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Conserved domains on  [gi|640507330|ref|WP_024943709|]
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MULTISPECIES: alpha/beta fold hydrolase [Aeromonas]

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, ...
 3-266 1.83e-45

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: 152.08  E-value: 1.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   3 QFMEIAGRQMAYLDEG-QGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDAlPEGACTLATLARDHLALL 81
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  82 DALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSFVglepqitcERYLGMLAMieqlgtipapiveqvaplffad 161
Cdd:COG0596   84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL--------AALAEPLRR---------------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330 162 qpDADLMSGFKARLAAwpadkvaamvavgrsfVTREDRIEWLEAISVPALVMTGSQDKARPVLEGYLMAEVL-GCPFKEV 240
Cdd:COG0596  134 --PGLAPEALAALLRA----------------LARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLpNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 640507330 241 PAAGHIASLENPAFVNDQLGAFLAAL 266
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-266 1.83e-45

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: 152.08  E-value: 1.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   3 QFMEIAGRQMAYLDEG-QGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDAlPEGACTLATLARDHLALL 81
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  82 DALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSFVglepqitcERYLGMLAMieqlgtipapiveqvaplffad 161
Cdd:COG0596   84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL--------AALAEPLRR---------------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330 162 qpDADLMSGFKARLAAwpadkvaamvavgrsfVTREDRIEWLEAISVPALVMTGSQDKARPVLEGYLMAEVL-GCPFKEV 240
Cdd:COG0596  134 --PGLAPEALAALLRA----------------LARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLpNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 640507330 241 PAAGHIASLENPAFVNDQLGAFLAAL 266
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 16-264 3.54e-38

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 134.41  E-value: 3.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   16 DEGQGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDAlPEGACTLATLARDHLALLDALGIDEFVLVGLS 95
Cdd:TIGR02427   9 AADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDA-PEGPYSIEDLADDVLALLDHLGIERAVFCGLS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   96 IGGMWGVELARMAPARLKGLVLMDSfvglEPQI-TCERYLGMLAMIEQLGTipAPIVEQVAPLFFAD---QPDADLMSGF 171
Cdd:TIGR02427  88 LGGLIAQGLAARRPDRVRALVLSNT----AAKIgTPESWNARIAAVRAEGL--AALADAVLERWFTPgfrEAHPARLDLY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  172 KARLAAWPADKVAAMVAVGRSFvtreDRIEWLEAISVPALVMTGSQDKARPVLEGYLMAE-VLGCPFKEVPAAGHIASLE 250
Cdd:TIGR02427 162 RNMLVRQPPDGYAGCCAAIRDA----DFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADlVPGARFAEIRGAGHIPCVE 237

                         250
                  ....*....|....
gi 640507330  251 NPAFVNDQLGAFLA 264
Cdd:TIGR02427 238 QPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-252 4.44e-22

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: 91.80  E-value: 4.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   21 PVLLFGHSYLWDSAMWAPQIEAL-KGQYRCIVPELWGHGDSDALPE-GACTLATLARDHLALLDALGIDEFVLVGLSIGG 98
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   99 MWGVELARMAPARLKGLVLMDSFVGLEPQITCERYLGMLaMIEQLGTIPAPIVEQVAPLFFADQ-----------PDADL 167
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL-FPGFFDGFVADFAPNPLGRLVAKLlallllrlrllKALPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  168 MSGFKARLAAWPADKVAAMVAVGRSFVTREDRIEWLEAISVPALVMTGSQDKARPVLEGYLMAEVLGCPFKEV-PAAGHI 246
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVViPDAGHF 239


                  ....*.
gi 640507330  247 ASLENP 252
Cdd:pfam00561 240 AFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 2-122 9.46e-20

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 86.20  E-value: 9.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   2 KQFMEIAGRQMAYLDEGQGPVLLFGH-----SYLWDSAMwaPQIEalkGQYRCIVPELWGHGDSDAlPEGACTLATLARD 76
Cdd:PRK03592   9 MRRVEVLGSRMAYIETGEGDPIVFLHgnptsSYLWRNII--PHLA---GLGRCLAPDLIGMGASDK-PDIDYTFADHARY 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 640507330  77 HLALLDALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSFV 122
Cdd:PRK03592  83 LDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIV 128
Esterase_713 cd12807
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ...
 19-194 6.11e-03

Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214006  Cd Length: 315  Bit Score: 37.30  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  19 QGPVLLFGHSYLWDSAMWAPQ-----------IEALKGQYRCIVPELwghgdSDALPEGACTLATLArdhlALLDALGid 87
Cdd:cd12807  121 LPAIFRAGDEFAWTNFRFGPTygvpfpdtqfpVEAVAEFYKQVVPDL-----NATLPTPNPTPNALA----ALADKLG-- 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  88 EFVLVGLSIGGMWGVELARMAPARLKGLvlmdsfVGLEPQITCERYlgmLAMIEQLGTIPAPIVeqvaplfFADQPDADL 167
Cdd:cd12807  190 GAVLLGHSQSGPFPLEAALLRPAGVKGI------VSVEPGCCPAPT---ADQIKTLAKIPILVV-------FGDHLDAAS 253

                        170       180
                 ....*....|....*....|....*..
gi 640507330 168 MSGFKARLAAWPADKVAAMVAVGRSFV 194
Cdd:cd12807  254 GPTWQQRLQACQAFVDRINAAGGDAKL 280
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-266 1.83e-45

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: 152.08  E-value: 1.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   3 QFMEIAGRQMAYLDEG-QGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDAlPEGACTLATLARDHLALL 81
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  82 DALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSFVglepqitcERYLGMLAMieqlgtipapiveqvaplffad 161
Cdd:COG0596   84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL--------AALAEPLRR---------------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330 162 qpDADLMSGFKARLAAwpadkvaamvavgrsfVTREDRIEWLEAISVPALVMTGSQDKARPVLEGYLMAEVL-GCPFKEV 240
Cdd:COG0596  134 --PGLAPEALAALLRA----------------LARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLpNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 640507330 241 PAAGHIASLENPAFVNDQLGAFLAAL 266
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 16-264 3.54e-38

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 134.41  E-value: 3.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   16 DEGQGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDAlPEGACTLATLARDHLALLDALGIDEFVLVGLS 95
Cdd:TIGR02427   9 AADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDA-PEGPYSIEDLADDVLALLDHLGIERAVFCGLS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   96 IGGMWGVELARMAPARLKGLVLMDSfvglEPQI-TCERYLGMLAMIEQLGTipAPIVEQVAPLFFAD---QPDADLMSGF 171
Cdd:TIGR02427  88 LGGLIAQGLAARRPDRVRALVLSNT----AAKIgTPESWNARIAAVRAEGL--AALADAVLERWFTPgfrEAHPARLDLY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  172 KARLAAWPADKVAAMVAVGRSFvtreDRIEWLEAISVPALVMTGSQDKARPVLEGYLMAE-VLGCPFKEVPAAGHIASLE 250
Cdd:TIGR02427 162 RNMLVRQPPDGYAGCCAAIRDA----DFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADlVPGARFAEIRGAGHIPCVE 237

                         250
                  ....*....|....
gi 640507330  251 NPAFVNDQLGAFLA 264
Cdd:TIGR02427 238 QPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-252 4.44e-22

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: 91.80  E-value: 4.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   21 PVLLFGHSYLWDSAMWAPQIEAL-KGQYRCIVPELWGHGDSDALPE-GACTLATLARDHLALLDALGIDEFVLVGLSIGG 98
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   99 MWGVELARMAPARLKGLVLMDSFVGLEPQITCERYLGMLaMIEQLGTIPAPIVEQVAPLFFADQ-----------PDADL 167
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL-FPGFFDGFVADFAPNPLGRLVAKLlallllrlrllKALPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  168 MSGFKARLAAWPADKVAAMVAVGRSFVTREDRIEWLEAISVPALVMTGSQDKARPVLEGYLMAEVLGCPFKEV-PAAGHI 246
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVViPDAGHF 239


                  ....*.
gi 640507330  247 ASLENP 252
Cdd:pfam00561 240 AFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 20-263 2.41e-21

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: 89.97  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   20 GPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDALPEGAC-TLATLARDHLA-LLDALGIDEFVLVGLSIG 97
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERyDFEEAAQLLLAtLLDQLGIEPFFLVGYSMG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   98 GMWGVELARMAPARLKGLVLMDSFVGLE-PQITCERYL--GMLA-MIEQLGtipapiVEQVA------PLFfADQ---PD 164
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLILESGSPGLQtEEERAARRQndEQLAqRFEQEG------LEAFLddwyqqPLF-ASQknlPP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  165 ADLMSGFKARLAAWPAdKVAAM-----VAVGRSFvtredrIEWLEAISVPALVMTGSQDKARPVLEGYLMAEVLGCPFKE 239
Cdd:TIGR03695 155 EQRQALRAERLANNPE-GLAKMlratgLGKQPSL------WPKLQALKIPVLYLCGERDEKFVQIAKEMQKLIPNLTLHI 227

