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Conserved domains on  [gi|491225110|ref|WP_005083398|]
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alpha/beta hydrolase [Mycobacteroides abscessus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 12118179)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  12369917|19508187|37582413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 7-221 1.52e-19

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


:

Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 83.29  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110    7 IVLVHGFWGG--------AAHWGNVIVELHGRGFEDLHAVEnpLTSLADDAARTRQMVQqiDGPVLLVGHSYGGAVITEA 78
Cdd:pfam12697   1 VVLVHGAGLSaaplaallAAGVAVLAPDLPGHGSSSPPPLD--LADLADLAALLDELGA--ARPVVLVGHSLGGAVALAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   79 GDLPNVAGLVYVAAFAPDAGESPgqlteqlPPAAAANLVPDSDGYLWIKQDKFRESFAQDLPEDAALVMAVTQKAPLAST 158
Cdd:pfam12697  77 AAAALVVGVLVAPLAAPPGLLAA-------LLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491225110  159 FgDAITAPAWRNKPSWYQV-STQDRMINPENERRMAQRIKPRKTIELDASHASLaSQPVAIADL 221
Cdd:pfam12697 150 L-ALLPLAAWRDLPVPVLVlAEEDRLVPELAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
 
Name Accession Description Interval E-value
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 7-221 1.52e-19

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 83.29  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110    7 IVLVHGFWGG--------AAHWGNVIVELHGRGFEDLHAVEnpLTSLADDAARTRQMVQqiDGPVLLVGHSYGGAVITEA 78
Cdd:pfam12697   1 VVLVHGAGLSaaplaallAAGVAVLAPDLPGHGSSSPPPLD--LADLADLAALLDELGA--ARPVVLVGHSLGGAVALAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   79 GDLPNVAGLVYVAAFAPDAGESPgqlteqlPPAAAANLVPDSDGYLWIKQDKFRESFAQDLPEDAALVMAVTQKAPLAST 158
Cdd:pfam12697  77 AAAALVVGVLVAPLAAPPGLLAA-------LLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491225110  159 FgDAITAPAWRNKPSWYQV-STQDRMINPENERRMAQRIKPRKTIELDASHASLaSQPVAIADL 221
Cdd:pfam12697 150 L-ALLPLAAWRDLPVPVLVlAEEDRLVPELAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-224 5.19e-15

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: 71.19  E-value: 5.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   3 SKPTIVLVHGFWGGAAHWGNVI-----------VELHGRGFEDLHAVENPLTSLADDAARTRQMVQqiDGPVLLVGHSYG 71
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIpalaagyrviaPDLRGHGRSDKPAGGYTLDDLADDLAALLDALG--LERVVLVGHSMG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110  72 GAVITE-AGDLPN-VAGLVYVAAFApDAGESPGQLTEQLPPAAAANLvpdsdgylwikqdkfRESFAQDLPEDAAlvmav 149
Cdd:COG0596  100 GMVALElAARHPErVAGLVLVDEVL-AALAEPLRRPGLAPEALAALL---------------RALARTDLRERLA----- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491225110 150 tqkaplastfgdAITAPAwrnkpsWYQVSTQDRMINPENERRMAQRIKPRKTIEL-DASHASLASQPVAIADLIAE 224
Cdd:COG0596  159 ------------RITVPT------LVIWGEKDPIVPPALARRLAELLPNAELVVLpGAGHFPPLEQPEAFAAALRD 216
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
 4-229 1.85e-05

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 44.50  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   4 KPTIVLVHGFWGGAAHWGNV------------IVELHGRGFEDLHAveNPLTSLADDAARTRQMVQQI--DGPVLLVGHS 69
Cdd:PLN02211  18 PPHFVLIHGISGGSWCWYKIrclmensgykvtCIDLKSAGIDQSDA--DSVTTFDEYNKPLIDFLSSLpeNEKVILVGHS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110  70 YGGAVITEAGD-LPNVAGL-VYVAAFAPDAGESPGQLTEQLPPAAAA---------NLVPDSDGYLWIKQDKFRESFAQD 138
Cdd:PLN02211  96 AGGLSVTQAIHrFPKKICLaVYVAATMLKLGFQTDEDMKDGVPDLSEfgdvyelgfGLGPDQPPTSAIIKKEFRRKILYQ 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110 139 LP--EDAALVMAVTQKAPLAstfgdAITAPAWRNK-------PSWYQVSTQDRMINPENERRMAQRIKPRKTIELDASHA 209
Cdd:PLN02211 176 MSpqEDSTLAAMLLRPGPIL-----ALRSARFEEEtgdidkvPRVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELESDHS 250

