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Conserved domains on  [gi|518913330|ref|WP_020069205|]
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S-formylglutathione hydrolase [Paraburkholderia caledonica]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 3-281 2.05e-173

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member TIGR02821:

Pssm-ID: 473884  Cd Length: 275  Bit Score: 479.66  E-value: 2.05e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330    3 ELLSSHACHGGEQRFYRHESQTVGLPMRFSVYLPPQALqpDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVAP 82
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAA--AGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   83 DTSPRGAGVPNESAAWDFGVGAGFYVDATQDPWARHYRMYSYVRDELRETVLKELPVDGSRLGIFGHSMGGHGALMMALR 162
Cdd:TIGR02821  79 DTSPRGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  163 NPDIYRSVSAFAPIAAPTRAPWGEKAFSGYLGENRETWKEYDASELVRRasRQFAEGILVDQGLADQFLAEQLYPDVFEA 242
Cdd:TIGR02821 159 NPDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVAD--GGRHSTILIDQGTADQFLDEQLRPDAFEQ 236

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 518913330  243 ACREAGQPLTLRRHAGYDHGYYFISTFIQDHIAHHAKVL 281
Cdd:TIGR02821 237 ACRAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 3-281 2.05e-173

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 479.66  E-value: 2.05e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330    3 ELLSSHACHGGEQRFYRHESQTVGLPMRFSVYLPPQALqpDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVAP 82
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAA--AGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   83 DTSPRGAGVPNESAAWDFGVGAGFYVDATQDPWARHYRMYSYVRDELRETVLKELPVDGSRLGIFGHSMGGHGALMMALR 162
Cdd:TIGR02821  79 DTSPRGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  163 NPDIYRSVSAFAPIAAPTRAPWGEKAFSGYLGENRETWKEYDASELVRRasRQFAEGILVDQGLADQFLAEQLYPDVFEA 242
Cdd:TIGR02821 159 NPDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVAD--GGRHSTILIDQGTADQFLDEQLRPDAFEQ 236

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 518913330  243 ACREAGQPLTLRRHAGYDHGYYFISTFIQDHIAHHAKVL 281
Cdd:TIGR02821 237 ACRAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-281 7.53e-146

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 410.32  E-value: 7.53e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   2 LELLSSHACHGGEQRFYRHESQTVGLPMRFSVYLPPQAlqPDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVA 81
Cdd:PLN02442   5 LKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPAS--DSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  82 PDTSPRGAGVPNESAAWDFGVGAGFYVDATQDPWaRHYRMYSYVRDELREtVLKEL--PVDGSRLGIFGHSMGGHGALMM 159
Cdd:PLN02442  83 PDTSPRGLNVEGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPK-LLSDNfdQLDTSRASIFGHSMGGHGALTI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 160 ALRNPDIYRSVSAFAPIAAPTRAPWGEKAFSGYLGENRETWKEYDASELVRRASrQFAEGILVDQGLADQFLAEQLYPDV 239
Cdd:PLN02442 161 YLKNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFN-DVSATILIDQGEADKFLKEQLLPEN 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 518913330 240 FEAACREAGQPLTLRRHAGYDHGYYFISTFIQDHIAHHAKVL 281
Cdd:PLN02442 240 FEEACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQAL 281
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
12-281 1.07e-100

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 294.43  E-value: 1.07e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  12 GGEQRFYRHESQTVGLPMRFSVYLPPQAlqPDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVAPDtsprgagv 91
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGY--DGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD-------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  92 pnesaawdfGVGAGFYVDATQDPwARHYRMYSYVRDELRETVLKELPVD--GSRLGIFGHSMGGHGALMMALRNPDIYRS 169
Cdd:COG0627   71 ---------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSadRERRAIAGLSMGGHGALTLALRHPDLFRA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 170 VSAFAPIAAPTRAPWGEKAFSGYLG-ENRETWKEYDASELVRRASRQFAegILVDQGLADQFLAEQlyPDVFEAACREAG 248
Cdd:COG0627  141 VAAFSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKLRAGLP--LYIDCGTADPFFLEA--NRQLHAALRAAG 216

                        250       260       270
                 ....*....|....*....|....*....|...
gi 518913330 249 QPLTLRRHAGYdHGYYFISTFIQDHIAHHAKVL 281
Cdd:COG0627  217 IPHTYRERPGG-HSWYYWASFLEDHLPFLARAL 248
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 22-276 1.69e-51

