|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
53-298 |
5.67e-54 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 176.46 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 53 VVFLHGLFGSKTNFNSIAKILaqQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAM 132
Cdd:PRK10673 19 IVLVHGLFGSLDNLGVLARDL--VNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 133 LLALQRPELVERLIAVDISPVESTgVSHFATYVAAMRAINIADELPRSRARKLADEQlssvIQDMAVRQHLLTNLVEVDg 212
Cdd:PRK10673 97 ALTALAPDRIDKLVAIDIAPVDYH-VRRHDEIFAAINAVSEAGATTRQQAAAIMRQH----LNEEGVIQFLLKSFVDGE- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 213 rfvWRVNLDALTQHLDKILAFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQDFIA 292
Cdd:PRK10673 171 ---WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246
|
....*.
gi 1887096796 293 AIRGFL 298
Cdd:PRK10673 247 AIRRYL 252
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
51-298 |
4.36e-40 |
|
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: 139.37 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 51 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 129
Cdd:COG0596 24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 130 TAMLLALQRPELVERLIAVDispvestgvSHFATYVAAMRAINIADELPRSRARKLADEQLSSVIQDMAVrqhlltnlve 209
Cdd:COG0596 102 VALELAARHPERVAGLVLVD---------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITV---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 210 vdgrfvwrvnldaltqhldkilafpqrqesylgPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQD 289
Cdd:COG0596 163 ---------------------------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEA 209
|
....*....
gi 1887096796 290 FIAAIRGFL 298
Cdd:COG0596 210 FAAALRDFL 218
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
51-287 |
1.54e-28 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 109.90 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 51 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP---DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMG 127
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSSRPKaqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 128 GKTAMLLALQRPELVERLIAVD-ISPVESTG--VSHFATYVAAMRAINIADELPRSRARKLADEQLSSViqdmaVRQHLL 204
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLLGaLDPPHELDeaDRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL-----LRLRLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 205 TNLVEVDGRFvWRVNLDA----LTQHLDKILAFPQRQE-----SYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTV 275
Cdd:pfam00561 155 KALPLLNKRF-PSGDYALakslVTGALLFIETWSTELRakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233
|
250
....*....|..
gi 1887096796 276 PNAGHWIHADRP 287
Cdd:pfam00561 234 PDAGHFAFLEGP 245
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
43-298 |
1.91e-14 |
|
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: 71.62 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 43 LLDGEAA-LPAVVFLHGLfgsKTNFNSIAKILAQQTGR-RVLTVDARNHGDSPhSPDMSYEI--MSQDLQDLLPQLGLVP 118
Cdd:TIGR02427 5 RLDGAADgAPVLVFINSL---GTDLRMWDPVLPALTPDfRVLRYDKRGHGLSD-APEGPYSIedLADDVLALLDHLGIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 119 CVVVGHSMGGKTAMLLALQRPELVERLIAVDISPVESTgVSHFATYVAAMRA---INIADE-LPR--SRARKLADEQLSS 192
Cdd:TIGR02427 81 AVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAKIGT-PESWNARIAAVRAeglAALADAvLERwfTPGFREAHPARLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 193 VIQDMAVRQhlltnlvEVDGrfvWRVNLDALTQhldkiLAFPQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQM 272
Cdd:TIGR02427 160 LYRNMLVRQ-------PPDG---YAGCCAAIRD-----ADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARF 224
|
250 260
....*....|....*....|....*.
