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Conserved domains on  [gi|489192988|ref|WP_003102328|]
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MULTISPECIES: alpha/beta fold hydrolase [Pseudomonas]

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, ...
 18-292 2.52e-30

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: 113.94  E-value: 2.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  18 RTLDFKGFPIRYWEAG-QGRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRAHrYSLLEQADLQQALL 96
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGG-YTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  97 GRLGIdEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFLNGglfpethrpvlsqklllsplgglfgrlfDRRALARNF 176
Cdd:COG0596   84 DALGL-ERVVLVGHSMGGMVALELAARHPE---RVAGLVLVDE----------------------------VLAALAEPL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 177 AkvfgprsqpgeteldafwsliESNQGQRVMHRLIRYIvdRREQRERWVAALQhggVPLRVIDGAVDPISGAHMVERYRQ 256
Cdd:COG0596  132 R---------------------RPGLAPEALAALLRAL--ARTDLRERLARIT---VPTLVIWGEKDPIVPPALARRLAE 185

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489192988 257 LVADADCVLLDGIGHYPQIEAPAAVLEHYLAFRARL 292
Cdd:COG0596  186 LLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 18-292 2.52e-30

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: 113.94  E-value: 2.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  18 RTLDFKGFPIRYWEAG-QGRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRAHrYSLLEQADLQQALL 96
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGG-YTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  97 GRLGIdEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFLNGglfpethrpvlsqklllsplgglfgrlfDRRALARNF 176
Cdd:COG0596   84 DALGL-ERVVLVGHSMGGMVALELAARHPE---RVAGLVLVDE----------------------------VLAALAEPL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 177 AkvfgprsqpgeteldafwsliESNQGQRVMHRLIRYIvdRREQRERWVAALQhggVPLRVIDGAVDPISGAHMVERYRQ 256
Cdd:COG0596  132 R---------------------RPGLAPEALAALLRAL--ARTDLRERLARIT---VPTLVIWGEKDPIVPPALARRLAE 185

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489192988 257 LVADADCVLLDGIGHYPQIEAPAAVLEHYLAFRARL 292
Cdd:COG0596  186 LLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 37-278 6.39e-19

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 83.71  E-value: 6.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988   37 PLLLIHGFPSAAWDWHYLWEPLA-QRYRVLVCDLLGFGDSAKPRA-HRYSLLEQADLQQALLGRLGIDePLHVLAHDYGD 114
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAqDDYRTDDLAEDLEYILEALGLE-KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  115 SVAQELLARHHEgrlRLASCVFLNGGLFPETHRPVLSQKLLLSPLG-----GLFGRLFDRRALARNFAKVFGPRSQPGET 189
Cdd:pfam00561  81 LIALAYAAKYPD---RVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLALLLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  190 ELDA------FWSLIESNQGQRVMHRLIRYIVDRReqrerwvAALQHGGVPLRVIDGAVDPISGAHMVERYRQLVADADC 263
Cdd:pfam00561 158 PLLNkrfpsgDYALAKSLVTGALLFIETWSTELRA-------KFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARL 230

                         250
                  ....*....|....*
gi 489192988  264 VLLDGIGHYPQIEAP 278
Cdd:pfam00561 231 VVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 1-291 3.38e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 77.68  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988   1 MTAALPGIPLEAWRRRGRTLDFKGFPIRYWEAGQ--GRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKp 78
Cdd:PRK14875  95 RRFAPEGIDEEDAGPAPRKARIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSK- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  79 RAHRYSLLEQADLQQALLGRLGIdEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFL-NGGLFPETHRPVLSQkllls 157
Cdd:PRK14875 174 AVGAGSLDELAAAVLAFLDALGI-ERAHLVGHSMGGAVALRLAARAPQ---RVASLTLIaPAGLGPEINGDYIDG----- 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 158 plgglFGRLFDRRALARNFAKVFGPRSQPGETELDAFWSLIESNQGQRVMHRLIRYIVDRREQRERWVAALQHGGVPLRV 237
Cdd:PRK14875 245 -----FVAAESRRELKPVLELLFADPALVTRQMVEDLLKYKRLDGVDDALRALADALFAGGRQRVDLRDRLASLAIPVLV 319