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: 169.18  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   22 SQTVGLPMRFSVYLPPQAlQPDAKVPALFYLAGlTCTEETFPIKAGAQRFAAQHGVALVAPDTSPRGAGVPNESAaWDFG 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDY-PPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSD-WDRG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  102 VgagfyvDATQDPWARHYRmySYVRDELRETVLKELPVDGSRLGIFGHSMGGHGALMMALRNPDIYRSVSAFAPIAAPTR 181
Cdd:pfam00756  78 L------NATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  182 APWGEkafsgylgENRETWKEYDASELVRRASR-QFAEGILVDQGLADQFLAEQLYPDVFEAACREAGQP--LTLRRHAG 258
Cdd:pfam00756 150 SMWGP--------EDDPAWQEGDPVLLAVALSAnNTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAeqLAYRGVGG 221

                         250       260
                  ....*....|....*....|....*
gi 518913330  259 YDHGY-------YFISTFIQDHIAH 276
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 3-281 2.05e-173

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 479.66  E-value: 2.05e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330    3 ELLSSHACHGGEQRFYRHESQTVGLPMRFSVYLPPQALqpDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVAP 82
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAA--AGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   83 DTSPRGAGVPNESAAWDFGVGAGFYVDATQDPWARHYRMYSYVRDELRETVLKELPVDGSRLGIFGHSMGGHGALMMALR 162
Cdd:TIGR02821  79 DTSPRGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  163 NPDIYRSVSAFAPIAAPTRAPWGEKAFSGYLGENRETWKEYDASELVRRasRQFAEGILVDQGLADQFLAEQLYPDVFEA 242
Cdd:TIGR02821 159 NPDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVAD--GGRHSTILIDQGTADQFLDEQLRPDAFEQ 236

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 518913330  243 ACREAGQPLTLRRHAGYDHGYYFISTFIQDHIAHHAKVL 281
Cdd:TIGR02821 237 ACRAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-281 7.53e-146

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 410.32  E-value: 7.53e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   2 LELLSSHACHGGEQRFYRHESQTVGLPMRFSVYLPPQAlqPDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVA 81
Cdd:PLN02442   5 LKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPAS--DSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  82 PDTSPRGAGVPNESAAWDFGVGAGFYVDATQDPWaRHYRMYSYVRDELREtVLKEL--PVDGSRLGIFGHSMGGHGALMM 159
Cdd:PLN02442  83 PDTSPRGLNVEGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPK-LLSDNfdQLDTSRASIFGHSMGGHGALTI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 160 ALRNPDIYRSVSAFAPIAAPTRAPWGEKAFSGYLGENRETWKEYDASELVRRASrQFAEGILVDQGLADQFLAEQLYPDV 239
Cdd:PLN02442 161 YLKNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFN-DVSATILIDQGEADKFLKEQLLPEN 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 518913330 240 FEAACREAGQPLTLRRHAGYDHGYYFISTFIQDHIAHHAKVL 281
Cdd:PLN02442 240 FEEACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQAL 281
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
12-281 1.07e-100

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 294.43  E-value: 1.07e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  12 GGEQRFYRHESQTVGLPMRFSVYLPPQAlqPDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVAPDtsprgagv 91
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGY--DGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD-------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  92 pnesaawdfGVGAGFYVDATQDPwARHYRMYSYVRDELRETVLKELPVD--GSRLGIFGHSMGGHGALMMALRNPDIYRS 169
Cdd:COG0627   71 ---------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSadRERRAIAGLSMGGHGALTLALRHPDLFRA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 170 VSAFAPIAAPTRAPWGEKAFSGYLG-ENRETWKEYDASELVRRASRQFAegILVDQGLADQFLAEQlyPDVFEAACREAG 248
Cdd:COG0627  141 VAAFSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKLRAGLP--LYIDCGTADPFFLEA--NRQLHAALRAAG 216

                        250       260       270
                 ....*....|....*....|....*....|...
gi 518913330 249 QPLTLRRHAGYdHGYYFISTFIQDHIAHHAKVL 281
Cdd:COG0627  217 IPHTYRERPGG-HSWYYWASFLEDHLPFLARAL 248
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 22-276 1.69e-51