                         250       260
                  ....*....|....*....|....
gi 640507330  240 VPAAGHIASLENPAFVNDQLGAFL 263
Cdd:TIGR03695 228 IPNAGHNIHLENPEAFAKILLAFL 251
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 2-122 9.46e-20

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 86.20  E-value: 9.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   2 KQFMEIAGRQMAYLDEGQGPVLLFGH-----SYLWDSAMwaPQIEalkGQYRCIVPELWGHGDSDAlPEGACTLATLARD 76
Cdd:PRK03592   9 MRRVEVLGSRMAYIETGEGDPIVFLHgnptsSYLWRNII--PHLA---GLGRCLAPDLIGMGASDK-PDIDYTFADHARY 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 640507330  77 HLALLDALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSFV 122
Cdd:PRK03592  83 LDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIV 128
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 3-265 3.31e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 83.07  E-value: 3.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   3 QFMEIAGRQMAYLDEGQG---PVLLFgHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDALPEGAcTLATLARDHLA 79
Cdd:PRK14875 112 RKARIGGRTVRYLRLGEGdgtPVVLI-HGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAG-SLDELAAAVLA 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  80 LLDALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSfVGLEPQITCErYLGmlamieqlGTIPAPIVEQVAP--- 156
Cdd:PRK14875 190 FLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP-AGLGPEINGD-YID--------GFVAAESRRELKPvle 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330 157 LFFADQpdaDLMSG--FKARLAAWPADKV-AAMVAVGRSF----VTREDRIEWLEAISVPALVMTGSQDKARPV-----L 224
Cdd:PRK14875 260 LLFADP---ALVTRqmVEDLLKYKRLDGVdDALRALADALfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAahaqgL 336

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 640507330 225 EGYLMAEVLgcpfkevPAAGHIASLENPAFVNDQLGAFLAA 265
Cdd:PRK14875 337 PDGVAVHVL-------PGAGHMPQMEAAADVNRLLAEFLGK 370
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
6-150 1.81e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 61.94  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   6 EIAGRQMAYLDEGQGPVLLFgHSYLWDSAMWAPQIEALKGQ-YRCIVPELWGHGDSDALPEGACTLATLARDHLALLDAL 84
Cdd:COG2267   15 RLRGRRWRPAGSPRGTVVLV-HGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDAL 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  85 ---GIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSFVGLEPQITC-ERYLGMLAMIEQLGTIPAPI 150
Cdd:COG2267   94 rarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPsARWLRALRLAEALARIDVPV 163
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 4-117 9.77e-10

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 57.94  E-value: 9.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   4 FMEIAGRqMAYLDEGQGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDALPEGACTLATLARDHLALLDA 83
Cdd:PRK03204  19 FDSSRGR-IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFGYQIDEHARVIGEFVDH 97

                         90       100       110
                 ....*....|....*....|....*....|....
gi 640507330  84 LGIDEFVLVGLSIGGMWGVELARMAPARLKGLVL 117
Cdd:PRK03204  98 LGLDRYLSMGQDWGGPISMAVAVERADRVRGVVL 131
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
5-266 1.61e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 56.87  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   5 MEIAGRQMAYLDEGQGPVLLFgHSYL---WDSAMWAPQIEAlKGqYRCIVPELWGHGDSdalPEgacTLATL-------- 73
Cdd:COG1647    1 MKILGAEPFFLEGGRKGVLLL-HGFTgspAEMRPLAEALAK-AG-YTVYAPRLPGHGTS---PE---DLLKTtwedwled 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  74 ARDHLALLDALGiDEFVLVGLSIGGMWGVELARMAPArLKGLVLMDSFVglepqitceRYLGMLAMIeqlgtipAPIVEQ 153
Cdd:COG1647   72 VEEAYEILKAGY-DKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPAL---------KIDDPSAPL-------LPLLKY 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330 154 VAPLFFADQPDADLMSGFKARLAAWPADKVAAMVAVGRSfvTREDriewLEAISVPALVMTGSQDKARPVLEGYLMAEVL 233
Cdd:COG1647  134 LARSLRGIGSDIEDPEVAEYAYDRTPLRALAELQRLIRE--VRRD----LPKITAPTLIIQSRKDEVVPPESARYIYERL 207

