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Conserved domains on  [gi|2036720018|emb|CAF1904781|]
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2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate synthase [Bacillus subtilis]

Protein Classification

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase( domain architecture ID 11497333)

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (MenH) is an important enzyme in the biosynthesis of menaquinone, catalyzing an unusual 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) to form 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 23-272 5.97e-128

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: 363.46  E-value: 5.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  23 ASEAVVCLHGFTGSKQSWTFLDEML-PDSRLIKIDCLGHGETDAPLNGKRYSTSRQVSD-LAEIFDQLKLHKVKLIGYSM 100
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALgPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLlLATLLDQLGIEPFFLVGYSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 101 GGRLAYSFAMTYPERVSALVLESTTPGLKTLGERRERIMRDRKLADFILRDGLKAFVAYWENIPLFSSQQRLAEDIRHRI 180
Cdd:TIGR03695  81 GGRIALYYALQYPERVQGLILESGSPGLQTEEERAARRQNDEQLAQRFEQEGLEAFLDDWYQQPLFASQKNLPPEQRQAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 181 RSGRLRNNKIGLANSLTGMGTGSQPSLWSRVEEIDVPVLLICGEWDEKFCAINQEVHKMLPSSRIEIVPKAGHTVHVEQP 260
Cdd:TIGR03695 161 RAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEMQKLIPNLTLHIIPNAGHNIHLENP 240

                         250
                  ....*....|..
gi 2036720018 261 RLFGKIVSEFLT 272
Cdd:TIGR03695 241 EAFAKILLAFLE 252
 
Name Accession Description Interval E-value
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 23-272 5.97e-128

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: 363.46  E-value: 5.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  23 ASEAVVCLHGFTGSKQSWTFLDEML-PDSRLIKIDCLGHGETDAPLNGKRYSTSRQVSD-LAEIFDQLKLHKVKLIGYSM 100
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALgPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLlLATLLDQLGIEPFFLVGYSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 101 GGRLAYSFAMTYPERVSALVLESTTPGLKTLGERRERIMRDRKLADFILRDGLKAFVAYWENIPLFSSQQRLAEDIRHRI 180
Cdd:TIGR03695  81 GGRIALYYALQYPERVQGLILESGSPGLQTEEERAARRQNDEQLAQRFEQEGLEAFLDDWYQQPLFASQKNLPPEQRQAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 181 RSGRLRNNKIGLANSLTGMGTGSQPSLWSRVEEIDVPVLLICGEWDEKFCAINQEVHKMLPSSRIEIVPKAGHTVHVEQP 260
Cdd:TIGR03695 161 RAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEMQKLIPNLTLHIIPNAGHNIHLENP 240

                         250
                  ....*....|..
gi 2036720018 261 RLFGKIVSEFLT 272
Cdd:TIGR03695 241 EAFAKILLAFLE 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-273 1.30e-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: 150.15  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   1 MGTVNITVSDGVRYAVADEGPNAsEAVVCLHGFTGSKQSWTFLDEMLPDS-RLIKIDCLGHGETDAPlnGKRYSTSRQVS 79
Cdd:COG0596     1 MSTPRFVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGyRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  80 DLAEIFDQLKLHKVKLIGYSMGGRLAYSFAMTYPERVSALVLESttpglkTLGERRERIMRDRKLADFILRDGLKAFvay 159
Cdd:COG0596    78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------EVLAALAEPLRRPGLAPEALAALLRAL--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 160 weniplfssqqrlaedirhrirsgrlrnnkiglansltgmgtgSQPSLWSRVEEIDVPVLLICGEWDEKF-CAINQEVHK 238
Cdd:COG0596   149 -------------------------------------------ARTDLRERLARITVPTLVIWGEKDPIVpPALARRLAE 185

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2036720018 239 MLPSSRIEIVPKAGHTVHVEQPRLFGKIVSEFLTS 273
Cdd:COG0596   186 LLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 9-272 2.62e-38

