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Conserved domains on  [gi|1370808539|gb|AVR14999|]
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alpha/beta hydrolase [Burkholderia vietnamiensis]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 21-287 3.35e-42

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: 144.37  E-value: 3.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  21 FVKAAGTTFAYRELGPHGgIPLVLLNHWGAVLDNFDPrIVDGLAHKHRVIAVDYRGIGLSGGIA-PVTVGEMARDTIALI 99
Cdd:COG0596     6 FVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRP-LIPALAAGYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 100 HAMGFDRVDLLGFSLGGFVAQDVALKAPGLVRKLILTGtgpagghgidrvgavswplmlkglltlrdpkaylfftsttng 179
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------------ 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 180 rRAASAFLKRLkerktgRDKGPTPRAFLHQLRAIKAWgqQAPQDLTNLPMPVLIANGDNDIMVPTALSHDMAHRIPDAQL 259
Cdd:COG0596   122 -EVLAALAEPL------RRPGLAPEALAALLRALART--DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAEL 192

                         250       260
                  ....*....|....*....|....*...
gi 1370808539 260 IIYQDAGHGGIFQHYTSFVPTALEFLSQ 287
Cdd:COG0596   193 VVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 21-287 3.35e-42

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: 144.37  E-value: 3.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  21 FVKAAGTTFAYRELGPHGgIPLVLLNHWGAVLDNFDPrIVDGLAHKHRVIAVDYRGIGLSGGIA-PVTVGEMARDTIALI 99
Cdd:COG0596     6 FVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRP-LIPALAAGYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 100 HAMGFDRVDLLGFSLGGFVAQDVALKAPGLVRKLILTGtgpagghgidrvgavswplmlkglltlrdpkaylfftsttng 179
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------------ 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 180 rRAASAFLKRLkerktgRDKGPTPRAFLHQLRAIKAWgqQAPQDLTNLPMPVLIANGDNDIMVPTALSHDMAHRIPDAQL 259
Cdd:COG0596   122 -EVLAALAEPL------RRPGLAPEALAALLRALART--DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAEL 192

                         250       260
                  ....*....|....*....|....*...
gi 1370808539 260 IIYQDAGHGGIFQHYTSFVPTALEFLSQ 287
Cdd:COG0596   193 VVLPGAGHFPPLEQPEAFAAALRDFLAR 220
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 26-267 1.53e-19

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 87.31  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  26 GTTFAYRELGPHGGIPLVLLNHWGAVLDNFDPRIvDGLAHKHRVIAVDYRGIGLSGG-IAPVTVGEMARDTIALIHAMGF 104
Cdd:PRK14875  118 GRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNH-AALAAGRPVIALDLPGHGASSKaVGAGSLDELAAAVLAFLDALGI 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 105 DRVDLLGFSLGGFVAQDVALKAPGLVRKLILtgTGPAG-GHGIDR------VGAVSwPLMLKGLLTLrdpkayLFFTSTT 177
Cdd:PRK14875  197 ERAHLVGHSMGGAVALRLAARAPQRVASLTL--IAPAGlGPEINGdyidgfVAAES-RRELKPVLEL------LFADPAL 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 178 NGRRAASAFL--KRLKERktgrdkgptpRAFLHQL-RAIKAWGQQAPQ---DLTNLPMPVLIANGDNDIMVPTALSHDMA 251
Cdd:PRK14875  268 VTRQMVEDLLkyKRLDGV----------DDALRALaDALFAGGRQRVDlrdRLASLAIPVLVIWGEQDRIIPAAHAQGLP 337

                         250
                  ....*....|....*.
gi 1370808539 252 hriPDAQLIIYQDAGH 267
Cdd:PRK14875  338 ---DGVAVHVLPGAGH 350
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 41-274 5.89e-19

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: 83.71  E-value: 5.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  41 PLVLLNH-WGAVLDNFdPRIVDGLAHKH-RVIAVDYRGIGLSGGIAP---VTVGEMARDTIALIHAMGFDRVDLLGFSLG 115
Cdd:pfam00561   1 PPVLLLHgLPGSSDLW-RKLAPALARDGfRVIALDLRGFGKSSRPKAqddYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 116 GFVAQDVALKAPGLVRKLILTGT-GPAGGHG-IDRVGAVSWPLMLKGllTLRDPKAYLFFTSTtnGRRAASAFLKRLKER 193
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAlDPPHELDeADRFILALFPGFFDG--FVADFAPNPLGRLV--AKLLALLLLRLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 194 KTGRDKGPTPRAFLHQLRAIKAWGQQAPQDLTNLPM---------PVLIANGDNDIMVPTALSHDMAHRIPDAQLIIYQD 264
Cdd:pfam00561 156 ALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRakflgrldePTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPD 235

