4.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  20 PVVLLGHSYLWDKGMWSAQLDTLA-SQYRVIVPDLWGHGESDGFPEGTR-NLDDLTRHALALLDHLNIERCSIVGLSVGG 97
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  98 MWGAIAALLAPERITGLVLMDTyLGKETEATKAYYFSLINKLEETGAFPAPLL---------DIVVPIFFRpgIDPQSPL 168
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFPGFFDGFVADFApnplgrlvaKLLALLLLR--LRLLKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 169 YQAFRAALAGM-NAEQLRQTIAPLGRMIFGRDDRLGLIEQLNADtTLVMCGDADIPRPPEETREMAGLIGCPYVLV-PEA 246
Cdd:pfam00561 158 PLLNKRFPSGDyALAKSLVTGALLFIETWSTELRAKFLGRLDEP-TLIIWGDQDPLVPPQALEKLAQLFPNARLVViPDA 236

                  ....*....
gi 2184988178 247 GHIANLENP 255
Cdd:pfam00561 237 GHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
6-269 3.27e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 77.29  E-value: 3.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   6 IDGKALHYSDQGTG---PVVLLgHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDgfPE-GTRNLDDLTRHALALLD 81
Cdd:PRK14875  116 IGGRTVRYLRLGEGdgtPVVLI-HGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS--KAvGAGSLDELAAAVLAFLD 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  82 HLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTY-LGKE----------TEATKAyyfSLINKLEETGAFPA--- 147
Cdd:PRK14875  193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAgLGPEingdyidgfvAAESRR---ELKPVLELLFADPAlvt 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 148 -PLLDIVVPIFFRPGI-DPQSPLyqAFRAALAGMNAEQLRQTIAPLG---RMIFGRDDRLglieqlnadttlvmcgdadI 222
Cdd:PRK14875  270 rQMVEDLLKYKRLDGVdDALRAL--ADALFAGGRQRVDLRDRLASLAipvLVIWGEQDRI-------------------I 328
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2184988178 223 PRPpeETREMAGLIGCpyVLVPEAGHIANLENPDFVSGALMTFLARV 269
Cdd:PRK14875  329 PAA--HAQGLPDGVAV--HVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
7-155 8.30e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 68.88  E-value: 8.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   7 DGKALHY----SDQGTGPVVLLGHSYLWDKGMWSAQLDTLASQ-YRVIVPDLWGHGESDGFPEGTRNLDDLTRHALALLD 81
Cdd:COG2267    12 DGLRLRGrrwrPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  82 HLNIE---RCSIVGLSVGGMWGAIAALLAPERITGLVLMDT-YLGKETEATKAYYFSLINKLEETGAFPAPLL------D 151
Cdd:COG2267    92 ALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPaYRADPLLGPSARWLRALRLAEALARIDVPVLvlhggaD 171

                  ....
gi 2184988178 152 IVVP 155
Cdd:COG2267   172 RVVP 175
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
1-121 1.12e-11

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 63.86  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   1 MPNLLIDGKALHYSDQGTGPVVLLGH-----SYLWDKGMwsaqlDTLASQYRVIVPDLWGHGESDGFPEGTRnLDDLTRH 75
Cdd:PRK03592    9 MRRVEVLGSRMAYIETGEGDPIVFLHgnptsSYLWRNII-----PHLAGLGRCLAPDLIGMGASDKPDIDYT-FADHARY 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2184988178  76 ALALLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYL 121
Cdd:PRK03592   83 LDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIV 128
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
7-268 2.04e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 59.26  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   7 DGKALHY-----SDQGTGPVVLLGHSYLWDK-GMWSAQLDTLASQ-YRVIVPDLWGHGESDGFPeGTRNLDDLTR--HAL 77
Cdd:COG1506     6 DGTTLPGwlylpADGKKYPVVVYVHGGPGSRdDSFLPLAQALASRgYAVLAPDYRGYGESAGDW-GGDEVDDVLAaiDYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  78 ALLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMdtylgketeatkAYYFSLINKLEETGAFPAPLLDivVPIF 157
Cdd:COG1506    85 AARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVAL------------AGVSDLRSYYGTTREYTERLMG--GPWE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 158 FRPGIDPQSPLYqafraalagmNAEQLRqtiAPLgrmifgrddrlglieqlnadttLVMCGDADIPRPPEETREM---AG 234
Cdd:COG1506   151 DPEAYAARSPLA----------YADKLK---TPL----------------------LLIHGEADDRVPPEQAERLyeaLK 195
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2184988178 235 LIGCP--YVLVPEAGH-IANLENPDFVsGALMTFLAR 268
Cdd:COG1506   196 KAGKPveLLVYPGEGHgFSGAGAPDYL-ERILDFLDR 231
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
42-269 1.32e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 57.26  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  42 LASQ-YRVIVPDLWGHGESDGFPEGTRnLDDLTRHALALLDHL--NIERCSIVGLSVGgmwGAIAALLAPER--ITGLVL 116
Cdd:COG1647    38 LAKAgYTVYAPRLPGHGTSPEDLLKTT-WEDWLEDVEEAYEILkaGYDKVIVIGLSMG---GLLALLLAARYpdVAGLVL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 117 MDTYLgketeatkayyfslinKLEETGAFPAPLLDIVVPIFFRPGIDPQSPLYQAFRAALAGMNAeqlrqtIAPLGRMIf 196
Cdd:COG1647   114 LSPAL----------------KIDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLRA------LAELQRLI- 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2184988178 197 grDDRLGLIEQLNADtTLVMCGDADIPRPPEETREMAGLIGCP---YVLVPEAGH-IANLENPDFVSGALMTFLARV 269
Cdd:COG1647   171 --REVRRDLPKITAP-TLIIQSRKDEVVPPESARYIYERLGSPdkeLVWLEDSGHvITLDKDREEVAEEILDFLERL 244
PRK10673 PRK10673
esterase;
42-144 2.21e-08