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 143.07  E-value: 2.62e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018    9 SDGVRYA--VADEGPNASEAVVC-LHGFTGSKQSWT-FLDEMLPDSRLIKIDCLGHGETDAPLNGKRYSTSRQVSD--LA 82
Cdd:PLN02980  1353 VDGFSCLikVHEVGQNAEGSVVLfLHGFLGTGEDWIpIMKAISGSARCISIDLPGHGGSKIQNHAKETQTEPTLSVelVA 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   83 EIFDQLKLH----KVKLIGYSMGGRLAYSFAMTYPERVSALVLESTTPGLKTLGERRERIMRDRKLADFILRDGLKAFVA 158
Cdd:PLN02980  1433 DLLYKLIEHitpgKVTLVGYSMGARIALYMALRFSDKIEGAVIISGSPGLKDEVARKIRSAKDDSRARMLIDHGLEIFLE 1512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  159 YWENIPLFSS---QQRLAEDIRHRIRSGRLRNnkigLANSLTGMGTGSQPSLWSRVEEIDVPVLLICGEWDEKFCAINQE 235
Cdd:PLN02980  1513 NWYSGELWKSlrnHPHFNKIVASRLLHKDVPS----LAKLLSDLSIGRQPSLWEDLKQCDTPLLLVVGEKDVKFKQIAQK 1588

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2036720018  236 V-HKMLPSSR-----------IEIVPKAGHTVHVEQPRLFGKIVSEFLT 272
Cdd:PLN02980  1589 MyREIGKSKEsgndkgkeiieIVEIPNCGHAVHLENPLPVIRALRKFLT 1637
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 26-260 1.17e-29

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: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  26 AVVCLHGFTGSKQSWTFLDEMLPDS--RLIKIDCLGHGETDAPLNGKRYSTSRQVSDLAEIFDQLKLHKVKLIGYSMGGR 103
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDgfRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 104 LAYSFAMTYPERVSALVLEST-TPGLKTLGERRERIMRDRKLADFILRDGLKAFVAYWENIPLFSSQQRLAEDIRHRIRS 182
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAlDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 183 GRLRNNKIGLANSLtGMGTGSQPSLWSRVEE------IDVPVLLICGEWDEKFCAINQEV-HKMLPSSRIEIVPKAGHTV 255
Cdd:pfam00561 162 KRFPSGDYALAKSL-VTGALLFIETWSTELRakflgrLDEPTLIIWGDQDPLVPPQALEKlAQLFPNARLVVIPDAGHFA 240


                  ....*
gi 2036720018 256 HVEQP 260
Cdd:pfam00561 241 FLEGP 245
C80_toxinA_B-like cd20502
Peptidase C80 cysteine binding domain of Clostridium difficile toxins A and B, and related ...
 21-138 3.53e-03

Peptidase C80 cysteine binding domain of Clostridium difficile toxins A and B, and related proteins; This peptidase C80 family includes the major virulence factors of Clostridium difficile multidomain toxins TcdA and TcdB. These large homologous toxins contain several distinct domains including a cysteine protease domain (CPD) that autoproteolytically releases a cytotoxic effector domain upon binding of intracellular inositol hexakisphosphate. C. difficile is a major cause of intestinal tissue damage and inflammation, and TcdA is generally more inflammatory whereas TcdB is more cytotoxic; studies show that the CPD is an internal regulator of the proinflammatory activity. Site-directed mutagenesis has identified functional residues Asp/His/Cys in Clostridium toxin B.


