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Conserved domains on  [gi|501231543|ref|WP_012274561|]
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MULTISPECIES: poly(3-hydroxyalkanoate) depolymerase [Pseudomonas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA_depoly_arom super family cl30397
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
4-279 0e+00

poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans, Pseudomonas putida BM01, and related species. This enzyme is part of polyester storage and mobilization system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on carbon sources such as benzoic acid or phenylacetic acid. [Energy metabolism, Other]


The actual alignment was detected with superfamily member TIGR02240:

Pssm-ID: 131294  Cd Length: 276  Bit Score: 552.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543    4 PYIFRTVELDDQSIRTAVRPGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKL 83
Cdd:TIGR02240   1 PFIFRTIDLDGQSIRTAVRPGKEGLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   84 TARMLDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAAGAVMVPGKPKVLWMMASPRRYVQPSHVIRIAPMI 163
Cdd:TIGR02240  81 AARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGAVMVPGKPKVLMMMASPRRYIQPSHGIHIAPDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  164 YGGGFRRDPDLAMHHAAKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHI 243
Cdd:TIGR02240 161 YGGAFRRDPELAMAHASKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPIIPLINMRLLAWRIPNAELHI 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 501231543  244 IDDGHLFLITRAEAVAPIIMKFLQQERQRAVMHPRP 279
Cdd:TIGR02240 241 IDDGHLFLITRAEAVAPIIMKFLAEERQRAVMHPRP 276
 
Name Accession Description Interval E-value
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
4-279 0e+00

poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans, Pseudomonas putida BM01, and related species. This enzyme is part of polyester storage and mobilization system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on carbon sources such as benzoic acid or phenylacetic acid. [Energy metabolism, Other]


Pssm-ID: 131294  Cd Length: 276  Bit Score: 552.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543    4 PYIFRTVELDDQSIRTAVRPGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKL 83
Cdd:TIGR02240   1 PFIFRTIDLDGQSIRTAVRPGKEGLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   84 TARMLDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAAGAVMVPGKPKVLWMMASPRRYVQPSHVIRIAPMI 163
Cdd:TIGR02240  81 AARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGAVMVPGKPKVLMMMASPRRYIQPSHGIHIAPDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  164 YGGGFRRDPDLAMHHAAKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHI 243
Cdd:TIGR02240 161 YGGAFRRDPELAMAHASKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPIIPLINMRLLAWRIPNAELHI 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 501231543  244 IDDGHLFLITRAEAVAPIIMKFLQQERQRAVMHPRP 279
Cdd:TIGR02240 241 IDDGHLFLITRAEAVAPIIMKFLAEERQRAVMHPRP 276
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
8-268 4.13e-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: 138.98  E-value: 4.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   8 RTVELDDqsIRTAVRPGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKLTARM 87
Cdd:COG0596    5 RFVTVDG--VRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  88 LDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAAgavmvpgkpkvlwmmaspRRYVQPSHVIRIAPmiyggg 167
Cdd:COG0596   83 LDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL------------------AALAEPLRRPGLAP------ 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543 168 frrdpdlamhhaakvrsggkLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHIIDD- 246
Cdd:COG0596  139 --------------------EALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGa 198
                        250       260
                 ....*....|....*....|..
gi 501231543 247 GHLFLITRAEAVAPIIMKFLQQ 268
Cdd:COG0596  199 GHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
29-255 1.73e-38

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: 135.32  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   29 TPLLIFNGIGANLELVFPFIEALDPD-LEVIAFDVPGVGGSSTPR--HPYRFPGLAKLTARMLDYLDYGQVNVIGVSWGG 105
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  106 ALAQQFAHDYPERCKKLVLAAT-----AAGAVMVPGKPKVLWMMASPRRYVQPSHVIRIAPMIYGGGFRRD------PDL 174
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAldpphELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLrllkalPLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  175 AMHHAAKVRSGGKLGYYWQLFAGLGWT---SIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHIIDD-GHLF 250
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLFIETWStelRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDaGHFA 240