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489192988 238 IDGAVDPI-SGAHMveryRQLVADADCVLLDGIGHYPQIEAPAAVLEHYLAFRAR 291
Cdd:PRK14875 320 IWGEQDRIiPAAHA----QGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 35-159 9.58e-08

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: 51.83  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988   35 GRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRA-HRYSLLEQA-DLQQALLGRLGIdEPLHVLAHDY 112
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDiERYDFEEAAqLLLATLLDQLGI-EPFFLVGYSM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489192988  113 GDSVAQELLARHHEG--RLRLASCvflNGGLFPETHRPV-------LSQKLLLSPL 159
Cdd:TIGR03695  81 GGRIALYYALQYPERvqGLILESG---SPGLQTEEERAArrqndeqLAQRFEQEGL 133
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 18-292 2.52e-30

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: 113.94  E-value: 2.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  18 RTLDFKGFPIRYWEAG-QGRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRAHrYSLLEQADLQQALL 96
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGG-YTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  97 GRLGIdEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFLNGglfpethrpvlsqklllsplgglfgrlfDRRALARNF 176
Cdd:COG0596   84 DALGL-ERVVLVGHSMGGMVALELAARHPE---RVAGLVLVDE----------------------------VLAALAEPL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 177 AkvfgprsqpgeteldafwsliESNQGQRVMHRLIRYIvdRREQRERWVAALQhggVPLRVIDGAVDPISGAHMVERYRQ 256
Cdd:COG0596  132 R---------------------RPGLAPEALAALLRAL--ARTDLRERLARIT---VPTLVIWGEKDPIVPPALARRLAE 185

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489192988 257 LVADADCVLLDGIGHYPQIEAPAAVLEHYLAFRARL 292
Cdd:COG0596  186 LLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 37-278 6.39e-19

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 83.71  E-value: 6.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988   37 PLLLIHGFPSAAWDWHYLWEPLA-QRYRVLVCDLLGFGDSAKPRA-HRYSLLEQADLQQALLGRLGIDePLHVLAHDYGD 114
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAqDDYRTDDLAEDLEYILEALGLE-KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  115 SVAQELLARHHEgrlRLASCVFLNGGLFPETHRPVLSQKLLLSPLG-----GLFGRLFDRRALARNFAKVFGPRSQPGET 189
Cdd:pfam00561  81 LIALAYAAKYPD---RVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLALLLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  190 ELDA------FWSLIESNQGQRVMHRLIRYIVDRReqrerwvAALQHGGVPLRVIDGAVDPISGAHMVERYRQLVADADC 263
Cdd:pfam00561 158 PLLNkrfpsgDYALAKSLVTGALLFIETWSTELRA-------KFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARL 230

                         250
                  ....*....|....*
gi 489192988  264 VLLDGIGHYPQIEAP 278
Cdd:pfam00561 231 VVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 1-291 3.38e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 77.68  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988   1 MTAALPGIPLEAWRRRGRTLDFKGFPIRYWEAGQ--GRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKp 78
Cdd:PRK14875  95 RRFAPEGIDEEDAGPAPRKARIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSK- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  79 RAHRYSLLEQADLQQALLGRLGIdEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFL-NGGLFPETHRPVLSQkllls 157
Cdd:PRK14875 174 AVGAGSLDELAAAVLAFLDALGI-ERAHLVGHSMGGAVALRLAARAPQ---RVASLTLIaPAGLGPEINGDYIDG----- 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 158 plgglFGRLFDRRALARNFAKVFGPRSQPGETELDAFWSLIESNQGQRVMHRLIRYIVDRREQRERWVAALQHGGVPLRV 237
Cdd:PRK14875 245 -----FVAAESRRELKPVLELLFADPALVTRQMVEDLLKYKRLDGVDDALRALADALFAGGRQRVDLRDRLASLAIPVLV 319

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489192988 238 IDGAVDPI-SGAHMveryRQLVADADCVLLDGIGHYPQIEAPAAVLEHYLAFRAR 291
Cdd:PRK14875 320 IWGEQDRIiPAAHA----QGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 18-126 5.54e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 67.71  E-value: 5.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  18 RTLDFKGFPIRYWEAGQGRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRAHrYSLLEQADLQQALLG 97
Cdd:PRK03592  10 RRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDID-YTFADHARYLDAWFD 88