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 53.58  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  42 LASQYRVIVPDLWGHGESDGFPEgtRNLDDLTRHALALLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTyl 121
Cdd:PRK10673   39 LVNDHDIIQVDMRNHGLSPRDPV--MNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDI-- 114
                          90       100       110
                  ....*....|....*....|....*....|
gi 2184988178 122 gketeATKAYY-------FSLINKLEETGA 144
Cdd:PRK10673  115 -----APVDYHvrrhdeiFAAINAVSEAGA 139
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
11-121 2.54e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 53.71  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  11 LHYSDQGTGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGES---DGFpegTRNLDDLTRHALALLDHLNIER 87
Cdd:PRK03204   26 IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSerpSGF---GYQIDEHARVIGEFVDHLGLDR 102
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2184988178  88 CSIVGLSVGGMWGAIAALLAPERITGLVLMDTYL 121
Cdd:PRK03204  103 YLSMGQDWGGPISMAVAVERADRVRGVVLGNTWF 136
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
8-268 3.14e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 53.59  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   8 GKALHYSDQGT-GPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESD-----GFPEGT-RNLDDLTRHALALL 80
Cdd:PLN02824   17 GYNIRYQRAGTsGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDkpnprSAPPNSfYTFETWGEQLNDFC 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  81 DHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLG----------------------KETEATKAYYFSLI-- 136
Cdd:PLN02824   97 SDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLINISLRglhikkqpwlgrpfikafqnllRETAVGKAFFKSVAtp 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 137 ----NKLEETGAFPAPLLDIVVPIFFRPGIDPQS-PLYQAFRAALAG-MNAEQLRQTIAPLgrmifgrddrlglieqlna 210
Cdd:PLN02824  177 etvkNILCQCYHDDSAVTDELVEAILRPGLEPGAvDVFLDFISYSGGpLPEELLPAVKCPV------------------- 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2184988178 211 dttLVMCGDADIPRPPEETREMAGLIGC-PYVLVPEAGHIANLENPDFVSGALMTFLAR 268
Cdd:PLN02824  238 ---LIAWGEKDPWEPVELGRAYANFDAVeDFIVLPGVGHCPQDEAPELVNPLIESFVAR 293
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
42-258 2.32e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 50.16  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  42 LASQYRVIVPDLWGHGESDGFPEGTRNLDDLTRHALALLDHLNIercSIVGLSVGGMwgaIAALLAPERITGLVLMDTYL 121
Cdd:pfam12697  18 LAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV---VLVGHSLGGA---VALAAAAAALVVGVLVAPLA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 122 GKETEAtkAYYFSLINKLEETGAFPAPLLDIVVPIFFrPGIDPQSPLYQAFRAALAGMNAEQLRQTIAPLGRMIfgrddr 201
Cdd:pfam12697  92 APPGLL--AALLALLARLGAALAAPAWLAAESLARGF-LDDLPADAEWAAALARLAALLAALALLPLAAWRDLP------ 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2184988178 202 lglieqlnaDTTLVMCGDADIPrPPEETREMAGLIGCPYVLVPEAGHiANLENPDFV 258
Cdd:pfam12697 163 ---------VPVLVLAEEDRLV-PELAQRLLAALAGARLVVLPGAGH-LPLDDPEEV 208
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
15-120 4.94e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 49.53  E-value: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  15 DQGTGPVVLLGHSYLWDKGMWSAQLDTLASQ-YRVIVPDLWGHGESDGFPegtRNLDDLTRH-ALALLDHL----NIERC 88
Cdd:COG1073    33 ASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESEGEP---REEGSPERRdARAAVDYLrtlpGVDPE 109
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2184988178  89 SIV--GLSvggMWGAIAALLAPE--RITGLVLMDTY 120
Cdd:COG1073   110 RIGllGIS---LGGGYALNAAATdpRVKAVILDSPF 142
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
52-248 1.35e-06

