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Conserved domains on  [gi|1671264924|gb|TMG68877|]
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alpha/beta hydrolase [Chloroflexi bacterium]

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, ...
 35-291 4.22e-57

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: 182.89  E-value: 4.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  35 HAKVGGQSIFYRTAG-TGPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDA 113
Cdd:COG0596     6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 114 IGVVRAHVLGLSWGGMLAQELFRLHPARIDHLILADtyagwrgslpaDTVEQRRARCYRDAGRPRrevvaewvpadffle 193
Cdd:COG0596    86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-----------EVLAALAEPLRRPGLAPE--------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 194 aspalaaemaavvadfhplGFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGH 273
Cdd:COG0596   140 -------------------ALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGH 200

                         250
                  ....*....|....*...
gi 1671264924 274 VSNMEKREDFNAHVRRFL 291
Cdd:COG0596   201 FPPLEQPEAFAAALRDFL 218
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 35-291 4.22e-57

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: 182.89  E-value: 4.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  35 HAKVGGQSIFYRTAG-TGPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDA 113
Cdd:COG0596     6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 114 IGVVRAHVLGLSWGGMLAQELFRLHPARIDHLILADtyagwrgslpaDTVEQRRARCYRDAGRPRrevvaewvpadffle 193
Cdd:COG0596    86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-----------EVLAALAEPLRRPGLAPE--------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 194 aspalaaemaavvadfhplGFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGH 273
Cdd:COG0596   140 -------------------ALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGH 200

                         250
                  ....*....|....*...
gi 1671264924 274 VSNMEKREDFNAHVRRFL 291
Cdd:COG0596   201 FPPLEQPEAFAAALRDFL 218
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 43-291 6.95e-36

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: 129.01  E-value: 6.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  43 IFYRTAGTG---PTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDAIGVVRA 119
Cdd:TIGR02427   2 LHYRLDGAAdgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 120 HVLGLSWGGMLAQELFRLHPARIDHLILADTYA------GWRGSlpADTVEQRRARCYRDAgrprreVVAEWVPADFFlE 193
Cdd:TIGR02427  82 VFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAkigtpeSWNAR--IAAVRAEGLAALADA------VLERWFTPGFR-E 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 194 ASPALAAEMAAVVADFHPLGFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGH 273
Cdd:TIGR02427 153 AHPARLDLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGH 232

                         250
                  ....*....|....*...
gi 1671264924 274 VSNMEKREDFNAHVRRFL 291
Cdd:TIGR02427 233 IPCVEQPEAFNAALRDFL 250
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 29-291 1.97e-26

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 106.57  E-value: 1.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  29 AGGELVHAKVGGQSIFYRTAGT--GPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADT 106
Cdd:PRK14875  107 AGPAPRKARIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 107 LDEFLDAIGVVRAHVLGLSWGGMLAQELFRLHPARIDHLILADTyAGW---------RGSLPADTVEQRR---ARCYRDA 174
Cdd:PRK14875  187 VLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP-AGLgpeingdyiDGFVAAESRRELKpvlELLFADP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 175 GRPRREVVAEWVPADFFLEASPALAAemaavvadfhpLGFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAe 254
Cdd:PRK14875  266 ALVTRQMVEDLLKYKRLDGVDDALRA-----------LADALFAGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHA- 333

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1671264924 255 qfHAAIPGSELRVIPGAGHVSNMEKREDFNAHVRRFL 291
Cdd:PRK14875  334 --QGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 52-279 1.04e-25

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: 102.20  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  52 PTLLLLHGFLCDSRCWASQLAGLS-DRFTVVAWDAPGAGMSPDP--AEHFTIADWADTLDEFLDAIGVVRAHVLGLSWGG 128
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 129 MLAQELFRLHPARIDHLILADTYAGW---------RGSLPADTVEQRRARCYRDAGRPRREVVAEWVPadFFLEASPALA 199
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPheldeadrfILALFPGFFDGFVADFAPNPLGRLVAKLLALLL--LRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 200 AEMAAVVADFHPLGFRLMA---RSLADTDTTPVLK---TINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGH 273
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTgalLFIETWSTELRAKflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*.
gi 1671264924 274 VSNMEK 279
Cdd:pfam00561 239 FAFLEG 244
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 35-291 4.22e-57