                         90       100
                 ....*....|....*....|....*....
gi 489192988  98 RLGIDEPLHVLaHDYGDSVAQELLARHHE 126
Cdd:PRK03592  89 ALGLDDVVLVG-HDWGSALGFDWAARHPD 116
PLN02578 PLN02578
hydrolase
 22-281 4.98e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 65.63  E-value: 4.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  22 FKGFPIRYWEAGQGRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKprahrySLLE-QADL---QQALLG 97
Cdd:PLN02578  73 WRGHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDK------ALIEyDAMVwrdQVADFV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  98 RLGIDEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFLN-GGLFPETHRP---------VLSQKLLLSPLGGLFGRlf 167
Cdd:PLN02578 147 KEVVKEPAVLVGNSLGGFTALSTAVGYPE---LVAGVALLNsAGQFGSESREkeeaivveeTVLTRFVVKPLKEWFQR-- 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 168 drraLARNFakVFGPRSQPGETE------------LDAFwsLIES--------NQGQ---RVMHRLI----RYIVDRreq 220
Cdd:PLN02578 222 ----VVLGF--LFWQAKQPSRIEsvlksvykdksnVDDY--LVESitepaadpNAGEvyyRLMSRFLfnqsRYTLDS--- 290

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192988 221 rerwvaALQHGGVPLRVIDGAVDPISGAHMVERYRQLVADADCVLLDGiGHYPQIEAPAAV 281
Cdd:PLN02578 291 ------LLSKLSCPLLLLWGDLDPWVGPAKAEKIKAFYPDTTLVNLQA-GHCPHDEVPEQV 344
PRK05855 PRK05855
SDR family oxidoreductase;
35-133 1.49e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 64.62  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  35 GRP-LLLIHGFPsaawDWHYLWEP----LAQRYRVLVCDLLGFGDSAKPRAHR-YSLLEQADLQQALLGRLGIDEPLHVL 108
Cdd:PRK05855  24 DRPtVVLVHGYP----DNHEVWDGvaplLADRFRVVAYDVRGAGRSSAPKRTAaYTLARLADDFAAVIDAVSPDRPVHLL 99

                         90       100
                 ....*....|....*....|....*
gi 489192988 109 AHDYGDSVAQELLARhHEGRLRLAS 133
Cdd:PRK05855 100 AHDWGSIQGWEAVTR-PRAAGRIAS 123
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 15-78 1.56e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 54.74  E-value: 1.56e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489192988  15 RRGRTLDFKGFPIRYWEAG-QGRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKP 78
Cdd:PLN02824   8 VETRTWRWKGYNIRYQRAGtSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP 72
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
24-138 2.00e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 53.47  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  24 GFPIRYW----EAGQGRPLLLIHGFPSAAWDWHYLWEPLAQR-YRVLVCDLLGFGDSAKPRAHRYSLLE-QADLQQAL-- 95
Cdd:COG2267   13 GLRLRGRrwrpAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDyVDDLRAALda 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489192988  96 LGRLGiDEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFLN 138
Cdd:COG2267   93 LRARP-GLPVVLLGHSMGGLIALLYAARYPD---RVAGLVLLA 131
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 27-281 2.55e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 54.09  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  27 IRYWEAGQGRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRAHRYSLLEQADLQQALLGRLGIDEPLh 106
Cdd:PRK03204  26 IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFGYQIDEHARVIGEFVDHLGLDRYL- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 107 VLAHDYGDSVAQELLARHHEgrlRLASCVFLNGGLFPEThrpVLSQKLLLSPLGglfGRLFDRRALARNF--AKVF--GP 182
Cdd:PRK03204 105 SMGQDWGGPISMAVAVERAD---RVRGVVLGNTWFWPAD---TLAMKAFSRVMS---SPPVQYAILRRNFfvERLIpaGT 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 183 RSQPGETELD---AFWSLIESNQGQRVMHRLIRYIVDRREQRERWVAAlQHGGVPLRVIDGAVDPI-SGAHMVERYRQLV 258
Cdd:PRK03204 176 EHRPSSAVMAhyrAVQPNAAARRGVAEMPKQILAARPLLARLAREVPA-TLGTKPTLLVWGMKDVAfRPKTILPRLRATF 254

