|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
6-264 |
9.89e-43 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 145.14 E-value: 9.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 6 HVHIVGRAGAArsLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAafeqHRYLTMDGYARDLNMLLDELAL 85
Cdd:COG0596 15 HYREAGPDGPP--VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP----AGGYTLDDLADDLAALLDALGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 86 KDVVLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSEADLNALYRAVTigrdawaeqfapvamgnrd 165
Cdd:COG0596 89 ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALA------------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 166 rpelaehfaraiksvpadailtvlcsifQCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGSTLRVIDAEGHL 245
Cdd:COG0596 150 ----------------------------RTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHF 201
|
250
....*....|....*....
gi 2190503809 246 PHMSAPERVIEALQDFVRA 264
Cdd:COG0596 202 PPLEQPEAFAAALRDFLAR 220
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
19-251 |
3.99e-24 |
|
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: 97.19 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDTIWPAFA-DEFRIVLYDHVGAGRSDPAAfEQHRYlTMDGYARDLNMLLDELALKDVVLVGHSMGA 97
Cdd:pfam00561 3 VLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPK-AQDDY-RTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 98 TASMLAAIARPEQFARLACIGASA-----RYLDEPGYHGGFSEADLNALYRAVTIGRDAWAEQFAPVAMGNRDRPELAEH 172
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDpphelDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 173 FARAIKSVPADAILTVLCSIF------QCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGSTLRVIDAEGHLP 246
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLfietwsTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....*
gi 2190503809 247 HMSAP 251
Cdd:pfam00561 241 FLEGP 245
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
5-263 |
1.97e-21 |
|
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: 90.11 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 5 HHVHiVGRAGAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSD----PAAFEQHryltmdgyARDLNMLL 80
Cdd:TIGR02427 3 HYRL-DGAADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDapegPYSIEDL--------ADDVLALL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 81 DELALKDVVLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSEADLNALYRAV--TIGR---DAWAEQ 155
Cdd:TIGR02427 74 DHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAKIGTPESWNARIAAVRAEGLAALAdaVLERwftPGFREA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 156 fapvamgnrdRPELAEHFARAIKSVPADAILTVLCSIFQCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGST 235
Cdd:TIGR02427 154 ----------HPARLDLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGAR 223
|
250 260
....*....|....*....|....*...
gi 2190503809 236 LRVIDAEGHLPHMSAPERVIEALQDFVR 263
Cdd:TIGR02427 224 FAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
14-265 |
7.08e-18 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 81.91 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 14 GAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAAFEQhrylTMDGYARDLNMLLDELALKDVVLVGH 93
Cdd:PRK14875 129 GDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAG----SLDELAAAVLAFLDALGIERAHLVGH 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 94 SMGATASMLAAIARPEQFARLACIgASARYLDE--PGYHGGFSEAD-LNALyravtigRDAWAEQFAPVAMGNRDRPELA 170
Cdd:PRK14875 205 SMGGAVALRLAARAPQRVASLTLI-APAGLGPEinGDYIDGFVAAEsRREL-------KPVLELLFADPALVTRQMVEDL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 171 EHFARaIKSVPaDAILTVLCSIF-----QCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHrtiAGSTLRVIDAEGHL 245
Cdd:PRK14875 277 LKYKR-LDGVD-DALRALADALFaggrqRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVHVLPGAGHM 351
|
250 260
....*....|....*....|
gi 2190503809 246 PHMSAPERVIEALQDFVRAP 265
Cdd:PRK14875 352 PQMEAAADVNRLLAEFLGKA 371
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
5-109 |
7.52e-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: 40.29 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 5 HHVHIVGRAGAARSLVFaHGFGTDQRAWD--TIWPAFADEFRIVLYDH-------VGAGRSDPAAFEQH---------RY 66
Cdd:cd12809 74 YEVYIVDQPGRGRSPWN-PEVGGPLAASTaeTVEQRFTAPERYNLWPQaklhtqwPGTGRRGDPIFDQFyasqvplltNL 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2190503809 67 LTMDGYARD-LNMLLDELalKDVVLVGHSMGATASMLAAIARPE 109
Cdd:cd12809 153 AEQEALVRAaGCALLDII--GPAILITHSQGGPFGWLAADARPD 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
6-264 |
9.89e-43 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 145.14 E-value: 9.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 6 HVHIVGRAGAArsLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAafeqHRYLTMDGYARDLNMLLDELAL 85
Cdd:COG0596 15 HYREAGPDGPP--VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP----AGGYTLDDLADDLAALLDALGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 86 KDVVLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSEADLNALYRAVTigrdawaeqfapvamgnrd 165
Cdd:COG0596 89 ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALA------------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 166 rpelaehfaraiksvpadailtvlcsifQCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGSTLRVIDAEGHL 245
Cdd:COG0596 150 ----------------------------RTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHF 201
|
250
....*....|....*....