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: 182.89  E-value: 4.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  35 HAKVGGQSIFYRTAG-TGPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDA 113
Cdd:COG0596     6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 114 IGVVRAHVLGLSWGGMLAQELFRLHPARIDHLILADtyagwrgslpaDTVEQRRARCYRDAGRPRrevvaewvpadffle 193
Cdd:COG0596    86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-----------EVLAALAEPLRRPGLAPE--------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 194 aspalaaemaavvadfhplGFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGH 273
Cdd:COG0596   140 -------------------ALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGH 200

                         250
                  ....*....|....*...
gi 1671264924 274 VSNMEKREDFNAHVRRFL 291
Cdd:COG0596   201 FPPLEQPEAFAAALRDFL 218
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 43-291 6.95e-36

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: 129.01  E-value: 6.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  43 IFYRTAGTG---PTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDAIGVVRA 119
Cdd:TIGR02427   2 LHYRLDGAAdgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 120 HVLGLSWGGMLAQELFRLHPARIDHLILADTYA------GWRGSlpADTVEQRRARCYRDAgrprreVVAEWVPADFFlE 193
Cdd:TIGR02427  82 VFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAkigtpeSWNAR--IAAVRAEGLAALADA------VLERWFTPGFR-E 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 194 ASPALAAEMAAVVADFHPLGFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGH 273
Cdd:TIGR02427 153 AHPARLDLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGH 232

                         250
                  ....*....|....*...
gi 1671264924 274 VSNMEKREDFNAHVRRFL 291
Cdd:TIGR02427 233 IPCVEQPEAFNAALRDFL 250
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 29-291 1.97e-26

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 106.57  E-value: 1.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  29 AGGELVHAKVGGQSIFYRTAGT--GPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADT 106
Cdd:PRK14875  107 AGPAPRKARIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 107 LDEFLDAIGVVRAHVLGLSWGGMLAQELFRLHPARIDHLILADTyAGW---------RGSLPADTVEQRR---ARCYRDA 174
Cdd:PRK14875  187 VLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP-AGLgpeingdyiDGFVAAESRRELKpvlELLFADP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 175 GRPRREVVAEWVPADFFLEASPALAAemaavvadfhpLGFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAe 254
Cdd:PRK14875  266 ALVTRQMVEDLLKYKRLDGVDDALRA-----------LADALFAGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHA- 333

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1671264924 255 qfHAAIPGSELRVIPGAGHVSNMEKREDFNAHVRRFL 291
Cdd:PRK14875  334 --QGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 52-279 1.04e-25

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: 102.20  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  52 PTLLLLHGFLCDSRCWASQLAGLS-DRFTVVAWDAPGAGMSPDP--AEHFTIADWADTLDEFLDAIGVVRAHVLGLSWGG 128
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 129 MLAQELFRLHPARIDHLILADTYAGW---------RGSLPADTVEQRRARCYRDAGRPRREVVAEWVPadFFLEASPALA 199
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPheldeadrfILALFPGFFDGFVADFAPNPLGRLVAKLLALLL--LRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 200 AEMAAVVADFHPLGFRLMA---RSLADTDTTPVLK---TINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGH 273
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTgalLFIETWSTELRAKflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*.
gi 1671264924 274 VSNMEK 279
Cdd:pfam00561 239 FAFLEG 244
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 38-292 1.07e-25