                  ....*
gi 501231543  251 LITRA 255
Cdd:pfam00561 241 FLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
2-268 5.81e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 68.05  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   2 PQPyifRTVELDDQSIRTAVRpGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLA 81
Cdd:PRK14875 109 PAP---RKARIGGRTVRYLRL-GEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  82 KLTARMLDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAA-GAVM----VPGkpkvlwMMASPRR------- 149
Cdd:PRK14875 185 AAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGlGPEIngdyIDG------FVAAESRrelkpvl 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543 150 ---YVQPSHVIRiaPMIYG-GGFRRDPDL--AMHHAAKvrsggklgyywQLFAGLGWTS--IHWLHKIQQPTLVLAGDDD 221
Cdd:PRK14875 259 ellFADPALVTR--QMVEDlLKYKRLDGVddALRALAD-----------ALFAGGRQRVdlRDRLASLAIPVLVIWGEQD 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 501231543 222 PLIPLINMRLLAwriPNAQLHIIDD-GHLFLITRAEAVAPIIMKFLQQ 268
Cdd:PRK14875 326 RIIPAAHAQGLP---DGVAVHVLPGaGHMPQMEAAADVNRLLAEFLGK 370
 
Name Accession Description Interval E-value
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
4-279 0e+00

poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans, Pseudomonas putida BM01, and related species. This enzyme is part of polyester storage and mobilization system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on carbon sources such as benzoic acid or phenylacetic acid. [Energy metabolism, Other]


Pssm-ID: 131294  Cd Length: 276  Bit Score: 552.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543    4 PYIFRTVELDDQSIRTAVRPGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKL 83
Cdd:TIGR02240   1 PFIFRTIDLDGQSIRTAVRPGKEGLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   84 TARMLDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAAGAVMVPGKPKVLWMMASPRRYVQPSHVIRIAPMI 163
Cdd:TIGR02240  81 AARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGAVMVPGKPKVLMMMASPRRYIQPSHGIHIAPDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  164 YGGGFRRDPDLAMHHAAKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHI 243
Cdd:TIGR02240 161 YGGAFRRDPELAMAHASKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPIIPLINMRLLAWRIPNAELHI 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 501231543  244 IDDGHLFLITRAEAVAPIIMKFLQQERQRAVMHPRP 279
Cdd:TIGR02240 241 IDDGHLFLITRAEAVAPIIMKFLAEERQRAVMHPRP 276
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
8-268 4.13e-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: 138.98  E-value: 4.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   8 RTVELDDqsIRTAVRPGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKLTARM 87
Cdd:COG0596    5 RFVTVDG--VRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  88 LDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAAgavmvpgkpkvlwmmaspRRYVQPSHVIRIAPmiyggg 167
Cdd:COG0596   83 LDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL------------------AALAEPLRRPGLAP------ 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543 168 frrdpdlamhhaakvrsggkLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHIIDD- 246
Cdd:COG0596  139 --------------------EALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGa 198
                        250       260
                 ....*....|....*....|..
gi 501231543 247 GHLFLITRAEAVAPIIMKFLQQ 268
Cdd:COG0596  199 GHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
29-255 1.73e-38

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: 135.32  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   29 TPLLIFNGIGANLELVFPFIEALDPD-LEVIAFDVPGVGGSSTPR--HPYRFPGLAKLTARMLDYLDYGQVNVIGVSWGG 105
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  106 ALAQQFAHDYPERCKKLVLAAT-----AAGAVMVPGKPKVLWMMASPRRYVQPSHVIRIAPMIYGGGFRRD------PDL 174
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAldpphELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLrllkalPLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  175 AMHHAAKVRSGGKLGYYWQLFAGLGWT---SIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHIIDD-GHLF 250
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLFIETWStelRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDaGHFA 240