gi 2190503809 246 PHMSAPERVIEALQDFVRA 264
Cdd:COG0596 202 PPLEQPEAFAAALRDFLAR 220
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
19-251 |
3.99e-24 |
|
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: 97.19 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDTIWPAFA-DEFRIVLYDHVGAGRSDPAAfEQHRYlTMDGYARDLNMLLDELALKDVVLVGHSMGA 97
Cdd:pfam00561 3 VLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPK-AQDDY-RTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 98 TASMLAAIARPEQFARLACIGASA-----RYLDEPGYHGGFSEADLNALYRAVTIGRDAWAEQFAPVAMGNRDRPELAEH 172
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDpphelDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 173 FARAIKSVPADAILTVLCSIF------QCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGSTLRVIDAEGHLP 246
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLfietwsTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....*
gi 2190503809 247 HMSAP 251
Cdd:pfam00561 241 FLEGP 245
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
5-263 |
1.97e-21 |
|
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: 90.11 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 5 HHVHiVGRAGAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSD----PAAFEQHryltmdgyARDLNMLL 80
Cdd:TIGR02427 3 HYRL-DGAADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDapegPYSIEDL--------ADDVLALL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 81 DELALKDVVLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSEADLNALYRAV--TIGR---DAWAEQ 155
Cdd:TIGR02427 74 DHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAKIGTPESWNARIAAVRAEGLAALAdaVLERwftPGFREA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 156 fapvamgnrdRPELAEHFARAIKSVPADAILTVLCSIFQCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGST 235
Cdd:TIGR02427 154 ----------HPARLDLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGAR 223
|
250 260
....*....|....*....|....*...
gi 2190503809 236 LRVIDAEGHLPHMSAPERVIEALQDFVR 263
Cdd:TIGR02427 224 FAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
14-265 |
7.08e-18 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 81.91 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 14 GAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAAFEQhrylTMDGYARDLNMLLDELALKDVVLVGH 93
Cdd:PRK14875 129 GDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAG----SLDELAAAVLAFLDALGIERAHLVGH 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 94 SMGATASMLAAIARPEQFARLACIgASARYLDE--PGYHGGFSEAD-LNALyravtigRDAWAEQFAPVAMGNRDRPELA 170
Cdd:PRK14875 205 SMGGAVALRLAARAPQRVASLTLI-APAGLGPEinGDYIDGFVAAEsRREL-------KPVLELLFADPALVTRQMVEDL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 171 EHFARaIKSVPaDAILTVLCSIF-----QCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHrtiAGSTLRVIDAEGHL 245
Cdd:PRK14875 277 LKYKR-LDGVD-DALRALADALFaggrqRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVHVLPGAGHM 351
|
250 260
....*....|....*....|
gi 2190503809 246 PHMSAPERVIEALQDFVRAP 265
Cdd:PRK14875 352 PQMEAAADVNRLLAEFLGKA 371
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
5-264 |
3.27e-14 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 69.65 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 5 HHVHIVGRAGAARSLVFAHGFGTDQRAWDTIWPAFADE-FRIVLYDHVGAGRSDPaafEQHRYLTMDGYARDLNMLLDEL 83
Cdd:COG2267 17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDG---PRGHVDSFDDYVDDLRAALDAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 84 AL---KDVVLVGHSMGATASMLAAIARPEQFARLACIgaSARYLDEPGYHGGFseadlnALYRAVTIGRDawaeqfapva 160
Cdd:COG2267 94 RArpgLPVVLLGHSMGGLIALLYAARYPDRVAGLVLL--APAYRADPLLGPSA------RWLRALRLAEA---------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 161 mgnrdrpelaehfaraiksvpadailtvlcsifqcdyrqtLQRLQRPTLLLQTRADAAVPLEAAE-FLHRTIAGSTLRVI 239
Cdd:COG2267 156 ----------------------------------------LARIDVPVLVLHGGADRVVPPEAARrLAARLSPDVELVLL 195
|
250 260
....*....|....*....|....*.