Pssm-ID: 410975  Cd Length: 209  Bit Score: 37.69  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  21 PNASEAVVCLHGFTGSKQSW---TFLDEMLPDSRL-----IKIDCLGHGETD------APLNGKRYSTSrqvsdLAEIFD 86
Cdd:cd20502    26 PKNSEWLQLNDGEIADVLTWdggSIQEVYTIPLRLddegkVKLTLVGHGEDEfgtttfGGLNAEQLSTE-----LSSLFD 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  87 QLKLH------KVKLIGYSMggrLAYSFAM--TYPERVsALVLESTTPglkTLGERRERI 138
Cdd:cd20502   101 QIKLDikpksiKINLLGCNL---FDYSQNLeeTLPGQL-ALWLKSKSD---ALGISKEQI 153
 
Name Accession Description Interval E-value
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 23-272 5.97e-128

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: 363.46  E-value: 5.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  23 ASEAVVCLHGFTGSKQSWTFLDEML-PDSRLIKIDCLGHGETDAPLNGKRYSTSRQVSD-LAEIFDQLKLHKVKLIGYSM 100
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALgPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLlLATLLDQLGIEPFFLVGYSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 101 GGRLAYSFAMTYPERVSALVLESTTPGLKTLGERRERIMRDRKLADFILRDGLKAFVAYWENIPLFSSQQRLAEDIRHRI 180
Cdd:TIGR03695  81 GGRIALYYALQYPERVQGLILESGSPGLQTEEERAARRQNDEQLAQRFEQEGLEAFLDDWYQQPLFASQKNLPPEQRQAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 181 RSGRLRNNKIGLANSLTGMGTGSQPSLWSRVEEIDVPVLLICGEWDEKFCAINQEVHKMLPSSRIEIVPKAGHTVHVEQP 260
Cdd:TIGR03695 161 RAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEMQKLIPNLTLHIIPNAGHNIHLENP 240

                         250
                  ....*....|..
gi 2036720018 261 RLFGKIVSEFLT 272
Cdd:TIGR03695 241 EAFAKILLAFLE 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-273 1.30e-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: 150.15  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   1 MGTVNITVSDGVRYAVADEGPNAsEAVVCLHGFTGSKQSWTFLDEMLPDS-RLIKIDCLGHGETDAPlnGKRYSTSRQVS 79
Cdd:COG0596     1 MSTPRFVTVDGVRLHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGyRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  80 DLAEIFDQLKLHKVKLIGYSMGGRLAYSFAMTYPERVSALVLESttpglkTLGERRERIMRDRKLADFILRDGLKAFvay 159
Cdd:COG0596    78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------EVLAALAEPLRRPGLAPEALAALLRAL--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 160 weniplfssqqrlaedirhrirsgrlrnnkiglansltgmgtgSQPSLWSRVEEIDVPVLLICGEWDEKF-CAINQEVHK 238
Cdd:COG0596   149 -------------------------------------------ARTDLRERLARITVPTLVIWGEKDPIVpPALARRLAE 185

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2036720018 239 MLPSSRIEIVPKAGHTVHVEQPRLFGKIVSEFLTS 273
Cdd:COG0596   186 LLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 9-272 2.62e-38

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 143.07  E-value: 2.62e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018    9 SDGVRYA--VADEGPNASEAVVC-LHGFTGSKQSWT-FLDEMLPDSRLIKIDCLGHGETDAPLNGKRYSTSRQVSD--LA 82
Cdd:PLN02980  1353 VDGFSCLikVHEVGQNAEGSVVLfLHGFLGTGEDWIpIMKAISGSARCISIDLPGHGGSKIQNHAKETQTEPTLSVelVA 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   83 EIFDQLKLH----KVKLIGYSMGGRLAYSFAMTYPERVSALVLESTTPGLKTLGERRERIMRDRKLADFILRDGLKAFVA 158
Cdd:PLN02980  1433 DLLYKLIEHitpgKVTLVGYSMGARIALYMALRFSDKIEGAVIISGSPGLKDEVARKIRSAKDDSRARMLIDHGLEIFLE 1512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  159 YWENIPLFSS---QQRLAEDIRHRIRSGRLRNnkigLANSLTGMGTGSQPSLWSRVEEIDVPVLLICGEWDEKFCAINQE 235
Cdd:PLN02980  1513 NWYSGELWKSlrnHPHFNKIVASRLLHKDVPS----LAKLLSDLSIGRQPSLWEDLKQCDTPLLLVVGEKDVKFKQIAQK 1588