                  ....*
gi 501231543  251 LITRA 255
Cdd:pfam00561 241 FLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
13-268 2.19e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 73.11  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  13 DDQSIRTAV-RPGKPHLTPLLIFNGIGANLELVFPFIEAL-DPDLEVIAFDVPGVGGSSTPR-HPYRFPGLAKLTARMLD 89
Cdd:COG2267   12 DGLRLRGRRwRPAGSPRGTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPRgHVDSFDDYVDDLRAALD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  90 YL---DYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAagavmvpgkpkvlwmmasprryvqpshviriapmiygg 166
Cdd:COG2267   92 ALrarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA-------------------------------------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543 167 gFRRDPDLamhhaakvrsGGKLGYYWQLFAglgwtsIHWLHKIQQPTLVLAGDDDPLIPLINMR-LLAWRIPNAQLHIID 245
Cdd:COG2267  134 -YRADPLL----------GPSARWLRALRL------AEALARIDVPVLVLHGGADRVVPPEAARrLAARLSPDVELVLLP 196
                        250       260
                 ....*....|....*....|....*
gi 501231543 246 DG-HLFLITRA-EAVAPIIMKFLQQ 268
Cdd:COG2267  197 GArHELLNEPArEEVLAAILAWLER 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
2-268 5.81e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 68.05  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   2 PQPyifRTVELDDQSIRTAVRpGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLA 81
Cdd:PRK14875 109 PAP---RKARIGGRTVRYLRL-GEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  82 KLTARMLDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAA-GAVM----VPGkpkvlwMMASPRR------- 149
Cdd:PRK14875 185 AAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGlGPEIngdyIDG------FVAAESRrelkpvl 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543 150 ---YVQPSHVIRiaPMIYG-GGFRRDPDL--AMHHAAKvrsggklgyywQLFAGLGWTS--IHWLHKIQQPTLVLAGDDD 221
Cdd:PRK14875 259 ellFADPALVTR--QMVEDlLKYKRLDGVddALRALAD-----------ALFAGGRQRVdlRDRLASLAIPVLVIWGEQD 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 501231543 222 PLIPLINMRLLAwriPNAQLHIIDD-GHLFLITRAEAVAPIIMKFLQQ 268
Cdd:PRK14875 326 RIIPAAHAQGLP---DGVAVHVLPGaGHMPQMEAAADVNRLLAEFLGK 370
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
31-259 1.51e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 62.49  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   31 LLIFNGIGANlelVFPFIEALDPDLEVIAFDVPGVGGSSTPrhPYRFPGLAKLTARMLDYLDYGQVNVIGVSWGGALAQQ 110
Cdd:pfam12697   1 VVLVHGAGLS---AAPLAALLAAGVAVLAPDLPGHGSSSPP--PLDLADLADLAALLDELGAARPVVLVGHSLGGAVALA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  111 FAHDYPERCkkLVLAATAAGAVMVPGKPKvlWMMASPRRYVQPSHvirIAPMIYGGGFRRDPDLAMHHAAKVRSGGKLGY 190
Cdd:pfam12697  76 AAAAALVVG--VLVAPLAAPPGLLAALLA--LLARLGAALAAPAW---LAAESLARGFLDDLPADAEWAAALARLAALLA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501231543  191 YWQLFAGLGWTSIhwlhkiqQPTLVLAGDDDPLIPLINMRLLAwRIPNAQLHIIDDGHLFLITRAEAVA 259
Cdd:pfam12697 149 ALALLPLAAWRDL-------PVPVLVLAEEDRLVPELAQRLLA-ALAGARLVVLPGAGHLPLDDPEEVA 209
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
57-268 6.92e-10

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 58.03  E-value: 6.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  57 VIAFDVPGVGGSSTPrhpyrfpgLAKLTARM--------LDYL--DYGQVNVIGVSWGGALAQQFAHDYPErCKKLVLAA 126
Cdd:COG1647   45 VYAPRLPGHGTSPED--------LLKTTWEDwledveeaYEILkaGYDKVIVIGLSMGGLLALLLAARYPD-VAGLVLLS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543 127 TAAGavMVPGKPKVLWMMASPRRYVQpshviRIAPMIygggfrRDPDLAMHHAAKVRSGGklgyYWQLFAGLGWTSIHwL 206
Cdd:COG1647  116 PALK--IDDPSAPLLPLLKYLARSLR-----GIGSDI------EDPEVAEYAYDRTPLRA----LAELQRLIREVRRD-L 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501231543 207 HKIQQPTLVLAGDDDPLIPLINMRLLAWRI--PNAQLHIIDD-GHLFLITR-AEAVAPIIMKFLQQ 268
Cdd:COG1647  178 PKITAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDsGHVITLDKdREEVAEEILDFLER 243
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
31-251 4.48e-09