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 103.23  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  38 VGGQSIFYRTAGTGPT--LLLLHGFLCDSRCWASQLAGLSDR--FTVVAWDAPGAGMS--PD--PAEHFTIADWADTLDE 109
Cdd:TIGR01250  10 DGGYHLFTKTGGEGEKikLLLLHGGPGMSHEYLENLRELLKEegREVIMYDQLGCGYSdqPDdsDEELWTIDYFVDELEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 110 FLDAIGVVRAHVLGLSWGGMLAQELFRLHPARIDHLILADTYAG---W-------RGSLPADTVEQRRaRC--------- 170
Cdd:TIGR01250  90 VREKLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSapeYvkelnrlRKELPPEVRAAIK-RCeasgdydnp 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 171 -YRDAGRPRREV---VAEWVPadfflEASPALAAEMAAVV--ADFHPLGFRLMARsLADTDTTPVLKTINVPTLLLWGEG 244
Cdd:TIGR01250 169 eYQEAVEVFYHHllcRLRKWP-----EALKHLKSGGNTNVynIMQGPNEFTITGN-LKDWDITDKLSEIKVPTLLTVGEF 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1671264924 245 DRRSPlSVAEQFHAAIPGSELRVIPGAGHVSNMEKREDFNAHVRRFLL 292
Cdd:TIGR01250 243 DTMTP-EAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFIR 289
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
40-291 1.07e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.83  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  40 GQSIFYR----TAGTGPTLLLLHGFLCDSRCWASQLAGLSDR-FTVVAWDAPGAGMSPDPAEHF-TIADWADTLDEFLDA 113
Cdd:COG2267    13 GLRLRGRrwrpAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAALDA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 114 I---GVVRAHVLGLSWGGMLAQELFRLHPARIDHLILadtyagwrgslpadtveqrrarcyrdagrprrevvaewvpadf 190
Cdd:COG2267    93 LrarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVL------------------------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 191 fleASPALAAemaavvadfHPLgFRLMARSLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAI-PGSELRVIP 269
Cdd:COG2267   130 ---LAPAYRA---------DPL-LGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLP 196

                         250       260
                  ....*....|....*....|...
gi 1671264924 270 GAGHVSNMEK-REDFNAHVRRFL 291
Cdd:COG2267   197 GARHELLNEPaREEVLAAILAWL 219
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-291 6.56e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 69.97  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  39 GGQSIFYrtAGTGPTLLLLHGFLCDS---RCWASQLAglSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDAI- 114
Cdd:COG1647     5 GAEPFFL--EGGRKGVLLLHGFTGSPaemRPLAEALA--KAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 115 -GVVRAHVLGLSWGGMLAQELFRLHPArIDHLILADT---YAGWRGSLpadtveqrrarcyrdagRPRREVVAEWVPAdf 190
Cdd:COG1647    81 aGYDKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPalkIDDPSAPL-----------------LPLLKYLARSLRG-- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 191 flEASPALAAEMAAVVADFHPLGfrlMARSLAD--TDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGS--ELR 266
Cdd:COG1647   141 --IGSDIEDPEVAEYAYDRTPLR---ALAELQRliREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdkELV 215

                         250       260
                  ....*....|....*....|....*.
gi 1671264924 267 VIPGAGHVSNMEK-REDFNAHVRRFL 291
Cdd:COG1647   216 WLEDSGHVITLDKdREEVAEEILDFL 241
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 54-274 2.07e-13

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 67.88  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  54 LLLLHGFLCDSRCWASQLAglsDRFTVVAWDAPGAGMSPDPAEHFT-IADWADTLDEFLDAIGVVrahVLGLSWGGMLAQ 132
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLA---AGVAVLAPDLPGHGSSSPPPLDLAdLADLAALLDELGAARPVV---LVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 133 ELfrLHPARIDHLILADTYAGWRGSLPADTVEQRrarcyrdagRPRREVVAEWVPADFFLEASPALAAEMAAVVADFHPL 212
Cdd:pfam12697  75 AA--AAAALVVGVLVAPLAAPPGLLAALLALLAR---------LGAALAAPAWLAAESLARGFLDDLPADAEWAAALARL 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1671264924 213 gfrLMARSLADTDTTPVLKTINVPTLLLWGEgDRRSPlSVAEQFHAAIPGSELRVIPGAGHV 274
Cdd:pfam12697 144 ---AALLAALALLPLAAWRDLPVPVLVLAEE-DRLVP-ELAQRLLAALAGARLVVLPGAGHL 200
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
52-291 1.43e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 63.11  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  52 PTLLLLHGFLCDS----RCWASQLAglSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDeFLDAIGVV---RAHVLGL 124
Cdd:COG1506    24 PVVVYVHGGPGSRddsfLPLAQALA--SRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAID-YLAARPYVdpdRIGIYGH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 125 SWGGMLAQELFRLHPARIDHLILADTYAGWRgslpaDTVEQRRARCYRDAGRPrrevvaeWVPADFFLEASPALAAemaa 204
Cdd:COG1506   101 SYGGYMALLAAARHPDRFKAAVALAGVSDLR-----SYYGTTREYTERLMGGP-------WEDPEAYAARSPLAYA---- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 205 vvadfhplgfrlmarsladtdttpvlKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPG----SELRVIPGAGHVSNMEKR 280
Cdd:COG1506   165 --------------------------DKLKTPLLLIHGEADDRVPPEQAERLYEALKKagkpVELLVYPGEGHGFSGAGA 218