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2036720018  236 V-HKMLPSSR-----------IEIVPKAGHTVHVEQPRLFGKIVSEFLT 272
Cdd:PLN02980  1589 MyREIGKSKEsgndkgkeiieIVEIPNCGHAVHLENPLPVIRALRKFLT 1637
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 27-274 3.29e-36

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 129.19  E-value: 3.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  27 VVCLHGFTGSKQSWTFLDEMLPDSRLIKIDCLGHGEtdaplngkrySTSRQVSDLAE----IFDQLKLHKVK---LIGYS 99
Cdd:PRK11126    5 LVFLHGLLGSGQDWQPVGEALPDYPRLYIDLPGHGG----------SAAISVDGFADvsrlLSQTLQSYNILpywLVGYS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 100 MGGRLAYSFAM-TYPERVSALVLESTTPGLKTLGERRERIMRDRKLADFILRDGLKAFVAYWENIPLFSS---QQRLAED 175
Cdd:PRK11126   75 LGGRIAMYYACqGLAGGLCGLIVEGGNPGLQNAEERQARWQNDRQWAQRFRQEPLEQVLADWYQQPVFASlnaEQRQQLV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 176 IRhrirsgRLRNNKIGLANSLTGMGTGSQPSLWSRVEEIDVPVLLICGEWDEKFCAINQEvHKmLPSSrieIVPKAGHTV 255
Cdd:PRK11126  155 AK------RSNNNGAAVAAMLEATSLAKQPDLRPALQALTFPFYYLCGERDSKFQALAQQ-LA-LPLH---VIPNAGHNA 223

                         250
                  ....*....|....*....
gi 2036720018 256 HVEQPRLFGKIVSEFLTSI 274
Cdd:PRK11126  224 HRENPAAFAASLAQILRLI 242
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 26-260 1.17e-29

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: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  26 AVVCLHGFTGSKQSWTFLDEMLPDS--RLIKIDCLGHGETDAPLNGKRYSTSRQVSDLAEIFDQLKLHKVKLIGYSMGGR 103
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDgfRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 104 LAYSFAMTYPERVSALVLEST-TPGLKTLGERRERIMRDRKLADFILRDGLKAFVAYWENIPLFSSQQRLAEDIRHRIRS 182
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAlDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 183 GRLRNNKIGLANSLtGMGTGSQPSLWSRVEE------IDVPVLLICGEWDEKFCAINQEV-HKMLPSSRIEIVPKAGHTV 255
Cdd:pfam00561 162 KRFPSGDYALAKSL-VTGALLFIETWSTELRakflgrLDEPTLIIWGDQDPLVPPQALEKlAQLFPNARLVVIPDAGHFA 240


                  ....*
gi 2036720018 256 HVEQP 260
Cdd:pfam00561 241 FLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-271 7.88e-22

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 93.47  E-value: 7.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  10 DGVRYAVADEGPNASEAVVCLHGFTGSKQSWTFLDEMLPDSR-LIKIDCLGHGETDAPLngKRYSTSRQVSDLAEIFDQL 88
Cdd:PRK14875  117 GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRpVIALDLPGHGASSKAV--GAGSLDELAAAVLAFLDAL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  89 KLHKVKLIGYSMGGRLAYSFAMTYPERVSALVLEST-----------TPGLKTLGERRErimrdrkladfiLRDGLKAFV 157
Cdd:PRK14875  195 GIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPaglgpeingdyIDGFVAAESRRE------------LKPVLELLF 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 158 AyweNIPLFSSQqrLAEDIRHRIR----SGRLRnnkiGLANSLTGMGTGSQpSLWSRVEEIDVPVLLICGEWDEKFCAIN 233
Cdd:PRK14875  263 A---DPALVTRQ--MVEDLLKYKRldgvDDALR----ALADALFAGGRQRV-DLRDRLASLAIPVLVIWGEQDRIIPAAH 332