gi 1887096796 273 QTVPNAGHWIHADRPQDFIAAIRGFL 298
Cdd:TIGR02427 225 AEIRGAGHIPCVEQPEAFNAALRDFL 250
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
107-148 |
2.11e-05 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 45.31 E-value: 2.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1887096796 107 LQDLLPQLGlvPCVVVGHSMGGKTAMLLALQRPELVERLIAV 148
Cdd:cd12808 180 YDALLDRVG--PCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
53-298 |
5.67e-54 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 176.46 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 53 VVFLHGLFGSKTNFNSIAKILaqQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAM 132
Cdd:PRK10673 19 IVLVHGLFGSLDNLGVLARDL--VNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 133 LLALQRPELVERLIAVDISPVESTgVSHFATYVAAMRAINIADELPRSRARKLADEQlssvIQDMAVRQHLLTNLVEVDg 212
Cdd:PRK10673 97 ALTALAPDRIDKLVAIDIAPVDYH-VRRHDEIFAAINAVSEAGATTRQQAAAIMRQH----LNEEGVIQFLLKSFVDGE- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 213 rfvWRVNLDALTQHLDKILAFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQDFIA 292
Cdd:PRK10673 171 ---WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246
|
....*.
gi 1887096796 293 AIRGFL 298
Cdd:PRK10673 247 AIRRYL 252
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
51-298 |
4.36e-40 |
|
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: 139.37 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 51 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 129
Cdd:COG0596 24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 130 TAMLLALQRPELVERLIAVDispvestgvSHFATYVAAMRAINIADELPRSRARKLADEQLSSVIQDMAVrqhlltnlve 209
Cdd:COG0596 102 VALELAARHPERVAGLVLVD---------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITV---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 210 vdgrfvwrvnldaltqhldkilafpqrqesylgPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQD 289
Cdd:COG0596 163 ---------------------------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEA 209
|
....*....
gi 1887096796 290 FIAAIRGFL 298
Cdd:COG0596 210 FAAALRDFL 218
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
51-287 |
1.54e-28 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 109.90 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 51 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP---DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMG 127
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSSRPKaqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 128 GKTAMLLALQRPELVERLIAVD-ISPVESTG--VSHFATYVAAMRAINIADELPRSRARKLADEQLSSViqdmaVRQHLL 204
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLLGaLDPPHELDeaDRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL-----LRLRLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 205 TNLVEVDGRFvWRVNLDA----LTQHLDKILAFPQRQE-----SYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTV 275
Cdd:pfam00561 155 KALPLLNKRF-PSGDYALakslVTGALLFIETWSTELRakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233
|
250
....*....|..
gi 1887096796 276 PNAGHWIHADRP 287
Cdd:pfam00561 234 PDAGHFAFLEGP 245
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
42-298 |
2.31e-18 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 81.59 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 42 RLLDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDM--SYEIMSQDLQ---DLLPQLGL 116
Cdd:COG2267 20 RWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLRaalDALRARPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 117 VPCVVVGHSMGGKTAMLLALQRPELVERLIAvdISPvestgvshfatyvaamraINIADELPRSRARKLADEQLSSVIQD 196
Cdd:COG2267 99 LPVVLLGHSMGGLIALLYAARYPDRVAGLVL--LAP------------------AYRADPLLGPSARWLRALRLAEALAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 197 MAVrqhlltnlvevdgrfvwrvnldaltqhldkilafpqrqesylgPTLFLLGGNSQFVHPSHHPEIM-RLFPRAQMQTV 275
Cdd:COG2267 159 IDV-------------------------------------------PVLVLHGGADRVVPPEAARRLAaRLSPDVELVLL 195
|
250 260
....*....|....*....|....