                         250
                  ....*....|.
gi 1671264924 281 EDFNAHVRRFL 291
Cdd:COG1506   219 PDYLERILDFL 229
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 53-273 3.86e-10

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: 58.77  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  53 TLLLLHGFlCDSRCWASQLAG-LSDR-FTVVAWDAPGAGMSPDPAEHFT-IADWADTLDEFLDAIgvVRAH------VLG 123
Cdd:pfam12146   6 VVVLVHGL-GEHSGRYAHLADaLAAQgFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKI--REEHpglplfLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 124 LSWGGMLAQELFRLHPARIDHLILADTYAGWRGSLPAD---TVEQRRARCYRDAgRPRREVVAEWVPADffleaspalAA 200
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPilkLLAKLLGKLFPRL-RVPNNLLPDSLSRD---------PE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 201 EMAAVVADfhPL---GFRL-MARSLADT--DTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGS--ELRVIPGAG 272
Cdd:pfam12146 153 VVAAYAAD--PLvhgGISArTLYELLDAgeRLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPGLY 230


                  .
gi 1671264924 273 H 273
Cdd:pfam12146 231 H 231
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 38-193 1.42e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 57.70  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  38 VGGQSIFYRTAGTGPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDAIGVV 117
Cdd:PRK03592   14 VLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWFDALGLD 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1671264924 118 RAHVLGLSWGGMLAQELFRLHPARIDHLILADTYAG---WrGSLPADTVEQRRArcYRDAGRPRREVVAEwvpaDFFLE 193
Cdd:PRK03592   94 DVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRpmtW-DDFPPAVRELFQA--LRSPGEGEEMVLEE----NVFIE 165
PRK05855 PRK05855
SDR family oxidoreductase;
51-127 2.32e-08

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 54.99  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  51 GPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMS--PDPAEHFTIADWADTLDEFLDAIGVVRA-HVLGLSWG 127
Cdd:PRK05855   25 RPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSsaPKRTAAYTLARLADDFAAVIDAVSPDRPvHLLAHDWG 104
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 43-274 2.97e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 53.71  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  43 IFYRTAGTGPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEH-FTIADWADTLDEFLDAIGVVRAHV 121
Cdd:PRK03204   26 IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFgYQIDEHARVIGEFVDHLGLDRYLS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 122 LGLSWGGMLAQELFRLHPARIDHLILADTyAGWrgslPADTVEQR-----------------------RARCYRDAGRPR 178
Cdd:PRK03204  106 MGQDWGGPISMAVAVERADRVRGVVLGNT-WFW----PADTLAMKafsrvmssppvqyailrrnffveRLIPAGTEHRPS 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 179 REVVAEWVPADFFLEASPALaAEMAAVVADFHPLGFRLmARSLADTDTTPvlktinvPTLLLWGEGDRR-SPLSVAEQFH 257
Cdd:PRK03204  181 SAVMAHYRAVQPNAAARRGV-AEMPKQILAARPLLARL-AREVPATLGTK-------PTLLVWGMKDVAfRPKTILPRLR 251

