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Conserved domains on  [gi|691055762|ref|WP_032001131|]
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S-formylglutathione hydrolase [Acinetobacter baumannii]

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, ...
 2-276 5.70e-136

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: 384.90  E-value: 5.70e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762    2 QLLQKNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGkPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPD 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAG-PVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762   82 TSPRGGQVA-VGDNWDLGQGAGFYINATEAPWSEHYQMESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKY 160
Cdd:TIGR02821  80 TSPRGTGIAgEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  161 PEKFKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVsKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQAC 239
Cdd:TIGR02821 160 PDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLV-ADGGRHSTILIDQGTADQFLdEQLRPDAFEQAC 238

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 691055762  240 LKAGQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQL 276
Cdd:TIGR02821 239 RAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 2-276 5.70e-136

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: 384.90  E-value: 5.70e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762    2 QLLQKNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGkPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPD 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAG-PVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762   82 TSPRGGQVA-VGDNWDLGQGAGFYINATEAPWSEHYQMESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKY 160
Cdd:TIGR02821  80 TSPRGTGIAgEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  161 PEKFKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVsKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQAC 239
Cdd:TIGR02821 160 PDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLV-ADGGRHSTILIDQGTADQFLdEQLRPDAFEQAC 238

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 691055762  240 LKAGQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQL 276
Cdd:TIGR02821 239 RAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 6-278 2.79e-116

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 335.59  E-value: 2.79e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762   6 KNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGKpCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDTSPR 85
Cdd:PLN02442  10 VNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGK-VPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  86 GGQV-AVGDNWDLGQGAGFYINATEAPWsEHYQMESYLIDELYPLILKSFP-VNAQQVGIFGHSMGGHGALTLAFKYPEK 163
Cdd:PLN02442  89 GLNVeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYLKNPDK 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 164 FKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVSKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQACLKA 242
Cdd:PLN02442 168 YKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLkEQLLPENFEEACKEA 247

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 691055762 243 GQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQLEK 278
Cdd:PLN02442 248 GAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALKS 283
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
12-276 1.80e-96

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 283.65  E-value: 1.80e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  12 GEQRIYQFDSQLLKGSTKFGVYLPPAAlEGKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDtsprGGQvav 91
Cdd:COG0627    2 GRVVRVTVPSPALGREMPVSVYLPPGY-DGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----GGQ--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  92 gdnwdlgqgAGFYINATEAPwSEHYQMESYLIDELYPLILKSFPVNAQ--QVGIFGHSMGGHGALTLAFKYPEKFKSVSA 169
Cdd:COG0627   74 ---------ASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSADreRRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 170 FAPICAPTECAWGEKAFSHYLGT-DRDSWLAHDATALVSKNGAVFnEILVDQGLDDQ-FYEQVHpeKFKQACLKAGQPLT 247
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRAGL-PLYIDCGTADPfFLEANR--QLHAALRAAGIPHT 220

                        250       260
                 ....*....|....*....|....*....
gi 691055762 248 LRQHAGYdHGYYFIQTFMDEHLQFHAIQL 276
Cdd:COG0627  221 YRERPGG-HSWYYWASFLEDHLPFLARAL 248
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 21-271 7.74e-50

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: 164.94  E-value: 7.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762   21 SQLLKGSTKFGVYLPPAALEGKPCSTLFYLAGlTCTEETFAIKAHAQHMAAQLSLILITPDTSPRGGQVAVGDNWDLGQg 100
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRGL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  101 agfyiNATEAPWSEHYqmESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAPTECA 180
Cdd:pfam00756  79 -----NATEGPGAYAY--ETFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  181 WGEkafshylgTDRDSWLAHDATALVsKNGAVFNE---ILVDQGLDDQFY-EQVHPEKFKQACLKAGQP--LTLRQHAGY 254
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLA-VALSANNTrlrIYLDVGTREDFLgDQLPVEILEELAPNRELAeqLAYRGVGGY 222

                         250       260
                  ....*....|....*....|....
gi 691055762  255 DHGY-------YFIQTFMDEHLQF 271
Cdd:pfam00756 223 DHEYygghdwaYWRAQLIAALIDL 246
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 2-276 5.70e-136

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: 384.90  E-value: 5.70e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762    2 QLLQKNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGkPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPD 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAG-PVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762   82 TSPRGGQVA-VGDNWDLGQGAGFYINATEAPWSEHYQMESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKY 160
Cdd:TIGR02821  80 TSPRGTGIAgEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  161 PEKFKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVsKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQAC 239
Cdd:TIGR02821 160 PDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLV-ADGGRHSTILIDQGTADQFLdEQLRPDAFEQAC 238