gi 1887096796 276 PNAGHWIHADRPQD-FIAAIRGFL 298
Cdd:COG2267 196 PGARHELLNEPAREeVLAAILAWL 219
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
43-298 |
1.91e-14 |
|
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: 71.62 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 43 LLDGEAA-LPAVVFLHGLfgsKTNFNSIAKILAQQTGR-RVLTVDARNHGDSPhSPDMSYEI--MSQDLQDLLPQLGLVP 118
Cdd:TIGR02427 5 RLDGAADgAPVLVFINSL---GTDLRMWDPVLPALTPDfRVLRYDKRGHGLSD-APEGPYSIedLADDVLALLDHLGIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 119 CVVVGHSMGGKTAMLLALQRPELVERLIAVDISPVESTgVSHFATYVAAMRA---INIADE-LPR--SRARKLADEQLSS 192
Cdd:TIGR02427 81 AVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAKIGT-PESWNARIAAVRAeglAALADAvLERwfTPGFREAHPARLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 193 VIQDMAVRQhlltnlvEVDGrfvWRVNLDALTQhldkiLAFPQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQM 272
Cdd:TIGR02427 160 LYRNMLVRQ-------PPDG---YAGCCAAIRD-----ADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARF 224
|
250 260
....*....|....*....|....*.
gi 1887096796 273 QTVPNAGHWIHADRPQDFIAAIRGFL 298
Cdd:TIGR02427 225 AEIRGAGHIPCVEQPEAFNAALRDFL 250
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
39-298 |
6.87e-14 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 69.97 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 39 AEPRLLDGeaALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHS-PDMSYEIMSQDLQDLLPQL--G 115
Cdd:COG1647 6 AEPFFLEG--GRKGVLLLHGFTGSPAEMRPLAEALAKA-GYTVYAPRLPGHGTSPEDlLKTTWEDWLEDVEEAYEILkaG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 116 LVPCVVVGHSMGGKTAMLLALQRPElVERLIAvdISPV-----ESTGVSHFATYVAA-MRAINIADELPRSRARKLADEQ 189
Cdd:COG1647 83 YDKVIVIGLSMGGLLALLLAARYPD-VAGLVL--LSPAlkiddPSAPLLPLLKYLARsLRGIGSDIEDPEVAEYAYDRTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 190 LSSVIQdmavrqhlLTNLVEvdgrfVWRVNLDALTQhldkilafpqrqesylgPTLFLLGGNSQFVHPSHHPEIMRLF-- 267
Cdd:COG1647 160 LRALAE--------LQRLIR-----EVRRDLPKITA-----------------PTLIIQSRKDEVVPPESARYIYERLgs 209
|
250 260 270
....*....|....*....|....*....|..
gi 1887096796 268 PRAQMQTVPNAGHWIHADRPQDFIA-AIRGFL 298
Cdd:COG1647 210 PDKELVWLEDSGHVITLDKDREEVAeEILDFL 241
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
53-293 |
3.81e-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: 67.11 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 53 VVFLHGLFGSKTNFNSiakilAQQTGRRVLTVDARNHGDSPHSPDMSYEImsQDLQDLLPQLGLV-PCVVVGHSMGGKTA 131
Cdd:pfam12697 1 VVLVHGAGLSAAPLAA-----LLAAGVAVLAPDLPGHGSSSPPPLDLADL--ADLAALLDELGAArPVVLVGHSLGGAVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 132 MLLALqrpelVERLIAVDISPVeSTGVSHFATYVAAMRAINIADELPRSRARKLADEQLSSviqdmavrqhlltnlvEVD 211
Cdd:pfam12697 74 LAAAA-----AALVVGVLVAPL-AAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLD----------------DLP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 212 GRFVWRVNLDALTQHLDKILAFPQRQESYLGPTLFLLGGNSQFVHPsHHPEIMRLFPRAQMQTVPNAGHWIHaDRPQDFI 291
Cdd:pfam12697 132 ADAEWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPE-LAQRLLAALAGARLVVLPGAGHLPL-DDPEEVA 209
|
..
