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Conserved domains on  [gi|577651356|gb|EUI62760|]
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alpha/beta hydrolase [Staphylococcus aureus M1184]

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, ...
 10-261 1.92e-44

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: 149.38  E-value: 1.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  10 IQLTYQIEG-KGDPIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSES-YDLNDHVEDLKILMEKLNIHEA 87
Cdd:COG0596   12 VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  88 HILGHDLGGVVAKLFTDKYAYRVKSLTTIaskkDDLIHSFTQLLIQYQDDIAGFnkseayillfsklfrnqektmkwyqk 167
Cdd:COG0596   92 VLVGHSMGGMVALELAARHPERVAGLVLV----DEVLAALAEPLRRPGLAPEAL-------------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 168 qriysikseddsaVAIRSLILHKDEPMYLKKRTCvPTLLINGEHDPLIKDKNHFKLEAHFLNVTKKIFEHSGHAPHIEEP 247
Cdd:COG0596  142 -------------AALLRALARTDLRERLARITV-PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207

                        250
                 ....*....|....
gi 577651356 248 EAFMNYYLNFLKSV 261
Cdd:COG0596  208 EAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 10-261 1.92e-44

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: 149.38  E-value: 1.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  10 IQLTYQIEG-KGDPIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSES-YDLNDHVEDLKILMEKLNIHEA 87
Cdd:COG0596   12 VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  88 HILGHDLGGVVAKLFTDKYAYRVKSLTTIaskkDDLIHSFTQLLIQYQDDIAGFnkseayillfsklfrnqektmkwyqk 167
Cdd:COG0596   92 VLVGHSMGGMVALELAARHPERVAGLVLV----DEVLAALAEPLRRPGLAPEAL-------------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 168 qriysikseddsaVAIRSLILHKDEPMYLKKRTCvPTLLINGEHDPLIKDKNHFKLEAHFLNVTKKIFEHSGHAPHIEEP 247
Cdd:COG0596  142 -------------AALLRALARTDLRERLARITV-PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207

                        250
                 ....*....|....
gi 577651356 248 EAFMNYYLNFLKSV 261
Cdd:COG0596  208 EAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-247 6.67e-30

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: 112.21  E-value: 6.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   21 DPIILLHGLDGNLAGFEDLQHQLASS-YKVLTYDLRGHGKSSKS---ESYDLNDHVEDLKILMEKLNIHEAHILGHDLGG 96
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   97 VVAKLFTDKYAYRVKSLTTIASKKDDLIHSFTQLLI----------QYQDDIA-----GFNKSEAYILLFSKLFRNQEKT 161
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFIlalfpgffdgFVADFAPnplgrLVAKLLALLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  162 MKWYQKQRIYSIKSEDDSAVAIRSLILHKDePMYLKKRTCVPTLLINGEHDPLIKDKNHFKLEAHFLNVTKKIFEHSGHA 241
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLFIETWSTEL-RAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHF 239


                  ....*.
gi 577651356  242 PHIEEP 247
Cdd:pfam00561 240 AFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 22-259 3.08e-19

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 84.19  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   22 PIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSESYDLND----HVEDLKILMEKLNIHEAHILGHDLGGV 97
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDfeeaAQLLLATLLDQLGIEPFFLVGYSMGGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   98 VAKLFTDKYAYRVKS---------LTTIASKKDDLIHSftQLLIQY--QDDIAGFNKSEAYILLFSKLFR-NQEktmkwy 165
Cdd:TIGR03695  84 IALYYALQYPERVQGlilesgspgLQTEEERAARRQND--EQLAQRfeQEGLEAFLDDWYQQPLFASQKNlPPE------ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  166 QKQRIYSIKSEDDS---AVAIRSLILHKdEPMYLKK--RTCVPTLLINGEhdpliKDKNHFKL----EAHFLNVTKKIFE 236
Cdd:TIGR03695 156 QRQALRAERLANNPeglAKMLRATGLGK-QPSLWPKlqALKIPVLYLCGE-----RDEKFVQIakemQKLIPNLTLHIIP 229