                         250
                  ....*....|....*..
gi 1671264924 258 AAIPGSELRVIPGAGHV 274
Cdd:PRK03204  252 ATFPDHVLVELPNAKHF 268
PLN02578 PLN02578
hydrolase
 40-291 3.24e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 54.08  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  40 GQSIFYRTAGTGPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAEHFTIADWADTLDEFLDAIGVVRA 119
Cdd:PLN02578   75 GHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 120 HVLGLSWGGMLAQELFRLHPARIDHLIL---ADTYAGWRGSLPADTVEQRRArCYRDAGRPRREVVAEWV---------- 186
Cdd:PLN02578  155 VLVGNSLGGFTALSTAVGYPELVAGVALlnsAGQFGSESREKEEAIVVEETV-LTRFVVKPLKEWFQRVVlgflfwqakq 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 187 PA-----------------DFFLEA--SPALAAEMAAVVadfhplgFRLMARSLADTDT---TPVLKTINVPTLLLWGEG 244
Cdd:PLN02578  234 PSriesvlksvykdksnvdDYLVESitEPAADPNAGEVY-------YRLMSRFLFNQSRytlDSLLSKLSCPLLLLWGDL 306

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1671264924 245 DRRSPLSVAEQFHAAIPGSELrVIPGAGHVSNMEKREDFNAHVRRFL 291
Cdd:PLN02578  307 DPWVGPAKAEKIKAFYPDTTL-VNLQAGHCPHDEVPEQVNKALLEWL 352
PRK08775 PRK08775
homoserine O-succinyltransferase;
67-273 3.38e-08

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 54.03  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  67 WASQLAGLS-----DRFTVVAWDAPGAGMSPDPAehFTIADWADTLDEFLDAIGVVRAH-VLGLSWGGMLAQELFRLHPA 140
Cdd:PRK08775   84 WWEGLVGSGraldpARFRLLAFDFIGADGSLDVP--IDTADQADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 141 RIDHLIL------ADTYA-GWRGsLPADTVEQRRARCYRDAG------------------RPRREVVAEWVPADFFLEAS 195
Cdd:PRK08775  162 RVRTLVVvsgahrAHPYAaAWRA-LQRRAVALGQLQCAEKHGlalarqlamlsyrtpeefEERFDAPPEVINGRVRVAAE 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 196 PALAAEMAAVVADFHPLGFRLMARSLADTDTTPvlKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPG-SELRVIPGA-GH 273
Cdd:PRK08775  241 DYLDAAGAQYVARTPVNAYLRLSESIDLHRVDP--EAIRVPTVVVAVEGDRLVPLADLVELAEGLGPrGSLRVLRSPyGH 318
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 40-290 5.17e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 53.20  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  40 GQSIFYRTAGT-GPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMS--PDPAEH-----FTIADWADTLDEFL 111
Cdd:PLN02824   17 GYNIRYQRAGTsGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSdkPNPRSAppnsfYTFETWGEQLNDFC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 112 DAIGVVRAHVLGLSWGGML-------AQELFR-----------LH----PARIDHLI------LADTYAG---WRGSLPA 160
Cdd:PLN02824   97 SDVVGDPAFVICNSVGGVVglqaavdAPELVRgvmlinislrgLHikkqPWLGRPFIkafqnlLRETAVGkafFKSVATP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 161 DTVEQRRARCYRDAGRPRREVVaewvpadfflEA--SPALAAEMAAVVADF-----HPLGFRLMARsladtdttpvlktI 233
Cdd:PLN02824  177 ETVKNILCQCYHDDSAVTDELV----------EAilRPGLEPGAVDVFLDFisysgGPLPEELLPA-------------V 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1671264924 234 NVPTLLLWGEGDRRSPLSVAEQFHAAIPGSELRVIPGAGHVSNMEKREDFNAHVRRF 290
Cdd:PLN02824  234 KCPVLIAWGEKDPWEPVELGRAYANFDAVEDFIVLPGVGHCPQDEAPELVNPLIESF 290
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 50-291 2.15e-06