gi 2190503809 240 DAEGHLPHMSAP-ERVIEALQDFVRA 264
Cdd:COG2267 196 PGARHELLNEPArEEVLAAILAWLER 221
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
13-263 |
3.31e-13 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 67.27 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 13 AGAARSLVFAHGFGTDQRAWDTIWPAFADE-FRIVLYDHVGAGRSdPAAFEQhryLTMDGYARDLNMLLDELAL--KDVV 89
Cdd:COG1647 12 EGGRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTS-PEDLLK---TTWEDWLEDVEEAYEILKAgyDKVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 90 LVGHSMGATASMLAAIARPEqFARLACIGASARYLDEpgyhggfseadlnalyRAVTIGrdaWAEQFAPVAMGNRDRPEL 169
Cdd:COG1647 88 VIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDP----------------SAPLLP---LLKYLARSLRGIGSDIED 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 170 AEHFARAIKSVPADAILTVLcsIFQCDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGS--TLRVIDAEGHLPH 247
Cdd:COG1647 148 PEVAEYAYDRTPLRALAELQ--RLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdkELVWLEDSGHVIT 225
|
250
....*....|....*..
gi 2190503809 248 MS-APERVIEALQDFVR 263
Cdd:COG1647 226 LDkDREEVAEEILDFLE 242
|
|
| PLN02578 |
PLN02578 |
hydrolase |
5-262 |
5.23e-12 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 64.86 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 5 HHVHIVgRAGAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAAFEQHRYLTMDGYARdlnmLLDELA 84
Cdd:PLN02578 76 HKIHYV-VQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVAD----FVKEVV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 85 LKDVVLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSEADLNAL-----------YRAVTIGRDAW- 152
Cdd:PLN02578 151 KEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIVVEETVLtrfvvkplkewFQRVVLGFLFWq 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 153 AEQFAPV--AMGN--RDRPELAEHFARAIKSVPADA----ILTVLCSIF---QCDY--RQTLQRLQRPTLLLQTRADAAV 219
Cdd:PLN02578 231 AKQPSRIesVLKSvyKDKSNVDDYLVESITEPAADPnageVYYRLMSRFlfnQSRYtlDSLLSKLSCPLLLLWGDLDPWV 310
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2190503809 220 PLEAAEFLHRTIAGSTLRVIDAeGHLPHMSAPERVIEALQDFV 262
Cdd:PLN02578 311 GPAKAEKIKAFYPDTTLVNLQA-GHCPHDEVPEQVNKALLEWL 352
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
19-248 |
5.71e-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: 57.99 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDTIWPAFADE-FRIVLYDHVGAGRSDPAAFEQHRYltmDGYARDLNMLLDELAL----KDVVLVGH 93
Cdd:pfam12146 7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDGKRGHVPSF---DDYVDDLDTFVDKIREehpgLPLFLLGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 94 SMGATASMLAAIARPEQFARLACIGASARYldepgyhggfseadlnALYRAVTIGRdAWAEQFAPVA----MGNRDRPEL 169
Cdd:pfam12146 84 SMGGLIAALYALRYPDKVDGLILSAPALKI----------------KPYLAPPILK-LLAKLLGKLFprlrVPNNLLPDS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 170 AEHFARAIKSVPADAILTVLCSI-FQCDYRQTLQRLQR-------PTLLLQTRADAAVPLEAAEFLHRTIAGS--TLRVI 239
Cdd:pfam12146 147 LSRDPEVVAAYAADPLVHGGISArTLYELLDAGERLLRraaaitvPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLY 226
|
....*....