                         250
                  ....*....|
gi 1370808539 265 AGHGGIFQHY 274
Cdd:pfam00561 236 AGHFAFLEGP 245
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 21-287 3.35e-42

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: 144.37  E-value: 3.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  21 FVKAAGTTFAYRELGPHGgIPLVLLNHWGAVLDNFDPrIVDGLAHKHRVIAVDYRGIGLSGGIA-PVTVGEMARDTIALI 99
Cdd:COG0596     6 FVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRP-LIPALAAGYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 100 HAMGFDRVDLLGFSLGGFVAQDVALKAPGLVRKLILTGtgpagghgidrvgavswplmlkglltlrdpkaylfftsttng 179
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------------ 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 180 rRAASAFLKRLkerktgRDKGPTPRAFLHQLRAIKAWgqQAPQDLTNLPMPVLIANGDNDIMVPTALSHDMAHRIPDAQL 259
Cdd:COG0596   122 -EVLAALAEPL------RRPGLAPEALAALLRALART--DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAEL 192

                         250       260
                  ....*....|....*....|....*...
gi 1370808539 260 IIYQDAGHGGIFQHYTSFVPTALEFLSQ 287
Cdd:COG0596   193 VVLPGAGHFPPLEQPEAFAAALRDFLAR 220
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 26-267 1.53e-19

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 87.31  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  26 GTTFAYRELGPHGGIPLVLLNHWGAVLDNFDPRIvDGLAHKHRVIAVDYRGIGLSGG-IAPVTVGEMARDTIALIHAMGF 104
Cdd:PRK14875  118 GRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNH-AALAAGRPVIALDLPGHGASSKaVGAGSLDELAAAVLAFLDALGI 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 105 DRVDLLGFSLGGFVAQDVALKAPGLVRKLILtgTGPAG-GHGIDR------VGAVSwPLMLKGLLTLrdpkayLFFTSTT 177
Cdd:PRK14875  197 ERAHLVGHSMGGAVALRLAARAPQRVASLTL--IAPAGlGPEINGdyidgfVAAES-RRELKPVLEL------LFADPAL 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 178 NGRRAASAFL--KRLKERktgrdkgptpRAFLHQL-RAIKAWGQQAPQ---DLTNLPMPVLIANGDNDIMVPTALSHDMA 251
Cdd:PRK14875  268 VTRQMVEDLLkyKRLDGV----------DDALRALaDALFAGGRQRVDlrdRLASLAIPVLVIWGEQDRIIPAAHAQGLP 337

                         250
                  ....*....|....*.
gi 1370808539 252 hriPDAQLIIYQDAGH 267
Cdd:PRK14875  338 ---DGVAVHVLPGAGH 350
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 41-274 5.89e-19

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: 83.71  E-value: 5.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  41 PLVLLNH-WGAVLDNFdPRIVDGLAHKH-RVIAVDYRGIGLSGGIAP---VTVGEMARDTIALIHAMGFDRVDLLGFSLG 115
Cdd:pfam00561   1 PPVLLLHgLPGSSDLW-RKLAPALARDGfRVIALDLRGFGKSSRPKAqddYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 116 GFVAQDVALKAPGLVRKLILTGT-GPAGGHG-IDRVGAVSWPLMLKGllTLRDPKAYLFFTSTtnGRRAASAFLKRLKER 193
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAlDPPHELDeADRFILALFPGFFDG--FVADFAPNPLGRLV--AKLLALLLLRLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 194 KTGRDKGPTPRAFLHQLRAIKAWGQQAPQDLTNLPM---------PVLIANGDNDIMVPTALSHDMAHRIPDAQLIIYQD 264
Cdd:pfam00561 156 ALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRakflgrldePTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPD 235