                         250       260
                  ....*....|....*....|...
gi 577651356  237 HSGHAPHIEEPEAFMNYYLNFLK 259
Cdd:TIGR03695 230 NAGHNIHLENPEAFAKILLAFLE 252
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 17-250 1.28e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 78.45  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  17 EGKGDPIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKS-ESYDLNDHVEDLKILMEKLNIHEAHILGHDLG 95
Cdd:PRK14875 128 EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAvGAGSLDELAAAVLAFLDALGIERAHLVGHSMG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  96 GVVAKLFTDKYAYRVKSLTTIASK------KDDLIHSFtqlliqyqddiAGFNKSEAYILLFSKLFRNQEKTmkwyQKQR 169
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAglgpeiNGDYIDGF-----------VAAESRRELKPVLELLFADPALV----TRQM 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 170 IYSI---KSEDDSAVAIRSLILH-------KDEPMYLKKRTCVPTLLINGEHDPLIKDKNHFKLEAhflNVTKKIFEHSG 239
Cdd:PRK14875 273 VEDLlkyKRLDGVDDALRALADAlfaggrqRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPD---GVAVHVLPGAG 349

                        250
                 ....*....|.
gi 577651356 240 HAPHIEEPEAF 250
Cdd:PRK14875 350 HMPQMEAAADV 360
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 10-261 1.92e-44

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: 149.38  E-value: 1.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  10 IQLTYQIEG-KGDPIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSES-YDLNDHVEDLKILMEKLNIHEA 87
Cdd:COG0596   12 VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  88 HILGHDLGGVVAKLFTDKYAYRVKSLTTIaskkDDLIHSFTQLLIQYQDDIAGFnkseayillfsklfrnqektmkwyqk 167
Cdd:COG0596   92 VLVGHSMGGMVALELAARHPERVAGLVLV----DEVLAALAEPLRRPGLAPEAL-------------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 168 qriysikseddsaVAIRSLILHKDEPMYLKKRTCvPTLLINGEHDPLIKDKNHFKLEAHFLNVTKKIFEHSGHAPHIEEP 247
Cdd:COG0596  142 -------------AALLRALARTDLRERLARITV-PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207

                        250
                 ....*....|....
gi 577651356 248 EAFMNYYLNFLKSV 261
Cdd:COG0596  208 EAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-247 6.67e-30

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: 112.21  E-value: 6.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   21 DPIILLHGLDGNLAGFEDLQHQLASS-YKVLTYDLRGHGKSSKS---ESYDLNDHVEDLKILMEKLNIHEAHILGHDLGG 96
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   97 VVAKLFTDKYAYRVKSLTTIASKKDDLIHSFTQLLI----------QYQDDIA-----GFNKSEAYILLFSKLFRNQEKT 161
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFIlalfpgffdgFVADFAPnplgrLVAKLLALLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  162 MKWYQKQRIYSIKSEDDSAVAIRSLILHKDePMYLKKRTCVPTLLINGEHDPLIKDKNHFKLEAHFLNVTKKIFEHSGHA 241
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLFIETWSTEL-RAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHF 239


                  ....*.
gi 577651356  242 PHIEEP 247
Cdd:pfam00561 240 AFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 22-259 3.08e-19

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 84.19  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   22 PIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSESYDLND----HVEDLKILMEKLNIHEAHILGHDLGGV 97
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDfeeaAQLLLATLLDQLGIEPFFLVGYSMGGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   98 VAKLFTDKYAYRVKS---------LTTIASKKDDLIHSftQLLIQY--QDDIAGFNKSEAYILLFSKLFR-NQEktmkwy 165
Cdd:TIGR03695  84 IALYYALQYPERVQGlilesgspgLQTEEERAARRQND--EQLAQRfeQEGLEAFLDDWYQQPLFASQKNlPPE------ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  166 QKQRIYSIKSEDDS---AVAIRSLILHKdEPMYLKK--RTCVPTLLINGEhdpliKDKNHFKL----EAHFLNVTKKIFE 236
Cdd:TIGR03695 156 QRQALRAERLANNPeglAKMLRATGLGK-QPSLWPKlqALKIPVLYLCGE-----RDEKFVQIakemQKLIPNLTLHIIP 229