                        250       260
                 ....*....|....*....|
gi 491225110 210 SLASQPVAIADLIAEAAGDI 229
Cdd:PLN02211 251 PFFSTPFLLFGLLIKAAASV 270
 
Name Accession Description Interval E-value
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 7-221 1.52e-19

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 83.29  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110    7 IVLVHGFWGG--------AAHWGNVIVELHGRGFEDLHAVEnpLTSLADDAARTRQMVQqiDGPVLLVGHSYGGAVITEA 78
Cdd:pfam12697   1 VVLVHGAGLSaaplaallAAGVAVLAPDLPGHGSSSPPPLD--LADLADLAALLDELGA--ARPVVLVGHSLGGAVALAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   79 GDLPNVAGLVYVAAFAPDAGESPgqlteqlPPAAAANLVPDSDGYLWIKQDKFRESFAQDLPEDAALVMAVTQKAPLAST 158
Cdd:pfam12697  77 AAAALVVGVLVAPLAAPPGLLAA-------LLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491225110  159 FgDAITAPAWRNKPSWYQV-STQDRMINPENERRMAQRIKPRKTIELDASHASLaSQPVAIADL 221
Cdd:pfam12697 150 L-ALLPLAAWRDLPVPVLVlAEEDRLVPELAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-224 5.19e-15

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: 71.19  E-value: 5.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   3 SKPTIVLVHGFWGGAAHWGNVI-----------VELHGRGFEDLHAVENPLTSLADDAARTRQMVQqiDGPVLLVGHSYG 71
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIpalaagyrviaPDLRGHGRSDKPAGGYTLDDLADDLAALLDALG--LERVVLVGHSMG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110  72 GAVITE-AGDLPN-VAGLVYVAAFApDAGESPGQLTEQLPPAAAANLvpdsdgylwikqdkfRESFAQDLPEDAAlvmav 149
Cdd:COG0596  100 GMVALElAARHPErVAGLVLVDEVL-AALAEPLRRPGLAPEALAALL---------------RALARTDLRERLA----- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491225110 150 tqkaplastfgdAITAPAwrnkpsWYQVSTQDRMINPENERRMAQRIKPRKTIEL-DASHASLASQPVAIADLIAE 224
Cdd:COG0596  159 ------------RITVPT------LVIWGEKDPIVPPALARRLAELLPNAELVVLpGAGHFPPLEQPEAFAAALRD 216
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 7-92 8.41e-10

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 54.45  E-value: 8.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   7 IVLVHGFWGGAAHWGNVIVELHGRGFEdLHAVENPLT--SLADDAARTRQMVQQI-----DGPVLLVGHSYGG----AVI 75
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLRAAGYP-VYALNYPSTngSIEDSAEQLAAFVDAVlaatgAEKVDLVGHSMGGlvarYYL 86

                         90
                 ....*....|....*..
gi 491225110  76 TEAGDLPNVAGLVYVAA 92
Cdd:COG1075   87 KRLGGAAKVARVVTLGT 103
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
2-116 1.42e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 56.16  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   2 SSKPTIVLVHGFWGGAAHWGNVIVELHGRGFeDLHAVENP-----------LTSLADDAARTRQMVQQI----DGPVLLV 66
Cdd:COG2267   26 SPRGTVVLVHGLGEHSGRYAELAEALAAAGY-AVLAFDLRghgrsdgprghVDSFDDYVDDLRAALDALrarpGLPVVLL 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491225110  67 GHSYGGAVITE-AGDLPN-VAGLVYVA---AFAPDAGESPGQLTEQLPPAAAANL 116
Cdd:COG2267  105 GHSMGGLIALLyAARYPDrVAGLVLLApayRADPLLGPSARWLRALRLAEALARI 159
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
 4-229 1.85e-05