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: 55.68  E-value: 4.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   31 LLIFNGIGANLELVFPFIEAL-DPDLEVIAFDVPGVGGSstPRHPYRFPGLAKLTARMLDYLDYGQVN-------VIGVS 102
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALaAQGFAVYAYDHRGHGRS--DGKRGHVPSFDDYVDDLDTFVDKIREEhpglplfLLGHS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  103 WGGALAQQFAHDYPERCKKLVLAATA---AGAVMVPGKPKVLWMMAS--PRRYVQPSHvirIAPMIYgggfrRDPD-LAM 176
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGLILSAPAlkiKPYLAPPILKLLAKLLGKlfPRLRVPNNL---LPDSLS-----RDPEvVAA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501231543  177 HHAAKVRSGG-KLGYYWQLFAGLGWTSIHwLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNA--QLHIIDDG-HLFL 251
Cdd:pfam12146 157 YAADPLVHGGiSARTLYELLDAGERLLRR-AAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPGLyHELL 234
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
7-128 1.65e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 51.83  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543   7 FRTVELDDQSIRTAVRPGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPrhPYRFPGLAKLTAR 86
Cdd:PLN02894  84 FRSASNEPRFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRP--DFTCKSTEETEAW 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501231543  87 MLDYLD-------YGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATA 128
Cdd:PLN02894 162 FIDSFEewrkaknLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPA 210
PRK08775 PRK08775
homoserine O-succinyltransferase;
27-128 4.75e-06

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 47.09  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  27 HLTPLLIFNGIGANLELVFPFiEALDPD-LEVIAFDVPGVGGSSTPrhPYRFPGLAKLTARMLDYLDYGQVNVI-GVSWG 104
Cdd:PRK08775  72 HVAATATFPEKGWWEGLVGSG-RALDPArFRLLAFDFIGADGSLDV--PIDTADQADAIALLLDALGIARLHAFvGYSYG 148
                         90       100
                 ....*....|....*....|....
gi 501231543 105 GALAQQFAHDYPERCKKLVLAATA 128
Cdd:PRK08775 149 ALVGLQFASRHPARVRTLVVVSGA 172
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
57-268 4.87e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 46.55  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  57 VIAFDVPGVGGSSTPRHPYRFP----GLAKLTARmlDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKklvlaataAGAV 132
Cdd:COG1506   54 VLAPDYRGYGESAGDWGGDEVDdvlaAIDYLAAR--PYVDPDRIGIYGHSYGGYMALLAAARHPDRFK--------AAVA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543 133 MVPgkpkvlwmMASPRRYVqpsHVIRIAPMIYGGGFRRDPDLamhhaakvrsggklgyYWQlfaglgWTSIHWLHKIQQP 212
Cdd:COG1506  124 LAG--------VSDLRSYY---GTTREYTERLMGGPWEDPEA----------------YAA------RSPLAYADKLKTP 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501231543 213 TLVLAGDDDPLIPLINMRLLA----WRIPNAQLHIIDD-GHLFLITRAEAVAPIIMKFLQQ 268
Cdd:COG1506  171 LLLIHGEADDRVPPEQAERLYealkKAGKPVELLVYPGeGHGFSGAGAPDYLERILDFLDR 231
MET2 COG2021
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ...
50-129 8.84e-05

Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441624 [Multi-domain]  Cd Length: 355  Bit Score: 43.16  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231543  50 ALDPDlE--VIAFDVPG-VGGSSTPRH-------PY--RFPGL-----AKLTARMLDYLDYGQVN-VIGVSWGGALAQQF 111
Cdd:COG2021   67 AIDTD-RyfVICSNVLGgCYGSTGPASinpatgkPYglDFPVVtirdmVRAQKRLLDHLGIERLAaVIGGSMGGMQALEW 145
                         90
                 ....*....|....*...
gi 501231543 112 AHDYPERCKKLVLAATAA 129
Cdd:COG2021  146 AVSYPDRVRRAIVIATAA 163
metX PRK00175
homoserine O-acetyltransferase; Provisional
67-128 6.16e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 37.86  E-value: 6.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501231543  67 GSSTPRH-------PY--RFPGL-----AKLTARMLDYLDYGQVN-VIGVSWGGALAQQFAHDYPERCKK-LVLAATA 128
Cdd:PRK00175 105 GSTGPSSinpdtgkPYgsDFPVItirdwVRAQARLLDALGITRLAaVVGGSMGGMQALEWAIDYPDRVRSaLVIASSA 182
 
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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