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640507330 234 GCPFKEV---PAAGHIASLENPA-FVNDQLGAFLAAL 266
Cdd:COG1647  208 GSPDKELvwlEDSGHVITLDKDReEVAEEILDFLERL 244
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 41-257 3.24e-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: 52.48  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   41 EALKGQYRCIVPELWGHGDSDALPEGActlaTLARDHLALLDALGIDE-FVLVGLSIGGMWGVELARMAPARlkgLVLMD 119
Cdd:pfam12697  16 ALLAAGVAVLAPDLPGHGSSSPPPLDL----ADLADLAALLDELGAARpVVLVGHSLGGAVALAAAAAALVV---GVLVA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  120 SFVGLEPQITcerylgmlamiEQLGTIPAPIVEQVAPLFFADQPDADLMSGFKARLAAWPADKVAAMVAVGRSFVTREDR 199
Cdd:pfam12697  89 PLAAPPGLLA-----------ALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALLPLAA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 640507330  200 iewLEAISVPALVMtGSQDKARPVLEGYLMAEVLGCPFKEVPAAGHiASLENPAFVND 257
Cdd:pfam12697 158 ---WRDLPVPVLVL-AEEDRLVPELAQRLLAALAGARLVVLPGAGH-LPLDDPEEVAE 210
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 20-264 7.36e-07

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 49.07  E-value: 7.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  20 GPVLLFGHSYLWDSAMWAPQIEALKgQYRCIVPELWGHGDSDALP----EGACTLATlardhlALLDALGIDEFVLVGLS 95
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDWQPVGEALP-DYPRLYIDLPGHGGSAAISvdgfADVSRLLS------QTLQSYNILPYWLVGYS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  96 IGGmwgvelaRMA--------PARLKGLVLMDSFVGLEPQITCE-RYLGMLAMIEQLGTIPApivEQVaplfFAD---QP 163
Cdd:PRK11126  75 LGG-------RIAmyyacqglAGGLCGLIVEGGNPGLQNAEERQaRWQNDRQWAQRFRQEPL---EQV----LADwyqQP 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330 164 D-ADLMSGFKARLAAWPADK----VAAMVaVGRSFVTREDRIEWLEAISVPALVMTGSQD-KARPvlegylMAEVLGCPF 237
Cdd:PRK11126 141 VfASLNAEQRQQLVAKRSNNngaaVAAML-EATSLAKQPDLRPALQALTFPFYYLCGERDsKFQA------LAQQLALPL 213

                        250       260
                 ....*....|....*....|....*..
gi 640507330 238 KEVPAAGHIASLENPAFVNDQLGAFLA 264
Cdd:PRK11126 214 HVIPNAGHNAHRENPAAFAASLAQILR 240
PRK10673 PRK10673
esterase;
57-119 1.17e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.49  E-value: 1.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640507330  57 HGDSDALPEgaCTLATLARDHLALLDALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMD 119
Cdd:PRK10673  53 HGLSPRDPV--MNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 18-119 7.73e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 43.19  E-value: 7.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  18 GQGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSD------ALPEGACTLATLARDHLALLDALGIDEFVL 91
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDkpnprsAPPNSFYTFETWGEQLNDFCSDVVGDPAFV 106

                         90       100
                 ....*....|....*....|....*...
gi 640507330  92 VGLSIGGMWGVELARMAPARLKGLVLMD 119
Cdd:PLN02824 107 ICNSVGGVVGLQAAVDAPELVRGVMLIN 134
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 16-125 9.27e-05

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 43.69  E-value: 9.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   16 DEGQGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDAL-------PEGACTLATLARDHLALLDALGIDE 88
Cdd:PLN02980 1367 QNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQnhaketqTEPTLSVELVADLLYKLIEHITPGK 1446