                         250       260
                  ....*....|....*....|...
gi 577651356  237 HSGHAPHIEEPEAFMNYYLNFLK 259
Cdd:TIGR03695 230 NAGHNIHLENPEAFAKILLAFLE 252
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 17-250 1.28e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 78.45  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  17 EGKGDPIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKS-ESYDLNDHVEDLKILMEKLNIHEAHILGHDLG 95
Cdd:PRK14875 128 EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAvGAGSLDELAAAVLAFLDALGIERAHLVGHSMG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  96 GVVAKLFTDKYAYRVKSLTTIASK------KDDLIHSFtqlliqyqddiAGFNKSEAYILLFSKLFRNQEKTmkwyQKQR 169
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAglgpeiNGDYIDGF-----------VAAESRRELKPVLELLFADPALV----TRQM 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 170 IYSI---KSEDDSAVAIRSLILH-------KDEPMYLKKRTCVPTLLINGEHDPLIKDKNHFKLEAhflNVTKKIFEHSG 239
Cdd:PRK14875 273 VEDLlkyKRLDGVDDALRALADAlfaggrqRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPD---GVAVHVLPGAG 349

                        250
                 ....*....|.
gi 577651356 240 HAPHIEEPEAF 250
Cdd:PRK14875 350 HMPQMEAAADV 360
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
22-260 4.98e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 74.65  E-value: 4.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  22 PIILLHGLDGNLAGFEDLQHQLASS-YKVLTYDLRGHGKSSKSESY--DLNDHVEDLKILMEKLNIHEA---HILGHDLG 95
Cdd:COG2267   30 TVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLRAALDALRARPGlpvVLLGHSMG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  96 GVVAKLFTDKYAYRVKSLTTIASK--KDDLIHSftqlliqyqddiagfnkseayillfsklfrnqekTMKWYQKQRIYsi 173
Cdd:COG2267  110 GLIALLYAARYPDRVAGLVLLAPAyrADPLLGP----------------------------------SARWLRALRLA-- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 174 ksedDSAVAIRslilhkdepmylkkrtcVPTLLINGEHDPLIKDKNHFKLEAHFL-NVTKKIFEHSGHAPHIEEP-EAFM 251
Cdd:COG2267  154 ----EALARID-----------------VPVLVLHGGADRVVPPEAARRLAARLSpDVELVLLPGARHELLNEPArEEVL 212


                 ....*....
gi 577651356 252 NYYLNFLKS 260
Cdd:COG2267  213 AAILAWLER 221
PRK10673 PRK10673
esterase;
22-116 1.92e-13

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 68.22  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  22 PIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSESYDLNDHVEDLKILMEKLNIHEAHILGHDLGGVVAKL 101
Cdd:PRK10673  18 PIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMA 97

                         90
                 ....*....|....*
gi 577651356 102 FTDKYAYRVKSLTTI 116
Cdd:PRK10673  98 LTALAPDRIDKLVAI 112
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 23-250 2.44e-13

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 67.11  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   23 IILLHGLDgnlAGFEDLQHQLASSYKVLTYDLRGHGKSSkSESYDLNDhVEDLKILMEKL-NIHEAHILGHDLGGVVAkL 101
Cdd:pfam12697   1 VVLVHGAG---LSAAPLAALLAAGVAVLAPDLPGHGSSS-PPPLDLAD-LADLAALLDELgAARPVVLVGHSLGGAVA-L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  102 FTDKYAYRVKSLTTIASKKDDLIHSFTQLLIQYQDDIA--GFNKSEAYILLFSKLFRNQEKTMKWYQKQRIYSIKSEDDS 179
Cdd:pfam12697  75 AAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAapAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALLP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577651356  180 AVAIRSLIlhkdepmylkkrtcvPTLLINGEHDPLIKDKNHfKLEAHFLNVTKKIFEHSGHAPHiEEPEAF 250
Cdd:pfam12697 155 LAAWRDLP---------------VPVLVLAEEDRLVPELAQ-RLLAALAGARLVVLPGAGHLPL-DDPEEV 208
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 23-245 2.57e-12