                         250
                  ....*....|
gi 1370808539 265 AGHGGIFQHY 274
Cdd:pfam00561 236 AGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-287 2.56e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 70.42  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  21 FVKAAGTTFAYRELGPHGGI-PLVLLNH-WGAVLDNFDPRIVDGLAHKHRVIAVDYRGIGLSGG--IAPVTVGEMARDT- 95
Cdd:COG2267     8 LPTRDGLRLRGRRWRPAGSPrGTVVLVHgLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGprGHVDSFDDYVDDLr 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  96 --IALIHAMGFDRVDLLGFSLGGFVAQDVALKAPGLVRKLILTGTgpagghgidrvgavswplmlkglLTLRDPkaylff 173
Cdd:COG2267    88 aaLDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP-----------------------AYRADP------ 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 174 tsttngrraasaflkrlkerktgrDKGPTPRAFlhqlraikaWGQQAPQDLTNLPMPVLIANGDNDIMVPTALSHDMAHR 253
Cdd:COG2267   139 ------------------------LLGPSARWL---------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAAR 185

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370808539 254 I-PDAQLIIYQDAGHGGIFQHY-TSFVPTALEFLSQ 287
Cdd:COG2267   186 LsPDVELVLLPGARHELLNEPArEEVLAAILAWLER 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 69-267 1.53e-11

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: 62.62  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  69 VIAVDYRGIGLSGGiAPVTV---GEMARDTIALIHAMGFDRVD----LLGFSLGGFVAQDVALKAPGLVRKLILtgTGPA 141
Cdd:pfam12146  34 VYAYDHRGHGRSDG-KRGHVpsfDDYVDDLDTFVDKIREEHPGlplfLLGHSMGGLIAALYALRYPDKVDGLIL--SAPA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 142 ggHGIDRVGAVSWPLMLKGLLTLRDPKAYLfftsttnGRRAASAFLKRLKE--RKTGRD----KGPTPRAFLHQLRAika 215
Cdd:pfam12146 111 --LKIKPYLAPPILKLLAKLLGKLFPRLRV-------PNNLLPDSLSRDPEvvAAYAADplvhGGISARTLYELLDA--- 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370808539 216 wGQQAPQDLTNLPMPVLIANGDNDIMVPTALSHDMAHRIP--DAQLIIYQDAGH 267
Cdd:pfam12146 179 -GERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGstDKTLKLYPGLYH 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
41-287 1.04e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 60.42  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  41 PLVLLNH--WGAVLDNFDPRIvDGLAHK-HRVIAVDYRGIGLSGGIAPvtvGEMARDTIALIHAM------GFDRVDLLG 111
Cdd:COG1506    24 PVVVYVHggPGSRDDSFLPLA-QALASRgYAVLAPDYRGYGESAGDWG---GDEVDDVLAAIDYLaarpyvDPDRIGIYG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 112 FSLGGFVAQDVALKAPGLVRKliltgtgpagghGIDRVGAVSWPLMLKGLLTLRDPKAYLFFTsttngrraasaFLKRLK 191
Cdd:COG1506   100 HSYGGYMALLAAARHPDRFKA------------AVALAGVSDLRSYYGTTREYTERLMGGPWE-----------DPEAYA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 192 ERktgrdkgpTPRAFLHQLRAikawgqqapqdltnlpmPVLIANGDNDIMVPTALSHDMAHRI----PDAQLIIYQDAGH 267
Cdd:COG1506   157 AR--------SPLAYADKLKT-----------------PLLLIHGEADDRVPPEQAERLYEALkkagKPVELLVYPGEGH 211

                         250       260
                  ....*....|....*....|
gi 1370808539 268 GGIFQHYTSFVPTALEFLSQ 287
Cdd:COG1506   212 GFSGAGAPDYLERILDFLDR 231
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 42-273 5.15e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 55.17  E-value: 5.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  42 LVLLNHWGAVLDNFDPRivdgLAHKHRVIAVDYRGIGLSGGiAPVTVGEMARDTIALIHAMGFDRVDLLGFSLGGFVAQD 121
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL----LAAGVAVLAPDLPGHGSSSP-PPLDLADLADLAALLDELGAARPVVLVGHSLGGAVALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 122 VALKAPglVRKLILTGTGPAGGHGIDRVGAVS--WPLMLKGLLTLRDPKAYLFFTSTTNGRRAAsaflkrlkerktgrdk 199
Cdd:pfam12697  76 AAAAAL--VVGVLVAPLAAPPGLLAALLALLArlGAALAAPAWLAAESLARGFLDDLPADAEWA---------------- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370808539 200 gptpRAFLHQLRAIKAWGQQAPQDLTNLPMPVLIANGDNDIMvpTALSHDMAHRIPDAQLIIYQDAGHGGIFQH 273
Cdd:pfam12697 138 ----AALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLV--PELAQRLLAALAGARLVVLPGAGHLPLDDP 205
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
69-267 1.89e-08