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 640507330   89 FVLVGLSIGGMWGVELARMAPARLKGLVLMDSFVGLE 125
Cdd:PLN02980 1447 VTLVGYSMGARIALYMALRFSDKIEGAVIISGSPGLK 1483
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 12-121 1.15e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 42.65  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  12 MAYLDEGQ--GPVLLFGH-----SYLWdSAMWAPQIEAlkgQYRCIVPELWGHGDSDAlPEGACTLaTLARdHL----AL 80
Cdd:PRK00870  36 MHYVDEGPadGPPVLLLHgepswSYLY-RKMIPILAAA---GHRVIAPDLIGFGRSDK-PTRREDY-TYAR-HVewmrSW 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 640507330  81 LDALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDSF 121
Cdd:PRK00870 109 FEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTG 149
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
18-243 2.74e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 41.54  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  18 GQGPV-LLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDALpeGACTLATLArdhlALLDALGIDEFVLVGLSI 96
Cdd:PRK10349  10 GQGNVhLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGF--GALSLADMA----EAVLQQAPDKAIWLGWSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  97 GGMWGVELARMAPARLKGLVLM---------DSFVGLEPQI--------------TCERYLGMLAMIEQLGTIPAPIVEQ 153
Cdd:PRK10349  84 GGLVASQIALTHPERVQALVTVasspcfsarDEWPGIKPDVlagfqqqlsddfqrTVERFLALQTMGTETARQDARALKK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330 154 VapLFFADQPDADLMSGfkarlaawpadkvaamvavGRSFVTREDRIEWLEAISVPALVMTGSQD-----KARPVL---- 224
Cdd:PRK10349 164 T--VLALPMPEVDVLNG-------------------GLEILKTVDLRQPLQNVSMPFLRLYGYLDglvprKVVPMLdklw 222

                        250       260
                 ....*....|....*....|..
gi 640507330 225 ---EGYLMAEVLGCPFKEVPAA 243
Cdd:PRK10349 223 phsESYIFAKAAHAPFISHPAE 244
PRK05855 PRK05855
SDR family oxidoreductase;
20-101 3.18e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 41.89  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  20 GPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSDA-LPEGACTLATLARDHLALLDALGIDEFVLVglsIGG 98
Cdd:PRK05855  25 RPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSApKRTAAYTLARLADDFAAVIDAVSPDRPVHL---LAH 101


                 ...
gi 640507330  99 MWG 101
Cdd:PRK05855 102 DWG 104
PLN02578 PLN02578
hydrolase
 4-120 8.59e-04

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 40.21  E-value: 8.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330   4 FMEIAGRQMAYLDEGQGPVLLFGHSYLWDSAMWAPQIEALKGQYRCIVPELWGHGDSD-ALPEGActlATLARDHLA-LL 81
Cdd:PLN02578  70 FWTWRGHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDkALIEYD---AMVWRDQVAdFV 146

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 640507330  82 DALGIDEFVLVGLSIGGMWGVELARMAPARLKGLVLMDS 120
Cdd:PLN02578 147 KEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
PRK08775 PRK08775
homoserine O-succinyltransferase;
74-117 3.93e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 38.23  E-value: 3.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 640507330  74 ARDHLALLDALGIDE-FVLVGLSIGGMWGVELARMAPARLKGLVL 117
Cdd:PRK08775 124 ADAIALLLDALGIARlHAFVGYSYGALVGLQFASRHPARVRTLVV 168
Esterase_713 cd12807
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ...
 19-194 6.11e-03

Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214006  Cd Length: 315  Bit Score: 37.30  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  19 QGPVLLFGHSYLWDSAMWAPQ-----------IEALKGQYRCIVPELwghgdSDALPEGACTLATLArdhlALLDALGid 87
Cdd:cd12807  121 LPAIFRAGDEFAWTNFRFGPTygvpfpdtqfpVEAVAEFYKQVVPDL-----NATLPTPNPTPNALA----ALADKLG-- 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  88 EFVLVGLSIGGMWGVELARMAPARLKGLvlmdsfVGLEPQITCERYlgmLAMIEQLGTIPAPIVeqvaplfFADQPDADL 167
Cdd:cd12807  190 GAVLLGHSQSGPFPLEAALLRPAGVKGI------VSVEPGCCPAPT---ADQIKTLAKIPILVV-------FGDHLDAAS 253

                        170       180
                 ....*....|....*....|....*..
gi 640507330 168 MSGFKARLAAWPADKVAAMVAVGRSFV 194
Cdd:cd12807  254 GPTWQQRLQACQAFVDRINAAGGDAKL 280
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 16-124 6.32e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.58  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640507330  16 DEGQGPVLLFgHSYLWDSAMWAPQIEALKGQ-YRCIVPEL-WGHGDSDALpegACTLATLARdhlALLDALGIDEFVLVG 93
Cdd:COG1075    2 AATRYPVVLV-HGLGGSAASWAPLAPRLRAAgYPVYALNYpSTNGSIEDS---AEQLAAFVD---AVLAATGAEKVDLVG 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 640507330  94 LSIGGMwgveLARMAPARLKGLVLMDSFVGL 124
Cdd:COG1075   75 HSMGGL----VARYYLKRLGGAAKVARVVTL 101
 
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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