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: 169.18  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   22 SQTVGLPMRFSVYLPPQAlQPDAKVPALFYLAGlTCTEETFPIKAGAQRFAAQHGVALVAPDTSPRGAGVPNESAaWDFG 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDY-PPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSD-WDRG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  102 VgagfyvDATQDPWARHYRmySYVRDELRETVLKELPVDGSRLGIFGHSMGGHGALMMALRNPDIYRSVSAFAPIAAPTR 181
Cdd:pfam00756  78 L------NATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  182 APWGEkafsgylgENRETWKEYDASELVRRASR-QFAEGILVDQGLADQFLAEQLYPDVFEAACREAGQP--LTLRRHAG 258
Cdd:pfam00756 150 SMWGP--------EDDPAWQEGDPVLLAVALSAnNTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAeqLAYRGVGG 221

                         250       260
                  ....*....|....*....|....*
gi 518913330  259 YDHGY-------YFISTFIQDHIAH 276
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
12-258 3.65e-15

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 74.12  E-value: 3.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  12 GGEQRFYRHESQTVGLPMRFSVYLPPQALQPDAKVPALFYLAGLTCTEETFPIKAGAQRFA----AQHGV---ALVAPDT 84
Cdd:COG2382   78 HGTVETVTYPSKALGRTRRVWVYLPPGYDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILdnliAAGKIppmIVVMPDG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  85 SPRGAGVPNESAAWDFGvgagfyvdatqdpwarhyrmySYVRDELRETVLKELPV--DGSRLGIFGHSMGGHGALMMALR 162
Cdd:COG2382  158 GDGGDRGTEGPGNDAFE---------------------RFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALR 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 163 NPDIYRSVSafapiaaptrapwgekAFSGYLGENRETWKEYDASELVRRASRQFAEGILVDQGLADQFLAEQLypdVFEA 242
Cdd:COG2382  217 HPDLFGYVG----------------SFSGSFWWPPGDADRGGWAELLAAGAPKKPLRFYLDVGTEDDLLEANR---ALAA 277

                        250
                 ....*....|....*.
gi 518913330 243 ACREAGQPLTLRRHAG 258
Cdd:COG2382  278 ALKAKGYDVEYREFPG 293
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
26-264 9.38e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 68.89  E-value: 9.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  26 GLPMRFSVYLPPqalqPDAKVPALFYLAGLTCTEETFpIKAGAQRFAaQHGVALVAPDtsPRGAGvpnESAAwdfGVGAG 105
Cdd:COG1506    7 GTTLPGWLYLPA----DGKKYPVVVYVHGGPGSRDDS-FLPLAQALA-SRGYAVLAPD--YRGYG---ESAG---DWGGD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 106 FYVDATQdpWARHyrmysyvrdelretvLKELP-VDGSRLGIFGHSMGGHGALMMALRNPDIYRSVSAFAPIAAP----T 180
Cdd:COG1506   73 EVDDVLA--AIDY---------------LAARPyVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLrsyyG 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 181 RAPWGEKAFSGYLGENRETWKEYDASELVRRASRqfaeGILVDQGLADQFL----AEQLYpdvfeAACREAGQPLTLRRH 256
Cdd:COG1506  136 TTREYTERLMGGPWEDPEAYAARSPLAYADKLKT----PLLLIHGEADDRVppeqAERLY-----EALKKAGKPVELLVY 206


                 ....*...
gi 518913330 257 AGYDHGYY 264
Cdd:COG1506  207 PGEGHGFS 214
COG4099 COG4099
Predicted peptidase [General function prediction only];
1-178 5.83e-12

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 63.83  E-value: 5.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   1 MLELLSSHACHGGEQRFYRHESQtvGLPMRFSVYLPPqALQPDAKVPALFYL--AGLTCTEETFPIKAGAQRFA-----A 73
Cdd:COG4099    7 LLLLLGCAAQDGFEARTFTDPSD--GDTLPYRLYLPK-GYDPGKKYPLVLFLhgAGERGTDNEKQLTHGAPKFInpenqA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  74 QHGVALVAPdtsprgagvpnesaawdfgvgagfyvdatQDPWARHYRMYSYVRD--ELRETVLKELPVDGSRLGIFGHSM 151
Cdd:COG4099   84 KFPAIVLAP-----------------------------QCPEDDYWSDTKALDAvlALLDDLIAEYRIDPDRIYLTGLSM 134