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: 48.36  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  52 DLWGHGESDGFPEGTRNLDDLTRHALALLDHL----NIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLGketea 127
Cdd:pfam12146  38 DHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIreehPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALK----- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 128 TKAYYFSLINKLEetgafpAPLLDIVVP-IFFRPGIDPQSPL-YQAFRAALAgmnAEQLRQTIAPLGrmiFGRDDRLG-- 203
Cdd:pfam12146 113 IKPYLAPPILKLL------AKLLGKLFPrLRVPNNLLPDSLSrDPEVVAAYA---ADPLVHGGISAR---TLYELLDAge 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2184988178 204 -LIEQLNADT--TLVMCGDADIPRPPEETREMAGLIGCP---YVLVPEAGH 248
Cdd:pfam12146 181 rLLRRAAAITvpLLLLHGGADRVVDPAGSREFYERAGSTdktLKLYPGLYH 231
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
11-121 2.89e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 47.66  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  11 LHYSDQGT--GPVVLLGH-----SYLWDKgMwsaqLDTLASQ-YRVIVPDLWGHGESDgfpEGTRnLDDLT--RHA---L 77
Cdd:PRK00870   36 MHYVDEGPadGPPVLLLHgepswSYLYRK-M----IPILAAAgHRVIAPDLIGFGRSD---KPTR-REDYTyaRHVewmR 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2184988178  78 ALLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYL 121
Cdd:PRK00870  107 SWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTGL 150
PLN02578 PLN02578
hydrolase
8-119 3.43e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 47.53  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   8 GKALHYSDQGTGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESD-GFPEGTRNLddLTRHALALLDHLNIE 86
Cdd:PLN02578   75 GHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDkALIEYDAMV--WRDQVADFVKEVVKE 152
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2184988178  87 RCSIVGLSVGGMWGAIAALLAPERITGLVLMDT 119
Cdd:PLN02578  153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
18-268 3.83e-06

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 46.76  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  18 TGPVVLLGHSYLWDKGMWSAQLDTLaSQYRVIVPDLWGHGESDGFPegTRNLDDLTRHALALLDHLNIERCSIVGLSVGG 97
Cdd:PRK11126    1 GLPWLVFLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHGGSAAIS--VDGFADVSRLLSQTLQSYNILPYWLVGYSLGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  98 ---MWGAIAALlaPERITGLVLMDTYLGKETEATKAyyfsliNKLEETGAFPAPlldivvpifFRpgidpQSPL------ 168
Cdd:PRK11126   78 riaMYYACQGL--AGGLCGLIVEGGNPGLQNAEERQ------ARWQNDRQWAQR---------FR-----QEPLeqvlad 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178 169 -YQafRAALAGMNAEQlRQTiaplgrMIFGRDDRLG-----------------LIEQLNADTT--LVMCGDADiprppEE 228
Cdd:PRK11126  136 wYQ--QPVFASLNAEQ-RQQ------LVAKRSNNNGaavaamleatslakqpdLRPALQALTFpfYYLCGERD-----SK 201
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2184988178 229 TREMAGLIGCPYVLVPEAGHIANLENPDFVSGALMTFLAR 268
Cdd:PRK11126  202 FQALAQQLALPLHVIPNAGHNAHRENPAAFAASLAQILRL 241
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
15-269 3.43e-05