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 691055762  240 LKAGQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQL 276
Cdd:TIGR02821 239 RAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 6-278 2.79e-116

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 335.59  E-value: 2.79e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762   6 KNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGKpCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDTSPR 85
Cdd:PLN02442  10 VNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGK-VPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  86 GGQV-AVGDNWDLGQGAGFYINATEAPWsEHYQMESYLIDELYPLILKSFP-VNAQQVGIFGHSMGGHGALTLAFKYPEK 163
Cdd:PLN02442  89 GLNVeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYLKNPDK 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 164 FKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVSKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQACLKA 242
Cdd:PLN02442 168 YKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLkEQLLPENFEEACKEA 247

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 691055762 243 GQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQLEK 278
Cdd:PLN02442 248 GAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALKS 283
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
12-276 1.80e-96

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 283.65  E-value: 1.80e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  12 GEQRIYQFDSQLLKGSTKFGVYLPPAAlEGKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDtsprGGQvav 91
Cdd:COG0627    2 GRVVRVTVPSPALGREMPVSVYLPPGY-DGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----GGQ--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  92 gdnwdlgqgAGFYINATEAPwSEHYQMESYLIDELYPLILKSFPVNAQ--QVGIFGHSMGGHGALTLAFKYPEKFKSVSA 169
Cdd:COG0627   74 ---------ASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSADreRRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 170 FAPICAPTECAWGEKAFSHYLGT-DRDSWLAHDATALVSKNGAVFnEILVDQGLDDQ-FYEQVHpeKFKQACLKAGQPLT 247
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRAGL-PLYIDCGTADPfFLEANR--QLHAALRAAGIPHT 220

                        250       260
                 ....*....|....*....|....*....
gi 691055762 248 LRQHAGYdHGYYFIQTFMDEHLQFHAIQL 276
Cdd:COG0627  221 YRERPGG-HSWYYWASFLEDHLPFLARAL 248
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 21-271 7.74e-50

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: 164.94  E-value: 7.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762   21 SQLLKGSTKFGVYLPPAALEGKPCSTLFYLAGlTCTEETFAIKAHAQHMAAQLSLILITPDTSPRGGQVAVGDNWDLGQg 100
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRGL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  101 agfyiNATEAPWSEHYqmESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAPTECA 180
Cdd:pfam00756  79 -----NATEGPGAYAY--ETFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  181 WGEkafshylgTDRDSWLAHDATALVsKNGAVFNE---ILVDQGLDDQFY-EQVHPEKFKQACLKAGQP--LTLRQHAGY 254
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLA-VALSANNTrlrIYLDVGTREDFLgDQLPVEILEELAPNRELAeqLAYRGVGGY 222

                         250       260
                  ....*....|....*....|....
gi 691055762  255 DHGY-------YFIQTFMDEHLQF 271
Cdd:pfam00756 223 DHEYygghdwaYWRAQLIAALIDL 246
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
12-271 2.33e-20

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 88.76  E-value: 2.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  12 GEQRIYQFDSQLLKGSTKFGVYLPPAALE-GKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQL-------SLILITPDTS 83
Cdd:COG2382   79 GTVETVTYPSKALGRTRRVWVYLPPGYDNpGKKYPVLYLLDGGGGDEQDWFDQGRLPTILDNLiaagkipPMIVVMPDGG 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  84 PRGGqvavgDNWDLGQGAGFyinateapwsehyqmESYLIDELYPLILKSFPV--NAQQVGIFGHSMGGHGALTLAFKYP 161
Cdd:COG2382  159 DGGD-----RGTEGPGNDAF---------------ERFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALRHP 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 162 EKFKSVSAFAPICAPTEcawgekafshyLGTDRDSWLAHDATALVSKNGAVFneilVDQGLDDQFYEQVhpEKFKQACLK 241
Cdd:COG2382  219 DLFGYVGSFSGSFWWPP-----------GDADRGGWAELLAAGAPKKPLRFY----LDVGTEDDLLEAN--RALAAALKA 281

                        250       260       270
                 ....*....|....*....|....*....|
gi 691055762 242 AGQPLTLRQHAGyDHGYYFIQTFMDEHLQF 271
Cdd:COG2382  282 KGYDVEYREFPG-GHDWAVWRAALPDFLPW 310
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
136-270 2.92e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 58.87  E-value: 2.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 136 VNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAPTECAWGEKAFS-HYLGT---DRDSWLAHDATALVSK-NG 210
Cdd:COG1506   90 VDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTeRLMGGpweDPEAYAARSPLAYADKlKT 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 691055762 211 AVfneiLVDQGLDDqfyEQVHP---EKFKQACLKAGQPLTLRQHAGYDHGYYF---------IQTFMDEHLQ 270
Cdd:COG1506  170 PL----LLIHGEAD---DRVPPeqaERLYEALKKAGKPVELLVYPGEGHGFSGagapdylerILDFLDRHLK 234
COG4099 COG4099
Predicted peptidase [General function prediction only];
92-175 3.36e-09