                        250       260
                 ....*....|....*....|...
gi 489192988 259 ADADCVLLDGIGHYPQIEAPAAV 281
Cdd:PRK03204 255 PDHVLVELPNAKHFIQEDAPDRI 277
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 38-283 3.78e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 52.86  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988   38 LLLIHGFPSAAWDWHYLwepLAQRYRVLVCDLLGFGDSAKPRahrYSLLEQADLQqALLGRLGIDEPLHVLAHDYGDSVA 117
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL---LAAGVAVLAPDLPGHGSSSPPP---LDLADLADLA-ALLDELGAARPVVLVGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  118 QELLARHhegrlrLASCVFLNGGLFPETHRPVLSQKLLLSPLGGLFGRLFDRRALARNFAkvfgprsqpGETELDAFWSL 197
Cdd:pfam12697  74 LAAAAAA------LVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFL---------DDLPADAEWAA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  198 IESNQGQRVMHRLIRYivdrreqrerwVAALQHGGVPLRVIDGAvDPISgAHMVERYRQLVADADCVLLDGIGHYPQiEA 277
Cdd:pfam12697 139 ALARLAALLAALALLP-----------LAAWRDLPVPVLVLAEE-DRLV-PELAQRLLAALAGARLVVLPGAGHLPL-DD 204


                  ....*.
gi 489192988  278 PAAVLE 283
Cdd:pfam12697 205 PEEVAE 210
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 37-167 7.37e-08

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 52.96  E-value: 7.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  37 PLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRA---HRYSLLEQADLQQALLGRLGIDEpLHVLAHDYG 113
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPgygFNYTLDEYVSSLESLIDELKSDK-VSLVVQGYF 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489192988 114 DSVAQELLARHHEgrlRLASCVFLNGGLFPEtHRPVLSQKLLLSPLggLFGRLF 167
Cdd:PLN03084 208 SPPVVKYASAHPD---KIKKLILLNPPLTKE-HAKLPSTLSEFSNF--LLGEIF 255
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 20-293 8.45e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 52.66  E-value: 8.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  20 LDFKGFPIR--YWEAGQ--GRPLLLIHGFPSaawdWHYLWE----PLAQR-YRVLVCDLLGFGDSAKP-RAHRYSLLEQA 89
Cdd:PRK00870  27 DDGDGGPLRmhYVDEGPadGPPVLLLHGEPS----WSYLYRkmipILAAAgHRVIAPDLIGFGRSDKPtRREDYTYARHV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  90 DLQQALLGRLGIdEPLHVLAHDYGDSVAQELLARHHEgrlRLASCVFLNGGLFPETHRPvlsqklllsPLGGLFGRLFDR 169
Cdd:PRK00870 103 EWMRSWFEQLDL-TDVTLVCQDWGGLIGLRLAAEHPD---RFARLVVANTGLPTGDGPM---------PDAFWAWRAFSQ 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 170 RALARNFAKVF--GPRSQPGETELDAFWSLI--ESNQ-GQRVMHRLIRYIVDR---REQRERWvAALQHGGVPLRVIDGA 241
Cdd:PRK00870 170 YSPVLPVGRLVngGTVRDLSDAVRAAYDAPFpdESYKaGARAFPLLVPTSPDDpavAANRAAW-AVLERWDKPFLTAFSD 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489192988 242 VDPIS--GAHMVERYRQLVADADCVLLDGIGHYPQIEAPAAVLEHYLAFRARLD 293
Cdd:PRK00870 249 SDPITggGDAILQKRIPGAAGQPHPTIKGAGHFLQEDSGEELAEAVLEFIRATP 302
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 35-159 9.58e-08