gi 1887096796 292 AA 293
Cdd:pfam12697 210 EA 211
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
45-298 |
4.02e-13 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 67.35 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 45 DGEAALPAVVFLHGLFGSKTN-FNSIAKILAQQtGRRVLTVDARNHGDSPHSPdmsYEIMSQDLQ---DLLPQLGLVP-- 118
Cdd:COG1506 18 ADGKKYPVVVYVHGGPGSRDDsFLPLAQALASR-GYAVLAPDYRGYGESAGDW---GGDEVDDVLaaiDYLAARPYVDpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 119 -CVVVGHSMGGKTAMLLALQRPELVERLIAVDispvestGVSHFATYVAAMRAIN-IADELPRSRARKLADeqlSSVIqd 196
Cdd:COG1506 94 rIGIYGHSYGGYMALLAAARHPDRFKAAVALA-------GVSDLRSYYGTTREYTeRLMGGPWEDPEAYAA---RSPL-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 197 mavrqhlltnlvevdgrfvwrvnldaltQHLDKIlafpqrqesyLGPTLFLLGGNSQFVHPSHhpeIMRLF-------PR 269
Cdd:COG1506 162 ----------------------------AYADKL----------KTPLLLIHGEADDRVPPEQ---AERLYealkkagKP 200
|
250 260
....*....|....*....|....*....
gi 1887096796 270 AQMQTVPNAGHWIHADRPQDFIAAIRGFL 298
Cdd:COG1506 201 VELLVYPGEGHGFSGAGAPDYLERILDFL 229
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
46-298 |
1.25e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 67.28 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 46 GEAALPAVVFLHGLFGSKTN--FNsiakILAQQTGRRVLTVDARNHGDS-PHSPDMSYEIMSQDLQDLLPQLGLVPCVVV 122
Cdd:PRK14875 127 GEGDGTPVVLIHGFGGDLNNwlFN----HAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 123 GHSMGGKTAMLLALQRPELVERLiavdiSPVESTGVShfatyvaamRAINIA--DELPRSRARKladeQLSSVIQDMAVR 200
Cdd:PRK14875 203 GHSMGGAVALRLAARAPQRVASL-----TLIAPAGLG---------PEINGDyiDGFVAAESRR----ELKPVLELLFAD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 201 QHLLTN-LVEVDGRFvwrVNLDALTQHLDKILA--FPQ-RQESYLG--------PTLFLLGGNSQFVhPSHHPEimRLFP 268
Cdd:PRK14875 265 PALVTRqMVEDLLKY---KRLDGVDDALRALADalFAGgRQRVDLRdrlaslaiPVLVIWGEQDRII-PAAHAQ--GLPD 338
|
250 260 270
....*....|....*....|....*....|
gi 1887096796 269 RAQMQTVPNAGHWIHADRPQDFIAAIRGFL 298
Cdd:PRK14875 339 GVAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
52-286 |
4.53e-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: 64.54 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 52 AVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSP----HSPdmSYEIMSQDLQDLLPQL----GLVPCVVVG 123
Cdd:pfam12146 6 VVVLVHGLGEHSGRYAHLADALAAQ-GFAVYAYDHRGHGRSDgkrgHVP--SFDDYVDDLDTFVDKIreehPGLPLFLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 124 HSMGGKTAMLLALQRPELVERLI----AVDISPVESTGVSHFATYVAAMRAiniadelPRSRARKLADeqLSSVIQDMAV 199
Cdd:pfam12146 83 HSMGGLIAALYALRYPDKVDGLIlsapALKIKPYLAPPILKLLAKLLGKLF-------PRLRVPNNLL--PDSLSRDPEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 200 RQhLLTNLVEVDGRFVWRVNLDALtQHLDKILafpQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRA--QMQTVPN 277
Cdd:pfam12146 154 VA-AYAADPLVHGGISARTLYELL-DAGERLL---RRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPG 228
|
....*....