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 53.79  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  69 VIAVDYRGIGLSGG-IAPVTVGEMARDTIALIHAM--GFDRVDLLGFSLGGFVAQDVALKAPGlVRKLILTGtgPAgghg 145
Cdd:COG1647    45 VYAPRLPGHGTSPEdLLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMGGLLALLLAARYPD-VAGLVLLS--PA---- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 146 idrVGAVSWPLMLKGLLtlrdpkayLFFTSTTNGRRAAsafLKRLKERKTGRDKGPTPRafLHQLRAIkawGQQAPQDLT 225
Cdd:COG1647   118 ---LKIDDPSAPLLPLL--------KYLARSLRGIGSD---IEDPEVAEYAYDRTPLRA--LAELQRL---IREVRRDLP 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370808539 226 NLPMPVLIANGDNDIMVPTALSHDMAHRI--PDAQLIIYQDAGH 267
Cdd:COG1647   179 KITAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGH 222
PRK10673 PRK10673
esterase;
36-140 4.25e-08

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 52.81  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  36 PHGGIPLVLLNHWGAVLDNFDPRIVDgLAHKHRVIAVDYRGIGLSGGIAPVTVGEMARDTIALIHAMGFDRVDLLGFSLG 115
Cdd:PRK10673   13 PHNNSPIVLVHGLFGSLDNLGVLARD-LVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMG 91

                          90       100
                  ....*....|....*....|....*
gi 1370808539 116 GFVAQDVALKAPGLVRKLILTGTGP 140
Cdd:PRK10673   92 GKAVMALTALAPDRIDKLVAIDIAP 116
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 28-142 6.53e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 52.99  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  28 TFAYRELGPhggiPLVLLNHWGAVlDNFDPRIVDGLAHKHRVIAVDYRGIGLSGgiAPVTVGEMARDTIALI-------- 99
Cdd:PLN02894   98 TFDSKEDAP----TLVMVHGYGAS-QGFFFRNFDALASRFRVIAIDQLGWGGSS--RPDFTCKSTEETEAWFidsfeewr 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370808539 100 HAMGFDRVDLLGFSLGGFVAQDVALKAPGLVRKLILtgTGPAG 142
Cdd:PLN02894  171 KAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLIL--VGPAG 211
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
37-277 9.76e-07

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 48.86  E-value: 9.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  37 HGGIPLVLLNHWGavLDNFDPRIVDGLAHKHRVI-AVDYRGIGLSGGIAPVTVGEMArdtiALIHAMGFDRVDLLGFSLG 115
Cdd:PRK10349   11 QGNVHLVLLHGWG--LNAEVWRCIDEELSSHFTLhLVDLPGFGRSRGFGALSLADMA----EAVLQQAPDKAIWLGWSLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 116 GFVAQDVALKAPGLVRKLILTGTGPA-----GGHGIDrvgavswPLMLKGL-LTLRDP---KAYLFFTSTTNGRRAASAF 186
Cdd:PRK10349   85 GLVASQIALTHPERVQALVTVASSPCfsardEWPGIK-------PDVLAGFqQQLSDDfqrTVERFLALQTMGTETARQD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 187 LKRLKERKTGRdkgPTPRAFLHQ--LRAIKAWGQQAPqdLTNLPMPVLIANGDNDIMVPTALSHDMAHRIPDAQLIIYQD 264
Cdd:PRK10349  158 ARALKKTVLAL---PMPEVDVLNggLEILKTVDLRQP--LQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAK 232