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: 51.83  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988   35 GRPLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRA-HRYSLLEQA-DLQQALLGRLGIdEPLHVLAHDY 112
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDiERYDFEEAAqLLLATLLDQLGI-EPFFLVGYSM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489192988  113 GDSVAQELLARHHEG--RLRLASCvflNGGLFPETHRPV-------LSQKLLLSPL 159
Cdd:TIGR03695  81 GGRIALYYALQYPERvqGLILESG---SPGLQTEEERAArrqndeqLAQRFEQEGL 133
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 10-292 2.97e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 50.99  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  10 LEAWRRRGRTLDFKG-FPIRYWEAGQGR------PLLLIHGFPSAAWDWHYLWEPLAQRYRVLVCDLLGFGDSAKPRAHR 82
Cdd:PLN02679  56 LEEIYERCKKWKWKGeYSINYLVKGSPEvtssgpPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  83 YSLLEQADLQQALLGRLgIDEPLHVLAHDYGdSVAQeLLARHHEGRLRLASCVFLN--GGLfpeTHRPVLSQ---KLLLs 157
Cdd:PLN02679 136 YTMETWAELILDFLEEV-VQKPTVLIGNSVG-SLAC-VIAASESTRDLVRGLVLLNcaGGM---NNKAVVDDwriKLLL- 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 158 PL--------------GGLFGRLFDRRALARNFAKVFGPR-----------SQPGETE--LDAFWSLIESNQGQRVMhRL 210
Cdd:PLN02679 209 PLlwlidfllkqrgiaSALFNRVKQRDNLKNILLSVYGNKeavddelveiiRGPADDEgaLDAFVSIVTGPPGPNPI-KL 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 211 IRYIvdrreqrERWVAALQHGGVPLRVIDGAVdpisGAHMVERYRQLvADADCVLLDGIGHYPQIEAPAAVLEHYLAFRA 290
Cdd:PLN02679 288 IPRI-------SLPILVLWGDQDPFTPLDGPV----GKYFSSLPSQL-PNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLA 355


                 ..
gi 489192988 291 RL 292
Cdd:PLN02679 356 QL 357
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 39-124 4.84e-07

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 50.58  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  39 LLIHGFPSAAWDWHYLWEP-----LAQRYRVLVCDLLGFGDSAKPRAHRYSLLEQADL-QQALLGRLGIdEPLHVLAHDY 112
Cdd:PLN03087 205 LFIHGFISSSAFWTETLFPnfsdaAKSTYRLFAVDLLGFGRSPKPADSLYTLREHLEMiERSVLERYKV-KSFHIVAHSL 283

                         90
                 ....*....|..
gi 489192988 113 GDSVAQELLARH 124
Cdd:PLN03087 284 GCILALALAVKH 295
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
24-126 2.48e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.54  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  24 GFPIRYW----EAGQGRPL-LLIHGFPSAAWDWHYLW-EPLAQR-YRVLVCDLLGFGDSAKprahRYSLLEQADLQQA-- 94
Cdd:COG1506    7 GTTLPGWlylpADGKKYPVvVYVHGGPGSRDDSFLPLaQALASRgYAVLAPDYRGYGESAG----DWGGDEVDDVLAAid 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489192988  95 -LLGRLGID-EPLHVLAHDYGDSVAQELLARHHE 126
Cdd:COG1506   83 yLAARPYVDpDRIGIYGHSYGGYMALLAAARHPD 116
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
26-272 3.28e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 41.47  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988  26 PIRYWEAGQGrpLLLIHGFPSAAWDWHYLWEPLAQR-YRVLVCDLLGFGDS----AKPRAHRYslleQADLQQALLGRLG 100
Cdd:COG1647    8 PFFLEGGRKG--VLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSpedlLKTTWEDW----LEDVEEAYEILKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 101 IDEPLHVLAHDYGDSVAQELLARHHEgrlrLASCVFLNGGLFPEthrpvlSQKLLLSPLGGLFGRLFdrRALARNFAKVF 180
Cdd:COG1647   82 GYDKVIVIGLSMGGLLALLLAARYPD----VAGLVLLSPALKID------DPSAPLLPLLKYLARSL--RGIGSDIEDPE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192988 181 GPRSQPGETELDAFWSLiesnqgqrvmHRLIRYIvdrREQRERWVAalqhggvPLRVI----DGAVDPISGAHMVERYRQ 256
Cdd:COG1647  150 VAEYAYDRTPLRALAEL----------QRLIREV---RRDLPKITA-------PTLIIqsrkDEVVPPESARYIYERLGS 209

                        250
                 ....*....|....*.
gi 489192988 257 lvADADCVLLDGIGHY 272
Cdd:COG1647  210 --PDKELVWLEDSGHV 223
 
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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