gi 1887096796 278 AGHWIHADR 286
Cdd:pfam12146 229 LYHELLNEP 237
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
45-298 |
4.13e-11 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 61.85 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 45 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP--DMSYEImsQDLQDLLPQLGLVPCV-- 120
Cdd:COG1073 32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAEL-GFNVLAFDYRGYGESEGEPreEGSPER--RDARAAVDYLRTLPGVdp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 121 ----VVGHSMGGKTAMLLALQRPelveRLIAVdispVESTGVSHFATyVAAMRAINIADE-------LPRSRARKLADEQ 189
Cdd:COG1073 109 erigLLGISLGGGYALNAAATDP----RVKAV----ILDSPFTSLED-LAAQRAKEARGAylpgvpyLPNVRLASLLNDE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 190 LSSViqdmavrqhlltnlvevdgrfvwrvnldaltQHLDKIlafpqrqesyLGPTLFLLGGNSQFvHPSHHPEimRLFPR 269
Cdd:COG1073 180 FDPL-------------------------------AKIEKI----------SRPLLFIHGEKDEA-VPFYMSE--DLYEA 215
|
250 260 270
....*....|....*....|....*....|....
gi 1887096796 270 A----QMQTVPNAGHWIHADRPQD-FIAAIRGFL 298
Cdd:COG1073 216 AaepkELLIVPGAGHVDLYDRPEEeYFDKLAEFF 249
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
51-137 |
1.21e-10 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 60.24 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 51 PAVVFLHGLFGSKTNFNSIAKILAQqtgRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKT 130
Cdd:PRK11126 3 PWLVFLHGLLGSGQDWQPVGEALPD---YPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRI 79
|
....*..
gi 1887096796 131 AMLLALQ 137
Cdd:PRK11126 80 AMYYACQ 86
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
53-148 |
8.98e-09 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 52.14 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 53 VVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVdarNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTA- 131
Cdd:COG1075 8 VVLVHGLGGSAASWAPLAPRLRAA-GYPVYAL---NYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGLVAr 83
|
90
....*....|....*...
gi 1887096796 132 -MLLALQRPELVERLIAV 148
Cdd:COG1075 84 yYLKRLGGAAKVARVVTL 101
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
45-141 |
1.12e-08 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 54.59 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 45 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDMSYEIMSQ--------DLQ---DLLPQ 113
Cdd:COG0412 24 AGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA-GYVVLAPDLYGRGGPGDDPDEARALMGAldpellaaDLRaalDWLKA 102
|
90 100 110
....*....|....*....|....*....|.
gi 1887096796 114 LGLV---PCVVVGHSMGGKTAMLLALQRPEL 141
Cdd:COG0412 103 QPEVdagRVGVVGFCFGGGLALLAAARGPDL 133
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
45-153 |
9.43e-07 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 48.72 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 45 DGEAALPAVVFLHG---LFGSKTNFNSIAKILAQQTGRRVLTVDARnhgdspHSPDMSYEIMSQDLQDLL-------PQL 114
Cdd:COG0657 8 GAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAARAGAAVVSVDYR------LAPEHPFPAALEDAYAALrwlranaAEL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1887096796 115 GLVP--CVVVGHSMGGKTAMLLALQRPELVERLIA--VDISPV 153
Cdd:COG0657 82 GIDPdrIAVAGDSAGGHLAAALALRARDRGGPRPAaqVLIYPV 124
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
53-153 |
1.23e-06 |
|
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.