gi 2190503809 240 DAEGHLPHM 248
Cdd:pfam12146 227 PGLYHELLN 235
|
|
| PRK05855 |
PRK05855 |
SDR family oxidoreductase; |
19-264 |
1.78e-09 |
|
SDR family oxidoreductase;
Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 57.68 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSD-PAAFEQHRyltMDGYARDLNMLLDELAL-KDVVLVGHSMG 96
Cdd:PRK05855 28 VVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSaPKRTAAYT---LARLADDFAAVIDAVSPdRPVHLLAHDWG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 97 ATAsMLAAIARPEQFARLAC---------------------------IGASARYLDEPGYHGGFSEADLNALYRAVTIGR 149
Cdd:PRK05855 105 SIQ-GWEAVTRPRAAGRIASftsvsgpsldhvgfwlrsglrrptprrLARALGQLLRSWYIYLFHLPVLPELLWRLGLGR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 150 DAWAEqfapvamgnRDRPELAEHFARAIKSVPADAILTVlcSIFQCDYRQTLQRLQR-----PTLLLQTRADAAVPLEAA 224
Cdd:PRK05855 184 AWPRL---------LRRVEGTPVDPIPTQTTLSDGAHGV--KLYRANMIRSLSRPRErytdvPVQLIVPTGDPYVRPALY 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2190503809 225 EFLHRTIAGSTLRVIDAeGHLPHMSAPERVIEALQDFVRA 264
Cdd:PRK05855 253 DDLSRWVPRLWRREIKA-GHWLPMSHPQVLAAAVAEFVDA 291
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
12-262 |
1.03e-08 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 54.74 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 12 RAGAA-RSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSD---PAAFEQHRYLTMDGYARDLNMLLDELALKD 87
Cdd:PLN02824 24 RAGTSgPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDkpnPRSAPPNSFYTFETWGEQLNDFCSDVVGDP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 88 VVLVGHSMGATASMLAAIARPEQFARLACIGASARYL---DEPGYHGGFSEAdLNALYRAVTIGRDAWAEQFAPVAMGN- 163
Cdd:PLN02824 104 AFVICNSVGGVVGLQAAVDAPELVRGVMLINISLRGLhikKQPWLGRPFIKA-FQNLLRETAVGKAFFKSVATPETVKNi 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 164 ---------RDRPELAEHFAR-AIKSVPADAILTVLCsifqcdY------RQTLQRLQRPTLLLQTRADAAVPLEAAEFL 227
Cdd:PLN02824 183 lcqcyhddsAVTDELVEAILRpGLEPGAVDVFLDFIS------YsggplpEELLPAVKCPVLIAWGEKDPWEPVELGRAY 256
|
250 260 270
....*....|....*....|....*....|....*
gi 2190503809 228 HRTIAGSTLRVIDAEGHLPHMSAPERVIEALQDFV 262
Cdd:PLN02824 257 ANFDAVEDFIVLPGVGHCPQDEAPELVNPLIESFV 291
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
19-257 |
1.52e-08 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 53.63 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDtiwPAFADEFRIVLYDHVGAGRSDPAAFeqhrylTMDGYARDLNMLLDELALKDVVLVGHSMGAT 98
Cdd:pfam12697 1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPPPL------DLADLADLAALLDELGAARPVVLVGHSLGGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 99 ASMLAAIARPEQFARLACIGASARYLD-EPGYHGGFSEADLNALYRAVTIGRDAWAEQFAPVAMGNRDRPELAEHFARAI 177
Cdd:pfam12697 72 VALAAAAAALVVGVLVAPLAAPPGLLAaLLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 178 KSVPADailtvlcsifqcdyrqtLQRLQRPTLLLQTRaDAAVPLEAAEFLhRTIAGSTLRVIDAEGHLPHmSAPERVIEA 257
Cdd:pfam12697 152 LLPLAA-----------------WRDLPVPVLVLAEE-DRLVPELAQRLL-AALAGARLVVLPGAGHLPL-DDPEEVAEA 211
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
19-263 |
2.44e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 53.10 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQ-RAWDTIWPAFADE-FRIVLYDHVGAGRSDPAAFEQhryltmdgYARDLNMLLDELALKD------VVL 90
Cdd:COG1506 26 VVYVHGGPGSRdDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGD--------EVDDVLAAIDYLAARPyvdpdrIGI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 91 VGHSMGATASMLAAIARPEQFARLACIGASaryldepgyhggfseADLNALYRAVTIGRDAWAEQFapvamgnRDRPELA 170
Cdd:COG1506 98 YGHSYGGYMALLAAARHPDRFKAAVALAGV---------------SDLRSYYGTTREYTERLMGGP-------WEDPEAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 171 EHFAraiksvPADAIltvlcsifqcdyrqtlQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAG----STLRVIDAEGHLP 246
Cdd:COG1506 156 AARS------PLAYA----------------DKLKTPLLLIHGEADDRVPPEQAERLYEALKKagkpVELLVYPGEGHGF 213
|
250
....*....|....*..