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 45.23  E-value: 3.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   15 DQGTGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGFPEGTRNLDD--LTRHALA-----LLDHLNIER 87
Cdd:PLN02980  1367 QNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNHAKETQTEptLSVELVAdllykLIEHITPGK 1446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   88 CSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLGKETEATKAyyFSLINKLEETGAFPAPLLDIVVPIFFRPGI----- 162
Cdd:PLN02980  1447 VTLVGYSMGARIALYMALRFSDKIEGAVIISGSPGLKDEVARK--IRSAKDDSRARMLIDHGLEIFLENWYSGELwkslr 1524
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  163 -DPQspLYQAFRAALAGMNAEQLRQTIAPL--GRMIFGRDDrlglIEQLNADTTLVMcGDADIpRPPEETREMAGLIG-- 237
Cdd:PLN02980  1525 nHPH--FNKIVASRLLHKDVPSLAKLLSDLsiGRQPSLWED----LKQCDTPLLLVV-GEKDV-KFKQIAQKMYREIGks 1596
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2184988178  238 -----------CPYVLVPEAGHIANLENPDFVSGALMTFLARV 269
Cdd:PLN02980  1597 kesgndkgkeiIEIVEIPNCGHAVHLENPLPVIRALRKFLTRL 1639
PRK05855 PRK05855
SDR family oxidoreductase;
7-104 9.12e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 43.43  E-value: 9.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178   7 DGKALHYSDQG--TGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGfPEGTRN--LDDLTRHALALLDH 82
Cdd:PRK05855   11 DGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSA-PKRTAAytLARLADDFAAVIDA 89
                          90       100
                  ....*....|....*....|..
gi 2184988178  83 LNIERcsIVGLsVGGMWGAIAA 104
Cdd:PRK05855   90 VSPDR--PVHL-LAHDWGSIQG 108
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
16-115 5.39e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.39  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  16 QGTGPVVLLgHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGFpeGTRNLDDLTRHALALLDhlniERCSIVGLSV 95
Cdd:PRK10349   11 QGNVHLVLL-HGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGF--GALSLADMAEAVLQQAP----DKAIWLGWSL 83
                          90       100
                  ....*....|....*....|
gi 2184988178  96 GGMWGAIAALLAPERITGLV 115
Cdd:PRK10349   84 GGLVASQIALTHPERVQALV 103
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
14-118 1.15e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 39.82  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  14 SDQGTGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGFPEGTRNLDDLTRHALALLDHLNIERCSIVGL 93
Cdd:PLN02679   83 EVTSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFSYTMETWAELILDFLEEVVQKPTVLIGN 162
                          90       100
                  ....*....|....*....|....*.
gi 2184988178  94 SVGGMWGAIAALLAPER-ITGLVLMD 118
Cdd:PLN02679  163 SVGSLACVIAASESTRDlVRGLVLLN 188
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
20-117 2.99e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 38.74  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  20 PVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDLWGHGESDGFPEGTRNlddlTRHALA-LLDHL-------NIERCSIV 91
Cdd:PLN02894  106 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKS----TEETEAwFIDSFeewrkakNLSNFILL 181
                          90       100
                  ....*....|....*....|....*.
gi 2184988178  92 GLSVGGMWGAIAALLAPERITGLVLM 117
Cdd:PLN02894  182 GHSFGGYVAAKYALKHPEHVQHLILV 207
PRK08775 PRK08775
homoserine O-succinyltransferase;
32-116 3.94e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 38.23  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  32 KGMWSAQ------LDTlaSQYRVIVPDLWGhgeSDGFPEGTRNLDDLTRHALALLDHLNIERCS-IVGLSVGGMWGAIAA 104
Cdd:PRK08775   82 KGWWEGLvgsgraLDP--ARFRLLAFDFIG---ADGSLDVPIDTADQADAIALLLDALGIARLHaFVGYSYGALVGLQFA 156
                          90
                  ....*....|..
gi 2184988178 105 LLAPERITGLVL 116
Cdd:PRK08775  157 SRHPARVRTLVV 168
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
15-116 4.53e-03

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 37.86  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184988178  15 DQGTGPVVLLGHSYLWDKGMWSAQLDTLASQYRVIVPDL------WGHGESDGFPEG-------TRNLDDLTRH------ 75
Cdd:COG3458    78 GEGPLPAVVEFHGYGGGRGLPHEDLDWAAAGYAVLVMDTrgqgssWGDTPDPGGYSGgalpgymTRGIDDPDTYyyrrvy 157
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2184988178  76 --------ALALLDHLNIERCSIVGLSVGGMWGAIAALLAPeRITGLVL 116
Cdd:COG3458   158 ldavravdALRSLPEVDGKRIGVTGGSQGGGLALAAAALDP-RVKAAAA 205
 
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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