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: 64.54  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   23 IILLHGLDGNLAGFEDLQHQLA-SSYKVLTYDLRGHGKSS--KSESYDLNDHVEDLKILMEKlnIHEAH------ILGHD 93
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAaQGFAVYAYDHRGHGRSDgkRGHVPSFDDYVDDLDTFVDK--IREEHpglplfLLGHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   94 LGGVVAKLFTDKYAYRVKSLttIAS-----KKDDLIHSFTQLLIQYQDDIAGfNKSEAYILLFSKLFRNQEKtMKWYQK- 167
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGL--ILSapalkIKPYLAPPILKLLAKLLGKLFP-RLRVPNNLLPDSLSRDPEV-VAAYAAd 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  168 -QRIYSIkseddSAVAIRSLILHKdepMYLKKRT---CVPTLLINGEHDPLIKDKNHFKL--EAHFLNVTKKIFEHSGHA 241
Cdd:pfam12146 161 pLVHGGI-----SARTLYELLDAG---ERLLRRAaaiTVPLLLLHGGADRVVDPAGSREFyeRAGSTDKTLKLYPGLYHE 232


                  ....
gi 577651356  242 PHIE 245
Cdd:pfam12146 233 LLNE 236
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
23-262 3.48e-11

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 61.50  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  23 IILLHGLDGNLAGFEDLQHQLASS-YKVLTYDLRGHGKSSKS-ESYDLNDHVEDLKILMEKL-NIHEA-HILGHDLGGVV 98
Cdd:COG1647   18 VLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEDlLKTTWEDWLEDVEEAYEILkAGYDKvIVIGLSMGGLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  99 AkLftdKYAYR---VKSLTTIAS--KKDDLIHSFTQLLIQYQDDIAGFNKSeayillfsklFRNQEKTMKWYQKQRIysi 173
Cdd:COG1647   98 A-L---LLAARypdVAGLVLLSPalKIDDPSAPLLPLLKYLARSLRGIGSD----------IEDPEVAEYAYDRTPL--- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 174 ksedDSAVAIRSLIlhKDEPMYLKKRTCvPTLLINGEHDPLIKDKNHFKLEAHF--LNVTKKIFEHSGH-APHIEEPEAF 250
Cdd:COG1647  161 ----RALAELQRLI--REVRRDLPKITA-PTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHvITLDKDREEV 233

                        250
                 ....*....|..
gi 577651356 251 MNYYLNFLKSVS 262
Cdd:COG1647  234 AEEILDFLERLA 245
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 18-257 8.58e-11

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 60.60  E-value: 8.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   18 GKGDP-IILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSESYDLNDHVEDLKILMEKlnihEAHILGHDLGG 96
Cdd:TIGR01738   1 GQGNVhLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPD----PAIWLGWSLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   97 VVAKLFTDKYAYRVKSLTTIASK-------------KDDLIHSFTQLLIQ-YQDDIAGFnksEAYILLFSKLFRNQEKTM 162
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTVASSpcfsaredwpegiKPDVLTGFQQQLSDdYQRTIERF---LALQTLGTPTARQDARAL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  163 kwyqKQRIYSIKS-EDDSAVAIRSLILHKDEPMYLKKRTcVPTLLINGEHDPLIKDKNhfkleAHFLNVTKK-----IFE 236
Cdd:TIGR01738 154 ----KQTLLARPTpNVQVLQAGLEILATVDLRQPLQNIS-VPFLRLYGYLDGLVPAKV-----VPMLDKLAPhselyIFA 223

                         250       260
                  ....*....|....*....|.
gi 577651356  237 HSGHAPHIEEPEAFMNYYLNF 257
Cdd:TIGR01738 224 KAAHAPFLSHAEAFCALLVAF 244
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 21-118 5.06e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 52.52  E-value: 5.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  21 DPIILLHGLDGNLAGFEDLQHQLASS-YKVLTYDLRGHGKSSKSESYDLNDHVEDlkiLMEKLNIHEAHILGHDLGGVVA 99
Cdd:COG1075    6 YPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSAEQLAAFVDA---VLAATGAEKVDLVGHSMGGLVA 82

                         90       100
                 ....*....|....*....|.
gi 577651356 100 KLF--TDKYAYRVKSLTTIAS 118
Cdd:COG1075   83 RYYlkRLGGAAKVARVVTLGT 103
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
14-261 6.40e-08