gi 2190503809 247 HMSAPERVIEALQDFVR 263
Cdd:COG1506 214 SGAGAPDYLERILDFLD 230
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
19-258 |
1.01e-07 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 51.56 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSdpAAFEQhryLTMDgyarDLNMLLDELALKDVVLVGHSMGAT 98
Cdd:PRK10349 16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS--RGFGA---LSLA----DMAEAVLQQAPDKAIWLGWSLGGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 99 ASMLAAIARPEQFARLACIGASARYLDEPGYHG-------GFSEADLNALYRAVtigrdawaEQF-APVAMGNrdrpELA 170
Cdd:PRK10349 87 VASQIALTHPERVQALVTVASSPCFSARDEWPGikpdvlaGFQQQLSDDFQRTV--------ERFlALQTMGT----ETA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 171 EHFARAIKSV------PADAILTVLCSIFQ-CDYRQTLQRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGSTLRVIDAEG 243
Cdd:PRK10349 155 RQDARALKKTvlalpmPEVDVLNGGLEILKtVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAA 234
|
250
....*....|....*
gi 2190503809 244 HLPHMSAPERVIEAL 258
Cdd:PRK10349 235 HAPFISHPAEFCHLL 249
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
13-263 |
1.39e-07 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 51.53 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 13 AGAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAA----FEQHryltmdgyARDLNMLLDELALKDV 88
Cdd:PRK03592 24 TGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDidytFADH--------ARYLDAWFDALGLDDV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 89 VLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSEA---------------DLNALYRAV-------T 146
Cdd:PRK03592 96 VLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVRELfqalrspgegeemvlEENVFIERVlpgsilrP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 147 IGRDAWAEQFAPVAMGNRDRPELAehFARA--IKSVPADailtvLCSIFQcDYRQTLQRLQRPTLLLqtRADAAVPL--- 221
Cdd:PRK03592 176 LSDEEMAVYRRPFPTPESRRPTLS--WPRElpIDGEPAD-----VVALVE-EYAQWLATSDVPKLLI--NAEPGAILttg 245
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2190503809 222 EAAEFLHRTIAGSTLRVIDAEGHLPHMSAPERVIEALQDFVR 263
Cdd:PRK03592 246 AIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLR 287
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
19-118 |
1.32e-06 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 48.68 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSD-PAAFEqhryLTMDGYARDLNMLLDELALKDVVLVGHSMGA 97
Cdd:PLN02679 91 VLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDkPPGFS----YTMETWAELILDFLEEVVQKPTVLIGNSVGS 166
|
90 100
....*....|....*....|....*
gi 2190503809 98 TASMLAAIARPEQFAR----LACIG 118
Cdd:PLN02679 167 LACVIAASESTRDLVRglvlLNCAG 191
|
|
| PRK03204 |
PRK03204 |
haloalkane dehalogenase; Provisional |
14-182 |
2.14e-06 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179554 [Multi-domain] Cd Length: 286 Bit Score: 47.93 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 14 GAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSD-PAAFEqhryLTMDGYARDLNMLLDELALKDVVLVG 92
Cdd:PRK03204 32 GTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSErPSGFG----YQIDEHARVIGEFVDHLGLDRYLSMG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 93 HSMGATASMLAAIARPEQfARLACIGASARYLDEPGYHGGFSEADLNALYRAVTIGRDAWAEQFAPVAMGNRDRPELAEH 172
Cdd:PRK03204 108 QDWGGPISMAVAVERADR-VRGVVLGNTWFWPADTLAMKAFSRVMSSPPVQYAILRRNFFVERLIPAGTEHRPSSAVMAH 186
|
170
....*....|
gi 2190503809 173 FaRAIKSVPA 182
Cdd:PRK03204 187 Y-RAVQPNAA 195
|
|
| Abhydrolase_4 |
pfam08386 |
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ... |
207-244 |
5.21e-05 |
|
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.