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 47.91  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  50 TGPTLLLLHGFLCDSRCWASQLAGLSDrFTVVAWDAPGAGMSPD-PAEHFtiADWADTLDEFLDAIGVVRAHVLGLSWGG 128
Cdd:PRK11126    1 GLPWLVFLHGLLGSGQDWQPVGEALPD-YPRLYIDLPGHGGSAAiSVDGF--ADVSRLLSQTLQSYNILPYWLVGYSLGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 129 MLA-QELFRLHPARIDHLILADTYAGwrgsLPadTVEQRRARCYRD---AGRPRRE----VVAEW----VPADFFLEASP 196
Cdd:PRK11126   78 RIAmYYACQGLAGGLCGLIVEGGNPG----LQ--NAEERQARWQNDrqwAQRFRQEpleqVLADWyqqpVFASLNAEQRQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 197 ALAAEMA----AVVADFhplgfrLMARSLA-DTDTTPVLKTINVPTLLLWGEGDRRSpLSVAEQFhaaipGSELRVIPGA 271
Cdd:PRK11126  152 QLVAKRSnnngAAVAAM------LEATSLAkQPDLRPALQALTFPFYYLCGERDSKF-QALAQQL-----ALPLHVIPNA 219

                         250       260
                  ....*....|....*....|
gi 1671264924 272 GHVSNMEKREDFNAHVRRFL 291
Cdd:PRK11126  220 GHNAHRENPAAFAASLAQIL 239
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 48-291 2.89e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 47.60  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  48 AGTGPTLLLLHGFLC---DSRCWASQLAGLsdRFTVVAWDAPGAGMSP-DPAEhftiADWADTLDeFLDAIGVVRAH--- 120
Cdd:COG1073    34 SKKYPAVVVAHGNGGvkeQRALYAQRLAEL--GFNVLAFDYRGYGESEgEPRE----EGSPERRD-ARAAVDYLRTLpgv 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 121 ------VLGLSWGGMLAqelfrLHPARIDhliladtyagwrgslpadtveqRRARCyrdagrprrevVAEWVPADFFLEA 194
Cdd:COG1073   107 dperigLLGISLGGGYA-----LNAAATD----------------------PRVKA-----------VILDSPFTSLEDL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 195 SPALAAEMAAVVADFHPLGFRLMARSLADT--DTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGS-ELRVIPGA 271
Cdd:COG1073   149 AAQRAKEARGAYLPGVPYLPNVRLASLLNDefDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPkELLIVPGA 228

                         250       260
                  ....*....|....*....|.
gi 1671264924 272 GHVSNMEKRED-FNAHVRRFL 291
Cdd:COG1073   229 GHVDLYDRPEEeYFDKLAEFF 249
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
42-273 3.67e-06

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 47.32  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  42 SIFYRTAGTGPT-LLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAehftiadwADTLDEFLDAI---GVV 117
Cdd:PRK10349    3 NIWWQTKGQGNVhLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFG--------ALSLADMAEAVlqqAPD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 118 RAHVLGLSWGGMLAQELFRLHPARIDHLILADTYA------GWRGSLPaDTVEQRRARCYRDAGRPRREVVA------EW 185
Cdd:PRK10349   75 KAIWLGWSLGGLVASQIALTHPERVQALVTVASSPcfsardEWPGIKP-DVLAGFQQQLSDDFQRTVERFLAlqtmgtET 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 186 VPADFFLEASPALAAEMAAVvaDFHPLGFRLmarsLADTDTTPVLKTINVPTLLLWGEGDRRSPLSVAEQFHAAIPGSEL 265
Cdd:PRK10349  154 ARQDARALKKTVLALPMPEV--DVLNGGLEI----LKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSES 227


                  ....*...
gi 1671264924 266 RVIPGAGH 273
Cdd:PRK10349  228 YIFAKAAH 235
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 17-147 4.41e-05

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 44.49  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  17 PPSGASHRNRTPAGGelvhAKVGGQS--------IFYRTAGT--GPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAP 86
Cdd:PLN03084   87 SVQGSGNKAKDPIFG----LKMGAQSqassdlfrWFCVESGSnnNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWL 162