                        170       180
                 ....*....|....*....|....*..
gi 518913330 152 GGHGALMMALRNPDIYrsvSAFAPIAA 178
Cdd:COG4099  135 GGYGTWDLAARYPDLF---AAAVPICG 158
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
13-175 4.59e-09

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 55.76  E-value: 4.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  13 GEQRFYRHESQTVGLPMRFSVYLPPQALQPDAKVPALFYLAGltctEETFPIKAGAQRFAAQHG-----VALVAPDTSPR 87
Cdd:COG2819    5 GQTEYFTLESPILGEDRRIRVYLPPGYDAPEKRYPVLYMLDG----QNLFDALAGAVGTLSRLEggippAIVVGIGNGDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  88 GAG-------VPNESAAWDFGVGAGfyvdatqdpwARHYRmySYVRDELRETVLKELPVDGSRLGIFGHSMGGHGALMMA 160
Cdd:COG2819   81 GERrlrdytpPPAPGYPGPGGPGGG----------ADAFL--RFLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYAL 148

                        170
                 ....*....|....*
gi 518913330 161 LRNPDIYRSVSAFAP 175
Cdd:COG2819  149 LKYPDLFGRYIAISP 163
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 26-188 4.05e-08

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 53.08  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  26 GLPMRFSVYLPPqALQPDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVAPDTSPRGAGvpnesAAWDFGVGAG 105
Cdd:COG3509   34 GGTRTYRLYVPA-GYDGGAPLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPG-----RCWNWFDGRD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 106 FyVDATQDPwarhyrmySYVRDeLRETVLKELPVDGSRLGIFGHSMGGHGALMMALRNPDIYRSVsafAPIAAPTRAPWG 185
Cdd:COG3509  108 Q-RRGRDDV--------AFIAA-LVDDLAARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAV---APVAGLPYGAAS 174


                 ...
gi 518913330 186 EKA 188
Cdd:COG3509  175 DAA 177
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
64-175 2.83e-07

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 50.35  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  64 IKAGAQRFAAqHGVALVAPDTSPRGAGVPNESAAWDFGvgagfyvdATQDPWARHYRMYSYVRdelretVLKELP-VDGS 142
Cdd:COG0412   45 IRDVARRLAA-AGYVVLAPDLYGRGGPGDDPDEARALM--------GALDPELLAADLRAALD------WLKAQPeVDAG 109

                         90       100       110
                 ....*....|....*....|....*....|...
gi 518913330 143 RLGIFGHSMGGHGALMMALRNPDIyRSVSAFAP 175
Cdd:COG0412  110 RVGVVGFCFGGGLALLAAARGPDL-AAAVSFYG 141
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 33-261 1.34e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 45.29  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  33 VYLPPQalqPDAKVPALFYLAGLTCTEETFPIKAgaQRFAaQHGVALVAPDTS--------PRGAGVPNE---SAAWDFg 101
Cdd:COG1073   27 LYLPAG---ASKKYPAVVVAHGNGGVKEQRALYA--QRLA-ELGFNVLAFDYRgygesegePREEGSPERrdaRAAVDY- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 102 vgagfyvdatqdpwarhyrmysyvrdelretvLKELP-VDGSRLGIFGHSMGGHGALMMALRNPDI--YRSVSAFAPIAA 178
Cdd:COG1073  100 --------------------------------LRTLPgVDPERIGLLGISLGGGYALNAAATDPRVkaVILDSPFTSLED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 179 PTRAPWGEkAFSGYLGEN----RETW-----KEYDASELVRRASRQfaegILVDQGLADQFLAEQLYPDVFEAacreAGQ 249
Cdd:COG1073  148 LAAQRAKE-ARGAYLPGVpylpNVRLasllnDEFDPLAKIEKISRP----LLFIHGEKDEAVPFYMSEDLYEA----AAE 218