Pssm-ID: 429964 [Multi-domain] Cd Length: 98 Bit Score: 41.17 E-value: 5.21e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2190503809 207 PTLLLQTRADAAVPLEAAEFLHRTIAGSTLRVIDAEGH 244
Cdd:pfam08386 35 PVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGH 72
|
|
| PRK10673 |
PRK10673 |
esterase; |
73-117 |
5.53e-05 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 43.57 E-value: 5.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2190503809 73 ARDLNMLLDELALKDVVLVGHSMGATASM-LAAIArPEQFARLACI 117
Cdd:PRK10673 68 AQDLLDTLDALQIEKATFIGHSMGGKAVMaLTALA-PDRIDKLVAI 112
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
13-119 |
3.73e-04 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 39.04 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 13 AGAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAafEQHRYLtmdgyARDLNMLLDELALKDVVLVG 92
Cdd:COG1075 2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIE--DSAEQL-----AAFVDAVLAATGAEKVDLVG 74
|
90 100
....*....|....*....|....*....
gi 2190503809 93 HSMGATAS--MLAAIARPEQFARLACIGA 119
Cdd:COG1075 75 HSMGGLVAryYLKRLGGAAKVARVVTLGT 103
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
5-109 |
7.52e-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: 40.29 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 5 HHVHIVGRAGAARSLVFaHGFGTDQRAWD--TIWPAFADEFRIVLYDH-------VGAGRSDPAAFEQH---------RY 66
Cdd:cd12809 74 YEVYIVDQPGRGRSPWN-PEVGGPLAASTaeTVEQRFTAPERYNLWPQaklhtqwPGTGRRGDPIFDQFyasqvplltNL 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2190503809 67 LTMDGYARD-LNMLLDELalKDVVLVGHSMGATASMLAAIARPE 109
Cdd:cd12809 153 AEQEALVRAaGCALLDII--GPAILITHSQGGPFGWLAADARPD 194
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
18-114 |
1.16e-03 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 39.86 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 18 SLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAAFEQHRYLTMDGYARDLNMLLDELALKDVVLVGHSMGA 97
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQGYFS 208
|
90
....*....|....*..