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 52.33  E-value: 6.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  14 YQIEGKGD-PIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSESYDLndhvEDLKILMEKLNIHEAHILGH 92
Cdd:PRK10349   6 WQTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSL----ADMAEAVLQQAPDKAIWLGW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  93 DLGGVVAKLFTDKYAYRVKSLTTIASK------------KDDLIHSFTQlliQYQDDiagFNKSEAYILLFSKLFRNQEK 160
Cdd:PRK10349  82 SLGGLVASQIALTHPERVQALVTVASSpcfsardewpgiKPDVLAGFQQ---QLSDD---FQRTVERFLALQTMGTETAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 161 TMKWYQKQRIYSIKSEDDSAVAIRSLILHKDEPMYLKKRTCVPTLLINGEHDPLIKDKNHFKLEAHFLNVTKKIFEHSGH 240
Cdd:PRK10349 156 QDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAH 235

                        250       260
                 ....*....|....*....|.
gi 577651356 241 APHIEEPEAFMNYYLNFLKSV 261
Cdd:PRK10349 236 APFISHPAEFCHLLVALKQRV 256
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 36-117 2.98e-07

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 50.96  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  36 FEDLQHQLASSYKVLTYDLRGHGKSSK-SES-YDLNDHVEDL-KILMEKLNIHEAHILGHDLGGVVAKLFTDKYAYRVKS 112
Cdd:PLN03087 222 FPNFSDAAKSTYRLFAVDLLGFGRSPKpADSlYTLREHLEMIeRSVLERYKVKSFHIVAHSLGCILALALAVKHPGAVKS 301


                 ....*
gi 577651356 113 LTTIA 117
Cdd:PLN03087 302 LTLLA 306
PRK05855 PRK05855
SDR family oxidoreductase;
20-116 1.05e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 49.21  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  20 GDP----IILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSK---SESYDLNDHVEDLKILMEKLNIHEA-HILG 91
Cdd:PRK05855  21 GDPdrptVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSApkrTAAYTLARLADDFAAVIDAVSPDRPvHLLA 100

                         90       100
                 ....*....|....*....|....*..
gi 577651356  92 HDLGGVVA-KLFTDKYAY-RVKSLTTI 116
Cdd:PRK05855 101 HDWGSIQGwEAVTRPRAAgRIASFTSV 127
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 11-99 2.36e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 47.68  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  11 QLTYQIEGKGDPIILLHG------LDGN-LAGFEDLQHQLASsykvltyDLRGHGKSSKSE-SYDLNDHVEDLKILMEKL 82
Cdd:PRK03592  18 RMAYIETGEGDPIVFLHGnptssyLWRNiIPHLAGLGRCLAP-------DLIGMGASDKPDiDYTFADHARYLDAWFDAL 90

                         90
                 ....*....|....*..
gi 577651356  83 NIHEAHILGHDLGGVVA 99
Cdd:PRK03592  91 GLDDVVLVGHDWGSALG 107
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
22-118 9.18e-06

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 46.03  E-value: 9.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  22 PIILLHGLDGNLAGF-EDLQHQLASS-YKVLTYDLRGHGKS----SKSESYDLNDHVE-DLKILMEKLNIHEA----HIL 90
Cdd:COG4757   33 AVVLINPATGVPQRFyRPFARYLAERgFAVLTYDYRGIGLSrpgsLRGFDAGYRDWGElDLPAVLDALRARFPglplLLV 112

                         90       100
                 ....*....|....*....|....*...
gi 577651356  91 GHDLGGVVAKLFTDkyAYRVKSLTTIAS 118
Cdd:COG4757  113 GHSLGGQLLGLAPN--AERVDRLVTVAS 138
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
23-259 9.99e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.39  E-value: 9.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  23 IILLHGLDGN-LAGFEDLQHQLASS-YKVLTYDLRGHGKSSKS-ESYDLNDHVEDLKILMEKLNIHEAHI--LGHDLGGV 97
Cdd:COG1506   26 VVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDwGGDEVDDVLAAIDYLAARPYVDPDRIgiYGHSYGGY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  98 VAklftdkyayrvkslTTIASKKDDLIHSftqlLIqyqdDIAGFNKseayillfsklFRNQEKTMKWYqKQRIYSIKSED 177
Cdd:COG1506  106 MA--------------LLAAARHPDRFKA----AV----ALAGVSD-----------LRSYYGTTREY-TERLMGGPWED 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 178 DSAVAIRSLIlhkdepMYLKKRTCvPTLLINGEHDPLIKDKN----HFKLEAHFLNVTKKIFEHSGHAPHIEEPEAFMNY 253
Cdd:COG1506  152 PEAYAARSPL------AYADKLKT-PLLLIHGEADDRVPPEQaerlYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLER 224