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2036720018 234 QEvhkMLPS-SRIEIVPKAGHTVHVEQPRLFGKIVSEFL 271
Cdd:PRK14875  333 AQ---GLPDgVAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 43-272 4.07e-19

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: 83.95  E-value: 4.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  43 LDEMLPDSRLIKIDCLGHGETDAPlnGKRYSTSRQVSDLAEIFDQLKLHKVKLIGYSMGGRLAYSFAMTYPERVSALVLE 122
Cdd:TIGR02427  33 LPALTPDFRVLRYDKRGHGLSDAP--EGPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 123 STTPGLKTLGERRERImrdrklaDFILRDGLKAFV----AYWeniplFSSQQRLAEDIRHR-IRSGRLRNNKIGLANSLT 197
Cdd:TIGR02427 111 NTAAKIGTPESWNARI-------AAVRAEGLAALAdavlERW-----FTPGFREAHPARLDlYRNMLVRQPPDGYAGCCA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 198 GMGTGSqpsLWSRVEEIDVPVLLICGEWD-----EKFCAINQEVhkmlPSSRIEIVPKAGHTVHVEQPRLFGKIVSEFLT 272
Cdd:TIGR02427 179 AIRDAD---FRDRLGAIAVPTLCIAGDQDgstppELVREIADLV----PGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
3-261 5.73e-18

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 80.05  E-value: 5.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   3 TVNITVSDGVRYAVADEGPNASE--AVVCLHGFTGSKQSWTFLDEMLPDS--RLIKIDCLGHGETDAPLnGKRYSTSRQV 78
Cdd:COG2267     5 LVTLPTRDGLRLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEALAAAgyAVLAFDLRGHGRSDGPR-GHVDSFDDYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  79 SDLAEIFDQLKLH---KVKLIGYSMGGRLAYSFAMTYPERVSALVLESTtpglktlgerrerimrdrkladfilrdglka 155
Cdd:COG2267    84 DDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP------------------------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 156 fvAYWENiPLFSSQQRLAEDIRhrirsgrlrnnkiglansltgmgtgsqpsLWSRVEEIDVPVLLICGEWD--------E 227
Cdd:COG2267   133 --AYRAD-PLLGPSARWLRALR-----------------------------LAEALARIDVPVLVLHGGADrvvppeaaR 180

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2036720018 228 KFCAinqevhKMLPSSRIEIVPKAGHTVHVEQPR 261
Cdd:COG2267   181 RLAA------RLSPDVELVLLPGARHELLNEPAR 208
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
26-274 8.61e-15

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 71.90  E-value: 8.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  26 AVVCLHGFTGSKQSWTFLDEmlpdsRLIKIDCL-------GHGETDAPLNGKRYstSRQVSDLAEIFDQLKLH--KVKLI 96
Cdd:COG1647    17 GVLLLHGFTGSPAEMRPLAE-----ALAKAGYTvyaprlpGHGTSPEDLLKTTW--EDWLEDVEEAYEILKAGydKVIVI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  97 GYSMGGRLAYSFAMTYPErVSALVLEST-----------TPGLKTLGERRERIMRDRKLADfilrdglkAFVAYWENIPL 165
Cdd:COG1647    90 GLSMGGLLALLLAARYPD-VAGLVLLSPalkiddpsaplLPLLKYLARSLRGIGSDIEDPE--------VAEYAYDRTPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 166 FS--SQQRLAEDIRHRIrsgrlrnnkiglansltgmgtgsqpslwsrvEEIDVPVLLICGEWDEkfcAIN----QEVHKM 239
Cdd:COG1647   161 RAlaELQRLIREVRRDL-------------------------------PKITAPTLIIQSRKDE---VVPpesaRYIYER 206

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2036720018 240 LPSSRIEIV--PKAGH--TVHVEQPRLFGKIVsEFLTSI 274
Cdd:COG1647   207 LGSPDKELVwlEDSGHviTLDKDREEVAEEIL-DFLERL 244
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 59-258 7.19e-14