gi 2190503809 98 TASMLAAIARPEQFARL 114
Cdd:PLN03084 209 PPVVKYASAHPDKIKKL 225
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
19-135 |
3.21e-03 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 38.30 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 19 LVFAHGFGTDQRAWDTIWPAF-----------ADEFRIVLYDHVGAGRSDPaafeqhRYLTMDGYARdlnMLLDEL---- 83
Cdd:COG2382 115 LYLLDGGGGDEQDWFDQGRLPtildnliaagkIPPMIVVMPDGGDGGDRGT------EGPGNDAFER---FLAEELipfv 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 84 -----ALKD---VVLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSE 135
Cdd:COG2382 186 eknyrVSADpehRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDADRGGWAE 245
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
7-265 |
4.08e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 38.68 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 7 VHIVGRAGAARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDpaaFEQHRY-------LTMDGYARDLNML 79
Cdd:PLN02980 1362 VHEVGQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSK---IQNHAKetqteptLSVELVADLLYKL 1438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 80 LDELALKDVVLVGHSMGATASMLAAIARPEQFARLACIGASARYLDEPGYHGGFSEADLNALYrAVTIGRDAWAEQFAPV 159
Cdd:PLN02980 1439 IEHITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIISGSPGLKDEVARKIRSAKDDSRARM-LIDHGLEIFLENWYSG 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 160 AMGN--RDRPELAEHFARAI--KSVPADA-ILTVLCSIFQCDYRQTLQRLQRPTLLLQTRADAAVPlEAAEFLHRTIAGS 234
Cdd:PLN02980 1518 ELWKslRNHPHFNKIVASRLlhKDVPSLAkLLSDLSIGRQPSLWEDLKQCDTPLLLVVGEKDVKFK-QIAQKMYREIGKS 1596
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2190503809 235 T------------LRVIDAEGHLPHMSAPERVIEALQDFVRAP 265
Cdd:PLN02980 1597 KesgndkgkeiieIVEIPNCGHAVHLENPLPVIRALRKFLTRL 1639
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
76-146 |
4.57e-03 |
|
Lipase. 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: 238382 [Multi-domain] Cd Length: 153 Bit Score: 36.71 E-value: 4.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2190503809 76 LNMLLDELALKDVVLVGHSMGATASMLAA--IARPEQFARLACIG-ASARYLDEPGYHGGFSEADLNALYRAVT 146
Cdd:cd00741 18 LKSALAQYPDYKIHVTGHSLGGALAGLAGldLRGRGLGRLVRVYTfGPPRVGNAAFAEDRLDPSDALFVDRIVN 91
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
11-264 |
5.40e-03 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 37.20 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 11 GRAGAARSLVFAHGFGTDQRAWDTIWPAFADE-FRIVLYDHVGAGRSDpaafEQHRYLTmDGYARDLNMLLDELALKD-- 87
Cdd:COG1073 32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESE----GEPREEG-SPERRDARAAVDYLRTLPgv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 88 ----VVLVGHSMG-ATASMLAAIARpeqfaRLACIGASAryldepgyhgGFSEADLNALYRAvtigRDAWAEQFAPVAMG 162
Cdd:COG1073 107 dperIGLLGISLGgGYALNAAATDP-----RVKAVILDS----------PFTSLEDLAAQRA----KEARGAYLPGVPYL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 163 NRDRPE-LAEHFARAIKSVPadailtvlcsifqcdyrqtlqRLQRPTLLLQTRADAAVPLEAAEFLHRTIAGS-TLRVID 240
Cdd:COG1073 168 PNVRLAsLLNDEFDPLAKIE---------------------KISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPkELLIVP 226
|
250 260
....*....|....*....|....*
gi 2190503809 241 AEGH-LPHMSAPERVIEALQDFVRA 264
Cdd:COG1073 227 GAGHvDLYDRPEEEYFDKLAEFFKK 251
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
16-118 |
7.16e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 37.58 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 16 ARSLVFAHGFGTDQRAWDTIWPAFADEFRIVLYDHVGAGRSDPAAFE-QHRYLTMDGYARDLNMLLDELALKDVVLVGHS 94
Cdd:PLN02894 105 APTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHS 184
|
90 100
....*....|....*....|....
gi 2190503809 95 MGATASMLAAIARPEQFARLACIG 118
Cdd:PLN02894 185 FGGYVAAKYALKHPEHVQHLILVG 208
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
26-116 |
9.01e-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: 36.67 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190503809 26 GTDqraWDTIWPAFA--------DEFRIVLYD--HVGAGRSDPAAFEQHRYLTMDGYARD-LNMLLDEL----------A 84
Cdd:pfam00756 32 GTG---WFQNGPAKEgldrlaasGEIPPVIIVgsPRGGEVSFYSDWDRGLNATEGPGAYAyETFLTQELpplldanfptA 108
|
90 100 110
....*....|....*....|....*....|..
gi 2190503809 85 LKDVVLVGHSMGATASMLAAIARPEQFARLAC 116
Cdd:pfam00756 109 PDGRALAGQSMGGLGALYLALKYPDLFGSVSS 140
|
|
| |