                         250
                  ....*....|...
gi 1370808539 265 AGHGGIFQHYTSF 277
Cdd:PRK10349  233 AAHAPFISHPAEF 245
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 31-287 2.50e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 47.60  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  31 YRELGPHGGIPLVLLNH-WGAVLDNFDP---RIVD-GLAhkhrVIAVDYRGIGLSGGiAPVTVGEMA-RDTIALI-HAMG 103
Cdd:COG1073    28 YLPAGASKKYPAVVVAHgNGGVKEQRALyaqRLAElGFN----VLAFDYRGYGESEG-EPREEGSPErRDARAAVdYLRT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 104 FDRVD-----LLGFSLGGFVAQDVALkapglvrkliltgtgpagghgidrvgavswplmlkgllTLRDPKAYLFFTSTTN 178
Cdd:COG1073   103 LPGVDperigLLGISLGGGYALNAAA--------------------------------------TDPRVKAVILDSPFTS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 179 GRRAASAFLKRLKERKTGRDkgptprAFLHQLRAIKAWGQQAP--QDLTNLPMPVLIANGDNDIMVPTALSHDMAHRIPD 256
Cdd:COG1073   145 LEDLAAQRAKEARGAYLPGV------PYLPNVRLASLLNDEFDplAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAE 218

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370808539 257 A-QLIIYQDAGHGGIF-QHYTSFVPTALEFLSQ 287
Cdd:COG1073   219 PkELLIVPGAGHVDLYdRPEEEYFDKLAEFFKK 251
PRK05855 PRK05855
SDR family oxidoreductase;
21-111 9.77e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 46.51  E-value: 9.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  21 FVKAAGTTFAYRELGPHGGiPLVLLNH--------WGAVldnfdpriVDGLAHKHRVIAVDYRGIGLSGGIAPV---TVG 89
Cdd:PRK05855    7 VVSSDGVRLAVYEWGDPDR-PTVVLVHgypdnhevWDGV--------APLLADRFRVVAYDVRGAGRSSAPKRTaayTLA 77

                          90       100
                  ....*....|....*....|...
gi 1370808539  90 EMARDTIALIHAMGFDR-VDLLG 111
Cdd:PRK05855   78 RLADDFAAVIDAVSPDRpVHLLA 100
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 21-131 5.32e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 40.75  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  21 FVKAAGTTFAYRELGphGGIPLVLLnH--------WGAVLdnfdPRivdgLAHKHRVIAVDYRGIGLSGGIAP-VTVGEM 91
Cdd:PRK03592   11 RVEVLGSRMAYIETG--EGDPIVFL-HgnptssylWRNII----PH----LAGLGRCLAPDLIGMGASDKPDIdYTFADH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370808539  92 ARDTIALIHAMGFDRVDLLGFSLGGFVAQDVALKAPGLVR 131
Cdd:PRK03592   80 ARYLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVR 119
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
 204-285 5.81e-04

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: 38.47  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539 204 RAFLHQLRAIKAW--GQQAPQDLTNLPM--PVLIANGDNDIMVPTALSHDMAHRIPDAQLIIYQDAGHGGIFQHYTSFVP 279
Cdd:pfam08386   5 AYWAEGLLSCAGWpvPPVPPPDESTAKGapPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGHGAYIGGNACVDK 84


                  ....*.
gi 1370808539 280 TALEFL 285
Cdd:pfam08386  85 AVDAYL 90
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 38-138 1.41e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 39.45  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370808539  38 GGIPLVLLNHWGAVLDNFDPRIVDGLAHKHRVIAVDYRGIGLS---GGIApVTVGEMARDTIALIHAMGFDRVDLLGFSL 114
Cdd:PRK03204   32 GTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSerpSGFG-YQIDEHARVIGEFVDHLGLDRYLSMGQDW 110

                          90       100
                  ....*....|....*....|....
gi 1370808539 115 GGFVAQDVALKAPGLVRKLILTGT 138
Cdd:PRK03204  111 GGPISMAVAVERADRVRGVVLGNT 134
PRK08775 PRK08775
homoserine O-succinyltransferase;
66-135 4.95e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 37.85  E-value: 4.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370808539  66 KHRVIAVDYrgIGLSGGI-APVTVGEMARDTIALIHAMGFDRVD-LLGFSLGGFVAQDVALKAPGLVRKLIL 135
Cdd:PRK08775   99 RFRLLAFDF--IGADGSLdVPIDTADQADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPARVRTLVV 168
 
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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