                 ....*.
gi 577651356 254 YLNFLK 259
Cdd:COG1506  225 ILDFLD 230
PLN02578 PLN02578
hydrolase
 14-260 7.88e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 43.29  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  14 YQIEGKGDPIILLHGLDGNLAGFEDLQHQLASSYKVLTYDLRGHGKSSKSE-SYD---LNDHVEDlkiLMEKLNIHEAHI 89
Cdd:PLN02578  80 YVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALiEYDamvWRDQVAD---FVKEVVKEPAVL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  90 LGHDLGGVVAKLFTDKYAYRVKSLT---------TIASKKDDLIHS----FTQLLIQYQDDIAgfnksEAYILLFskLFr 156
Cdd:PLN02578 157 VGNSLGGFTALSTAVGYPELVAGVAllnsagqfgSESREKEEAIVVeetvLTRFVVKPLKEWF-----QRVVLGF--LF- 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356 157 nqektmkWYQKQ--RIYSI-KS--EDDSAV---AIRSLILHKDEP----MY-------------------LKKRTCvPTL 205
Cdd:PLN02578 229 -------WQAKQpsRIESVlKSvyKDKSNVddyLVESITEPAADPnageVYyrlmsrflfnqsrytldslLSKLSC-PLL 300

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 577651356 206 LINGEHDPLIKDKNHFKLEAhFLNVTKKIFEHSGHAPHIEEPEAFMNYYLNFLKS 260
Cdd:PLN02578 301 LLWGDLDPWVGPAKAEKIKA-FYPDTTLVNLQAGHCPHDEVPEQVNKALLEWLSS 354
PRK06489 PRK06489
hypothetical protein; Provisional
 20-106 1.19e-03

hypothetical protein; Provisional


Pssm-ID: 235815 [Multi-domain]  Cd Length: 360  Bit Score: 39.58  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  20 GDPIILLHGLDGNLAGF--EDLQHQL--------ASSYKVLTYDLRGHGKSSK-SES-------YDLNDHVE-DLKILME 80
Cdd:PRK06489  69 DNAVLVLHGTGGSGKSFlsPTFAGELfgpgqpldASKYFIILPDGIGHGKSSKpSDGlraafprYDYDDMVEaQYRLVTE 148

                         90       100
                 ....*....|....*....|....*..
gi 577651356  81 KLNI-HEAHILGHDLGGVVAKLFTDKY 106
Cdd:PRK06489 149 GLGVkHLRLILGTSMGGMHAWMWGEKY 175
COG4814 COG4814
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];
1-147 1.86e-03

Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];


Pssm-ID: 443842  Cd Length: 286  Bit Score: 38.77  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356   1 MNKVTINPQIQLTYQIEgkgdPIILLHGLDGNLAGFEDLQHQLASSY----KVLTYDLRGHGKSSKSESYDLNDH----- 71
Cdd:COG4814   28 TKSTVKSLKSKYNSKQT----PTIFIHGSGGTANSFNTMINRLNEKYgvghKVLTVTVSKDGKITYSGKIRKNAKnpiiq 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577651356  72 --VED-----------LKILMEKL----NIHEAHILGHDLGGVVAKLFTDKYAY-----RVKSLTTIASKKDDLIHSFTQ 129
Cdd:COG4814  104 vgFEDnrdsikkqakwLKKVLKYLkkkyGFKKFNAVGHSMGGLALTYYLEKYGNdkslpKLNKLVTIGGPFNGIENEDNN 183

                        170
                 ....*....|....*...
gi 577651356 130 LLIQYQDDIAGFNKSEAY 147
Cdd:COG4814  184 NLTDLLADGKPKPKTQAY 201
 
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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