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1671264924  87 GAGMS--PDPAEHF--TIADWADTLDEFLDAIGVVRAHVLGLSWGGMLAQELFRLHPARIDHLIL 147
Cdd:PLN03084  163 GFGFSdkPQPGYGFnyTLDEYVSSLESLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLIL 227
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 52-147 1.72e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 42.59  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  52 PTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDP---------AEHFTIadwaDTLDEFLDAIGVVRAHVL 122
Cdd:PLN02894  106 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPdftcksteeTEAWFI----DSFEEWRKAKNLSNFILL 181

                          90       100
                  ....*....|....*....|....*
gi 1671264924 123 GLSWGGMLAQELFRLHPARIDHLIL 147
Cdd:PLN02894  182 GHSFGGYVAAKYALKHPEHVQHLIL 206
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 51-114 2.74e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 42.13  E-value: 2.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1671264924  51 GPTLLLLHGFLCDSRCWASQLAGLSDRFTVVAWDAPGAGMSPDPAE-HFTIADWADTLDEFLDAI 114
Cdd:PLN02679   88 GPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGfSYTMETWAELILDFLEEV 152
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
197-285 8.77e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 8.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 197 ALAAEMAAVVAdFHPLGFRLMARSLADTDTTPVlktinvptLLLWGEGDRRSPLSVAEQFHAAIPGS----ELRVIPGAG 272
Cdd:COG0412   128 ARGPDLAAAVS-FYGGLPADDLLDLAARIKAPV--------LLLYGEKDPLVPPEQVAALEAALAAAgvdvELHVYPGAG 198

                          90
                  ....*....|...
gi 1671264924 273 HVSNMEKREDFNA 285
Cdd:COG0412   199 HGFTNPGRPRYDP 211
PRK10673 PRK10673
esterase;
74-149 9.09e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 40.10  E-value: 9.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1671264924  74 LSDRFTVVAWDAPGAGMSPDpAEHFTIADWADTLDEFLDAIGVVRAHVLGLSWGGMLAQELFRLHPARIDHLILAD 149
Cdd:PRK10673   39 LVNDHDIIQVDMRNHGLSPR-DPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
metX PRK00175
homoserine O-acetyltransferase; Provisional
 90-146 3.49e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 38.63  E-value: 3.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1671264924  90 MSPDPAEH---------FTIADWADTLDEFLDAIGVVRAH-VLGLSWGGMLAQELFRLHPARIDHLI 146
Cdd:PRK00175  110 SSINPDTGkpygsdfpvITIRDWVRAQARLLDALGITRLAaVVGGSMGGMQALEWAIDYPDRVRSAL 176
PRK06765 PRK06765
homoserine O-acetyltransferase; Provisional
 98-146 6.13e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 235859 [Multi-domain]  Cd Length: 389  Bit Score: 37.76  E-value: 6.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1671264924  98 FTIADWADTLDEFLDAIGVVRAH-VLGLSWGGMLAQELFRLHPARIDHLI 146
Cdd:PRK06765  141 VTILDFVRVQKELIKSLGIARLHaVMGPSMGGMQAQEWAVHYPHMVERMI 190
YpfH COG0400
Predicted esterase [General function prediction only];
47-213 9.09e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 36.42  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924  47 TAGTGPTLLLLHGfLCDSrcwASQLAGL-----SDRFTVVA--------------WDAPGAGMSPDPAEH-FTIADWADT 106
Cdd:COG0400     1 GGPAAPLVVLLHG-YGGD---EEDLLPLapelaLPGAAVLAprapvpegpggrawFDLSFLEGREDEEGLaAAAEALAAF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671264924 107 LDEFLDAIGVVRAHV--LGLSWGGMLAQELFRLHPARIDHLILadtyagWRGSLPADTVEQRRArcyRDAGRPRREVVA- 183
Cdd:COG0400    77 IDELEARYGIDPERIvlAGFSQGAAMALSLALRRPELLAGVVA------LSGYLPGEEALPAPE---AALAGTPVFLAHg 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1671264924 184 ---EWVPADFFLEASPALAAEMAAVVADFHPLG 213
Cdd:COG0400   148 tqdPVIPVERAREAAEALEAAGADVTYREYPGG 180
 
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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