Pssm-ID: 369540 Cd Length: 233 Bit Score: 48.51 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 53 VVFLHGLFGSKTNFNSIAKILAQQtgRRVLTVDARNHGDSP---HSPDMSYEIMSQDLQDLLPQLGLV------------ 117
Cdd:pfam07819 7 VLFIPGNAGSYKQVRSIASVAANL--YQVLRKLLQNDNGFHldfFSVDFNEELSAFHGRTLLDQAEYLndairyilslya 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1887096796 118 -------PCVVVGHSMGGKTA---MLLALQRPELVERLIAVDiSPV 153
Cdd:pfam07819 85 sgrpgptSVILIGHSMGGIVAraaLTLPNYIPQSVNTIITLS-SPH 129
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
53-298 |
1.91e-06 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 49.47 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 53 VVFLHGLFGSKTNFNSIAKILAQQTgrRVLTVDARNHGDSP---------HSPDMSYEIMSQDLQDLLPQLGLVPCVVVG 123
Cdd:PLN02980 1374 VLFLHGFLGTGEDWIPIMKAISGSA--RCISIDLPGHGGSKiqnhaketqTEPTLSVELVADLLYKLIEHITPGKVTLVG 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 124 HSMGGKTAMLLALQRPELVERLIAVDISPVESTGVShfatyvaamRAINIADElpRSRARKLADEQLSSVIQDM------ 197
Cdd:PLN02980 1452 YSMGARIALYMALRFSDKIEGAVIISGSPGLKDEVA---------RKIRSAKD--DSRARMLIDHGLEIFLENWysgelw 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 198 -AVRQH---------------------LLTNLVEVDGRFVWRvNLDALTQHLdkILAFPQRQESY--LGPTLFLLGGNSQ 253
Cdd:PLN02980 1521 kSLRNHphfnkivasrllhkdvpslakLLSDLSIGRQPSLWE-DLKQCDTPL--LLVVGEKDVKFkqIAQKMYREIGKSK 1597
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1887096796 254 FVHPSHHPEIMrlfpraQMQTVPNAGHWIHADRPQDFIAAIRGFL 298
Cdd:PLN02980 1598 ESGNDKGKEII------EIVEIPNCGHAVHLENPLPVIRALRKFL 1636
|
|
| COG4757 |
COG4757 |
Predicted alpha/beta hydrolase [General function prediction only]; |
42-148 |
1.06e-05 |
|
Predicted alpha/beta hydrolase [General function prediction only];
Pssm-ID: 443790 [Multi-domain] Cd Length: 289 Bit Score: 46.03 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 42 RLLDGEAALPAVVFLHGLFGSKTNF-NSIAKILAQQtGRRVLTVDARNHGDS-PHSP---DMSY-EIMSQD-------LQ 108
Cdd:COG4757 23 RLFPPAGPPRAVVLINPATGVPQRFyRPFARYLAER-GFAVLTYDYRGIGLSrPGSLrgfDAGYrDWGELDlpavldaLR 101
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1887096796 109 DLLPQLglvPCVVVGHSMGGKtaMLLALQRPELVERLIAV 148
Cdd:COG4757 102 ARFPGL---PLLLVGHSLGGQ--LLGLAPNAERVDRLVTV 136
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
107-148 |
2.11e-05 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 45.31 E-value: 2.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1887096796 107 LQDLLPQLGlvPCVVVGHSMGGKTAMLLALQRPELVERLIAV 148
Cdd:cd12808 180 YDALLDRVG--PCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
|
|
| PRK10566 |
PRK10566 |
esterase; Provisional |
49-141 |
1.31e-04 |
|
esterase; Provisional
Pssm-ID: 182555 [Multi-domain] Cd Length: 249 Bit Score: 42.67 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 49 ALPAVVFLHGLFGSKTNFNSIAKILAqQTGRRVLTVDARNH-----GDSPHSPDMSYEIMSQDLQDL------LPQLGLV 117
Cdd:PRK10566 26 PLPTVFFYHGFTSSKLVYSYFAVALA-QAGFRVIMPDAPMHgarfsGDEARRLNHFWQILLQNMQEFptlraaIREEGWL 104
|
90 100
....*....|....*....|....*..
gi 1887096796 118 P---CVVVGHSMGGKTAMLLALQRPEL 141
Cdd:PRK10566 105 LddrLAVGGASMGGMTALGIMARHPWV 131
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
100-148 |
1.51e-04 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214008 Cd Length: 280 Bit Score: 42.60 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1887096796 100 YEIMSQD-LQDLLPQLGlvPCVVVGHSMGGKTAMLLALQRPELVERLIAV 148
Cdd:cd12809 155 QEALVRAaGCALLDIIG--PAILITHSQGGPFGWLAADARPDLVKAIVAI 202
|
|
| Chlorophyllase |
pfam07224 |
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ... |
51-164 |
1.11e-03 |
|
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.