                        250
                 ....*....|..
gi 518913330 250 PLTLRRHAGYDH 261
Cdd:COG1073  219 PKELLIVPGAGH 230
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
131-264 3.51e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 40.68  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  131 ETVLKELPVDGSRLGIFGHSMGGHGALMMALRNPDIYRSVSAFAPIAAPTR----------APWGEKAFSGYLGENRETW 200
Cdd:pfam00326  53 EYLIEQGYTDPDRLAIWGGSYGGYLTGAALNQRPDLFKAAVAHVPVVDWLAymsdtslpftERYMEWGNPWDNEEGYDYL 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518913330  201 KEYDASELVRRASRqfaegILVDQGLADQ----FLAEQLYpdvfeAACREAGQPLTLRRHAGYDHGYY 264
Cdd:pfam00326 133 SPYSPADNVKVYPP-----LLLIHGLLDDrvppWQSLKLV-----AALQRKGVPFLLLIFPDEGHGIG 190
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
29-278 7.51e-04

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 39.86  E-value: 7.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  29 MRfsVYLPPQALQPDakvPALFYLAG---LTCTEETFPikAGAQRFAAQHGVALVAPD--TSPRgAGVPnesAAWDfgvg 103
Cdd:COG0657    1 MD--VYRPAGAKGPL---PVVVYFHGggwVSGSKDTHD--PLARRLAARAGAAVVSVDyrLAPE-HPFP---AALE---- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 104 agfyvDAtqdpwarhYRMYSYVRDELretvlKELPVDGSRLGIFGHSMGGHGALMMALRNPDIYRS-VSAFAPIAAPTra 182
Cdd:COG0657   66 -----DA--------YAALRWLRANA-----AELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPrPAAQVLIYPVL-- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 183 pwgekafsgylgenretwkEYDASELvrrasRQFAEG---ILVDQGLADQFLAEQLYpdvFEAACREAGQPLTLRRHAGY 259
Cdd:COG0657  126 -------------------DLTASPL-----RADLAGlppTLIVTGEADPLVDESEA---LAAALRAAGVPVELHVYPGG 178

                        250
                 ....*....|....*....
gi 518913330 260 DHGYYFISTFIQDHIAHHA 278
Cdd:COG0657  179 GHGFGLLAGLPEARAALAE 197
Esterase_PHB pfam10503
Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), ...
 29-188 5.41e-03

Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), feruloyl esterases (FAE), and poly(3-hydroxybutyrate) (PHB) depolymerases.


Pssm-ID: 431322 [Multi-domain]  Cd Length: 222  Bit Score: 37.35  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330   29 MRFSVYLPPQALQPDAKVPALFYLAGLTCTEETFPIKAGAQRFAAQHGVALVAPDTSPRGagvpNESAAWDFGVGAGfyv 108
Cdd:pfam10503   1 LAYALYLPPEAAGDGAPMPLVVMLHGCKQHADDFAAGTRINALADELGFAVLYPEQSKHA----HAHKCWNWFDEQG--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330  109 datqdpwARHYRMYSYVRDELRETVLKELPVDGSRLGIFGHSMGGHGALMMALRNPDIyrsvsaFAPIAAPTRAPWGEKA 188
Cdd:pfam10503  74 -------AARGGGEAASIAALAKAIAAAHRLDGARVYLAGLSAGAALAALLAHCYPDV------FAAVGLHSGLPFGCAA 140
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
139-160 6.91e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 37.39  E-value: 6.91e-03
                         10        20
                 ....*....|....*....|..
gi 518913330 139 VDGSRLGIFGHSMGGHGALMMA 160
Cdd:COG4188  149 LDLDRIGVIGHSLGGYTALALA 170
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 127-238 8.35e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 37.23  E-value: 8.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518913330 127 DELRETV---LKELPVDgsRLGIFGHSMGGHGALMMALRNPDIYRSVSAFAPiaaptrAPWGEKAFSGYL-----GENRE 198
Cdd:PRK14875 181 DELAAAVlafLDALGIE--RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP------AGLGPEINGDYIdgfvaAESRR 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518913330 199 TWKEY------DASELvrraSRQFAEGIL-------VDQGLADqfLAEQLYPD 238
Cdd:PRK14875 253 ELKPVlellfaDPALV----TRQMVEDLLkykrldgVDDALRA--LADALFAG 299
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 113-170 9.46e-03

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: 36.52  E-value: 9.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 518913330 113 DPWARHYRMYSYVRDeLREtVLKELPVDgsRLGIFGHSMGGHGALMMALRNPDIYRSV 170
Cdd:COG0596   64 DKPAGGYTLDDLADD-LAA-LLDALGLE--RVVLVGHSMGGMVALELAARHPERVAGL 117
 
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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