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 44.50  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   4 KPTIVLVHGFWGGAAHWGNV------------IVELHGRGFEDLHAveNPLTSLADDAARTRQMVQQI--DGPVLLVGHS 69
Cdd:PLN02211  18 PPHFVLIHGISGGSWCWYKIrclmensgykvtCIDLKSAGIDQSDA--DSVTTFDEYNKPLIDFLSSLpeNEKVILVGHS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110  70 YGGAVITEAGD-LPNVAGL-VYVAAFAPDAGESPGQLTEQLPPAAAA---------NLVPDSDGYLWIKQDKFRESFAQD 138
Cdd:PLN02211  96 AGGLSVTQAIHrFPKKICLaVYVAATMLKLGFQTDEDMKDGVPDLSEfgdvyelgfGLGPDQPPTSAIIKKEFRRKILYQ 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110 139 LP--EDAALVMAVTQKAPLAstfgdAITAPAWRNK-------PSWYQVSTQDRMINPENERRMAQRIKPRKTIELDASHA 209
Cdd:PLN02211 176 MSpqEDSTLAAMLLRPGPIL-----ALRSARFEEEtgdidkvPRVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELESDHS 250

                        250       260
                 ....*....|....*....|
gi 491225110 210 SLASQPVAIADLIAEAAGDI 229
Cdd:PLN02211 251 PFFSTPFLLFGLLIKAAASV 270
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
3-208 3.25e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.78  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   3 SKPTIVLVHGFWGGAAHWGNVIVELHGRGFedlhAVENPL-----TSLADDAARTRQM-----------VQQIDGPVLLV 66
Cdd:COG1647   14 GRKGVLLLHGFTGSPAEMRPLAEALAKAGY----TVYAPRlpghgTSPEDLLKTTWEDwledveeayeiLKAGYDKVIVI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110  67 GHSYGGAVITE-AGDLPNVAGLVYVA-AFAPDAGESP-----GQLTEQLPPAAAANLVPDSD--GYLWIKQDKFRESFaq 137
Cdd:COG1647   90 GLSMGGLLALLlAARYPDVAGLVLLSpALKIDDPSAPllpllKYLARSLRGIGSDIEDPEVAeyAYDRTPLRALAELQ-- 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491225110 138 dlpedaALVMAVtqKAPLastfgDAITAPAwrnkpswyQV--STQDRMINPENERRMAQRI--KPRKTIELDASH 208
Cdd:COG1647  168 ------RLIREV--RRDL-----PKITAPT--------LIiqSRKDEVVPPESARYIYERLgsPDKELVWLEDSG 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 5-97 1.98e-04

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: 41.34  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110    5 PTIVLVHGFWGGAAHWGNVIVEL--------------HGRGFEDLHAVENPLTSLADDAARTRQMVQQidGPVLLVGHSY 70
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALardgfrvialdlrgFGKSSRPKAQDDYRTDDLAEDLEYILEALGL--EKVNLVGHSM 78

                          90       100
                  ....*....|....*....|....*....
gi 491225110   71 GGAVITE-AGDLPN-VAGLVYVAAFAPDA 97
Cdd:pfam00561  79 GGLIALAyAAKYPDrVKALVLLGALDPPH 107
PLN02965 PLN02965
Probable pheophorbidase
 8-226 2.15e-04

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 41.44  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   8 VLVHGFWGGAAHWGNVIVELHGRGFE--------------------DLHAVENPLTSLADDAARtrqmvqqiDGPVLLVG 67
Cdd:PLN02965   7 VFVHGASHGAWCWYKLATLLDAAGFKstcvdltgagisltdsntvsSSDQYNRPLFALLSDLPP--------DHKVILVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110  68 HSYGGAVITEAGDL--PNVAGLVYVAAfapdAGESPGqlteQLPPAAAANLVPDSDGyLW----------------IKQD 129
Cdd:PLN02965  79 HSIGGGSVTEALCKftDKISMAIYVAA----AMVKPG----SIISPRLKNVMEGTEK-IWdytfgegpdkpptgimMKPE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110 130 KFRESFAQDLP-EDAALVMAVTQKAPLASTFG--DAITAPAWRNKPSWYQVSTQDRMINPENERRMAQRIKPRKTIEL-D 205
Cdd:PLN02965 150 FVRHYYYNQSPlEDYTLSSKLLRPAPVRAFQDldKLPPNPEAEKVPRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLeD 229