Pssm-ID: 254111 Cd Length: 307 Bit Score: 39.82 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 51 PAVVFLHGLFGSKTN----FNSIAK----ILAQQTGRRVLTVDARNHGDSPHSpdmSYEIMSQDLQDLLP---QLGLVPC 119
Cdd:pfam07224 47 PVVLFLHGTMLSNEFyslfFNHIAShgfiVVAPQLYRLFPPPSQQDEIDSAAE---VANWLPLGLQVVLPtgvEANLSKL 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1887096796 120 VVVGHSMGGKTAMLLALQ-RPEL-VERLIAVDisPVESTGVS-----HFATY 164
Cdd:pfam07224 124 ALSGHSRGGKTAFALALGySLDVtFSALIGVD--PVAGTSKDdrtdpHVLTY 173
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
40-148 |
1.18e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 40.28 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 40 EPRL-----LDGEAALPAVVFLHGLFGSK----TNFNSIAKILaqqtgrRVLTVDARNHGDSPHsPDMSYEIMSQ----- 105
Cdd:PLN02894 90 EPRFintvtFDSKEDAPTLVMVHGYGASQgfffRNFDALASRF------RVIAIDQLGWGGSSR-PDFTCKSTEEteawf 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1887096796 106 --DLQDLLPQLGLVPCVVVGHSMGGKTAMLLALQRPELVERLIAV 148
Cdd:PLN02894 163 idSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILV 207
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
46-147 |
2.44e-03 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 38.35 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 46 GEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVdarnHGDSPHSPDM--------------------SYEIMSQ 105
Cdd:COG0400 1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALP-GAAVLAP----RAPVPEGPGGrawfdlsflegredeeglaaAAEALAA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1887096796 106 DLQDLLPQLGLVPC--VVVGHSMGGKTAMLLALQRPELVERLIA 147
Cdd:COG0400 76 FIDELEARYGIDPEriVLAGFSQGAAMALSLALRRPELLAGVVA 119
|
|
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
100-179 |
2.46e-03 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 37.63 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096796 100 YEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLAL----QRPELVERLIAVDI-SPveSTGVSHFATYVAAM------ 168
Cdd:pfam01764 46 REQVLAELKRLLEKYPDYSIVVTGHSLGGALASLAALdlveNGLRLSSRVTVVTFgQP--RVGNLEFAKLHDSQgpkfsy 123
|
90
....*....|.
gi 1887096796 169 RAINIADELPR 179
Cdd:pfam01764 124 RVVHQRDIVPR 134
|
|
| Esterase_713 |
cd12807 |
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ... |
105-148 |
3.74e-03 |
|
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.
Pssm-ID: 214006 Cd Length: 315 Bit Score: 38.46 E-value: 3.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1887096796 105 QDLQDLLPQLGlvPCVVVGHSMGGKTAMLLALQRPELVERLIAV 148
Cdd:cd12807 179 NALAALADKLG--GAVLLGHSQSGPFPLEAALLRPAGVKGIVSV 220
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
117-147 |
4.53e-03 |
|
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 37.83 E-value: 4.53e-03
10 20 30
....*....|....*....|....*....|.
gi 1887096796 117 VPCVVVGHSMGGKTAMLLALQRPELVERLIA 147
Cdd:pfam00756 110 DGRALAGQSMGGLGALYLALKYPDLFGSVSS 140
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
100-150 |
9.37e-03 |
|
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238287 [Multi-domain] Cd Length: 229 Bit Score: 36.69 E-value: 9.37e-03
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....*....|....*....|....*....|....*....|....*....|.
gi 1887096796 100 YEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLALqrpELVERLIAVDI 150
Cdd:cd00519 111 YNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLAL---DLRLRGPGSDV 158
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