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: 69.17  E-value: 7.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  59 GHGETDaplnGKRY---STSRQVSDLAEIFDQLKLH----KVKLIGYSMGGRLAYSFAMTYPERVSALVLEST------- 124
Cdd:pfam12146  41 GHGRSD----GKRGhvpSFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPalkikpy 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 125 --TPGLKTLGERRERIMRD-----RKLADFILRDglKAFVAYWENIPLfssqqrlaedirhriRSGRLRnnkIGLANSLT 197
Cdd:pfam12146 117 laPPILKLLAKLLGKLFPRlrvpnNLLPDSLSRD--PEVVAAYAADPL---------------VHGGIS---ARTLYELL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2036720018 198 GMGtgsqPSLWSRVEEIDVPVLLICGEwDEKFCAI--NQEVHKMLPSS--RIEIVPKAGHTVHVE 258
Cdd:pfam12146 177 DAG----ERLLRRAAAITVPLLLLHGG-ADRVVDPagSREFYERAGSTdkTLKLYPGLYHELLNE 236
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 4-166 1.04e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 69.61  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   4 VNITVSDG--VRYAVADEGPNASEAVVCLHGftgsKQSWTFL-DEMLPD-----SRLIKIDCLGHGETDAPLNGKRYSTS 75
Cdd:PRK00870   24 VDVDDGDGgpLRMHYVDEGPADGPPVLLLHG----EPSWSYLyRKMIPIlaaagHRVIAPDLIGFGRSDKPTRREDYTYA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  76 RQVSDLAEIFDQLKLHKVKLIGYSMGGRLAYSFAMTYPERVSALVLESTtpGLKTlgerrerimrdrklADFILRDGLKA 155
Cdd:PRK00870  100 RHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT--GLPT--------------GDGPMPDAFWA 163

                         170
                  ....*....|.
gi 2036720018 156 FVAYWENIPLF 166
Cdd:PRK00870  164 WRAFSQYSPVL 174
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 27-263 1.75e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 62.11  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  27 VVCLHGFTgskQSWTFLDEMLPDS-RLIKIDCLGHGETDAPLngkrySTSRQVSDLAEIFDQLK-LHKVKLIGYSMGGRL 104
Cdd:pfam12697   1 VVLVHGAG---LSAAPLAALLAAGvAVLAPDLPGHGSSSPPP-----LDLADLADLAALLDELGaARPVVLVGHSLGGAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 105 AYSFAMTYPerVSALVLESTTPGLKTLGERRERIMRdrkladFILRDGLKAFVAYWENIPLFSSQQRLAEDIRHRIRSGR 184
Cdd:pfam12697  73 ALAAAAAAL--VVGVLVAPLAAPPGLLAALLALLAR------LGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLA 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2036720018 185 LRNNKIGlansltgmgtgsqPSLWSRVEEIDVPVLLICGEwDEKFCAINQEVHKMLPSSRIEIVPKAGHTVHvEQPRLF 263
Cdd:pfam12697 145 ALLAALA-------------LLPLAAWRDLPVPVLVLAEE-DRLVPELAQRLLAALAGARLVVLPGAGHLPL-DDPEEV 208
PRK05855 PRK05855
SDR family oxidoreductase;
6-88 8.73e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 61.92  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   6 ITVSDGVRYAVADEGPNASEAVVCLHGFTGSKQSWTFLDEMLPDS-RLIKIDCLGHGETDAPLNGKRYSTSRQVSDLAEI 84
Cdd:PRK05855    7 VVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRfRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAV 86