                        250       260
                 ....*....|....*....|.
gi 491225110 206 ASHASLASQPVAIADLIAEAA 226
Cdd:PLN02965 230 SDHSAFFSVPTTLFQYLLQAV 250
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
8-113 2.58e-04

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 40.22  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   8 VLVHGFWG-GAAHW--------GNV-IVELHGRgfedlhavENPltSLADDAARTRQMVQQIDGPVLLVGHSYGG-AVIT 76
Cdd:COG3545    1 LIVPGLGGsGPDHWqswwerelPTVrRVEQPDW--------DRP--DLDDWLAALDAAVAAADGPVVLVAHSLGClAVAH 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491225110  77 EAGDLPN-VAGLVYVAAFAPD-AGESPGQLTEQLPPAAA 113
Cdd:COG3545   71 WAARLPRkVAGALLVAPPDPErPGFLPELDAGFAPIPRA 109
Mbeg1-like pfam11187
Mbeg1-like; This family includes a group of uncharacterized proteins from bacteria. Recently, ...
 33-97 1.56e-03

Mbeg1-like; This family includes a group of uncharacterized proteins from bacteria. Recently, a member from Gemella sanguinis M325, Mbeg1 (for "microbiome bacteria effector gene") has been identified as the first example of this protein family being associated with a potential effector function in the human microbiome.


Pssm-ID: 402661 [Multi-domain]  Cd Length: 224  Bit Score: 38.44  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491225110   33 EDLHAVENPLTSLADDAAR-TRQMVQQIDGPVLLVGHSYGGaviteagdlpNVAglVYVAAFAPDA 97
Cdd:pfam11187  55 EDFNMSFMDEVPAQRSAAKyLNKILQHYPGKIYLGGHSKGG----------NLA--IYAAMNAEPD 108
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 5-74 2.25e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 38.14  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110    5 PTIVLVHGFWGGAAH-----------WGNVIVELHGRGFEdlhavENPLTSLADDAARTRQMVQQI--DGPVLLVGHSYG 71
Cdd:pfam00975   1 RPLFCFPPAGGSASSfrslarrlpppAEVLAVQYPGRGRG-----EPPLNSIEALADEYAEALRQIqpEGPYALFGHSMG 75


                  ...
gi 491225110   72 GAV 74
Cdd:pfam00975  76 GML 78
PLN02578 PLN02578
hydrolase
 5-120 2.61e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 38.28  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491225110   5 PTIVLVHGFWGGAAHWGNVIVELH-----------GRGFEDLHAVENPLTSLADD-AARTRQMVQQidgPVLLVGHSYGG 72
Cdd:PLN02578  87 LPIVLIHGFGASAFHWRYNIPELAkkykvyaldllGFGWSDKALIEYDAMVWRDQvADFVKEVVKE---PAVLVGNSLGG 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491225110  73 -AVITEAGDLPN-VAGLVYVaafapdagESPGQLTEQLPPAAAANLVPDS 120
Cdd:PLN02578 164 fTALSTAVGYPElVAGVALL--------NSAGQFGSESREKEEAIVVEET 205
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 25-96 3.82e-03

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.52  E-value: 3.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491225110  25 VELHGRGFEDLHAVENPLTSLADDAARtrQMVQQIDGPVLLVGHSYGGAVITE------AGDLPNVAGLVYVAAFAPD 96
Cdd:COG3208   38 VQLPGRGDRLGEPPLTSLEELADDLAE--ELAPLLDRPFALFGHSMGALLAFElarrleRRGRPLPAHLFVSGRRAPH 113
 
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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