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 55.74  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  92 GDNWD--LGQGAGFYINATE---------AP-------WSEHYQMEsyLIDELYPLILKSFPVNAQQVGIFGHSMGGHGA 153
Cdd:COG4099   62 GTDNEkqLTHGAPKFINPENqakfpaivlAPqcpeddyWSDTKALD--AVLALLDDLIAEYRIDPDRIYLTGLSMGGYGT 139

                         90       100
                 ....*....|....*....|..
gi 691055762 154 LTLAFKYPEKFksvSAFAPICA 175
Cdd:COG4099  140 WDLAARYPDLF---AAAVPICG 158
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
121-172 1.78e-08

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 53.84  E-value: 1.78e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 691055762 121 YLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAP 172
Cdd:COG2819  112 FLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 32-182 4.61e-06

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 46.92  E-value: 4.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  32 VYLPPAALEGKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDTSPRGGQ----VAVGDNWDLGQG-AGFyIN 106
Cdd:COG3509   41 LYVPAGYDGGAPLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPGrcwnWFDGRDQRRGRDdVAF-IA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 107 AteapwsehyqmesyLIDELypliLKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFA---PICAPTE-CAWG 182
Cdd:COG3509  120 A--------------LVDDL----AARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglpYGAASDAaCAPG 181
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
120-157 2.04e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 42.02  E-value: 2.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 691055762 120 SYLIDELYPLILKSFP----VNAQQVGIFGHSMGGHGALTLA 157
Cdd:COG4188  129 SFVLDQLLALNKSDPPlagrLDLDRIGVIGHSLGGYTALALA 170
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 143-176 1.29e-03

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: 39.51  E-value: 1.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 691055762  143 IFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAP 176
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILSAPALKI 113
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
131-180 1.44e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.18  E-value: 1.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 691055762 131 LKSFP-VNAQQVGIFGHSMGGHGALTLAFKYPEkFKSVSAFAPICAPTECA 180
Cdd:COG0412  100 LKAQPeVDAGRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGGLPADDLL 149
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
121-270 1.71e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 38.75  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  121 YLIDELYplilksfpVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPIC------APTECAWGEKAFSHylGTDR 194
Cdd:pfam00326  54 YLIEQGY--------TDPDRLAIWGGSYGGYLTGAALNQRPDLFKAAVAHVPVVdwlaymSDTSLPFTERYMEW--GNPW 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762  195 DSWLAHDATALVS--KNGAVFNEILVDQGLDDqfyEQVHP---EKFKQACLKAGQPLTLRQHAGYDHGYY---------- 259
Cdd:pfam00326 124 DNEEGYDYLSPYSpaDNVKVYPPLLLIHGLLD---DRVPPwqsLKLVAALQRKGVPFLLLIFPDEGHGIGkprnkveeya 200

                         170
                  ....*....|.
gi 691055762  260 FIQTFMDEHLQ 270
Cdd:pfam00326 201 RELAFLLEYLG 211
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 113-167 5.28e-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: 37.29  E-value: 5.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 691055762 113 SEHYQMESY------LIDELyplilksfpvNAQQVGIFGHSMGGHGALTLAFKYPEKFKSV 167
Cdd:COG0596   67 AGGYTLDDLaddlaaLLDAL----------GLERVVLVGHSMGGMVALELAARHPERVAGL 117
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
132-259 5.64e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 37.16  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 132 KSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKS-VSAFAPICAPTecawgekafshylgTDRDSWLAHDATALVSkng 210
Cdd:COG0657   79 AELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPrPAAQVLIYPVL--------------DLTASPLRADLAGLPP--- 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 691055762 211 avfneILVDQGLDDQFYEQVhpEKFKQACLKAGQPLTLRQHAGYDHGYY 259
Cdd:COG0657  142 -----TLIVTGEADPLVDES--EALAAALRAAGVPVELHVYPGGGHGFG 183
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 145-172 9.66e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 37.23  E-value: 9.66e-03
                         10        20
                 ....*....|....*....|....*...
gi 691055762 145 GHSMGGHGALTLAFKYPEKFKSVSAFAP 172
Cdd:PRK14875 203 GHSMGGAVALRLAARAPQRVASLTLIAP 230
 
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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