                  ....
gi 2036720018  85 FDQL 88
Cdd:PRK05855   87 IDAV 90
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 4-271 6.30e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 58.00  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   4 VNITVSDGVRYA----VADEGPNASEAVVCLHGFTGSK-QSWTFLDEM--------LPDSRlikidclGHGETDaplnGK 70
Cdd:COG1073    13 VTFKSRDGIKLAgdlyLPAGASKKYPAVVVAHGNGGVKeQRALYAQRLaelgfnvlAFDYR-------GYGESE----GE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  71 -RYSTSRQVSDLAEIFDQLKLH------KVKLIGYSMGGRLAYSFAMTYPeRVSALVLESTTPGLKTLGERRERIMRDRK 143
Cdd:COG1073    82 pREEGSPERRDARAAVDYLRTLpgvdpeRIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 144 LADFILRDGLkafvayweniplfssqqRLAEDIRHRIRSGrlrnnkiglansltgmgtgsqpslwSRVEEIDVPVLLICG 223
Cdd:COG1073   161 LPGVPYLPNV-----------------RLASLLNDEFDPL-------------------------AKIEKISRPLLFIHG 198

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2036720018 224 EWDEkfcAI----NQEVHKMLPSS-RIEIVPKAGH--TVHVEQPRLFGKIVsEFL 271
Cdd:COG1073   199 EKDE---AVpfymSEDLYEAAAEPkELLIVPGAGHvdLYDRPEEEYFDKLA-EFF 249
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 7-267 1.40e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 58.00  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   7 TVSDGVRY--AVADEGPNASEAVVCLHGFtGSKQSWTF--LDEMLPDSRLIKIDCLGHGETDAPlnGKRYSTSRQVSD-- 80
Cdd:PLN02894   86 SASNEPRFinTVTFDSKEDAPTLVMVHGY-GASQGFFFrnFDALASRFRVIAIDQLGWGGSSRP--DFTCKSTEETEAwf 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  81 ---LAEIFDQLKLHKVKLIGYSMGGRLAYSFAMTYPERVSALVLESTTpGLKTLGERR-ERIMRDR-----KLADF---- 147
Cdd:PLN02894  163 idsFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPA-GFSSESDDKsEWLTKFRatwkgAVLNHlwes 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 148 ------ILRdGL-------------KAFVAYWENIPLFSSQQRLAEDIRHRIRSGRlRNNKIGLaNSLTGMGTGSQPSLW 208
Cdd:PLN02894  242 nftpqkIIR-GLgpwgpnlvrryttARFGAHSTGDILSEEESKLLTDYVYHTLAAK-ASGELCL-KYIFSFGAFARKPLL 318

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2036720018 209 SRVEEIDVPVLLICG--EWDEKFCAINQEVHKMLPSSrIEIVPKAGHTVHVEQPRLFGKIV 267
Cdd:PLN02894  319 ESASEWKVPTTFIYGrhDWMNYEGAVEARKRMKVPCE-IIRVPQGGHFVFLDNPSGFHSAV 378
PRK10673 PRK10673
esterase;
19-274 3.70e-08

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 53.20  E-value: 3.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  19 EGPNASEAVVCLHGFTGSKQSWTFL-DEMLPDSRLIKIDCLGHGetdapLNGK----RYSTSRQvsDLAEIFDQLKLHKV 93
Cdd:PRK10673   11 QNPHNNSPIVLVHGLFGSLDNLGVLaRDLVNDHDIIQVDMRNHG-----LSPRdpvmNYPAMAQ--DLLDTLDALQIEKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  94 KLIGYSMGGRLAYSFAMTYPERVSALVLESTTP---------------------GLKTLGERRErIMRDRKLADFILRDG 152
Cdd:PRK10673   84 TFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPvdyhvrrhdeifaainavseaGATTRQQAAA-IMRQHLNEEGVIQFL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 153 LKAFV-AYWE-NIPLFSSQQrlaEDIrhrirsgrlrnnkIGlansltgmgtgsqpslWSRVEEIDVPVLLICGE----WD 226
Cdd:PRK10673  163 LKSFVdGEWRfNVPVLWDQY---PHI-------------VG----------------WEKIPAWPHPALFIRGGnspyVT 210

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2036720018 227 EKFcaiNQEVHKMLPSSRIEIVPKAGHTVHVEQPRLFGKIVSEFLTSI 274
Cdd:PRK10673  211 EAY---RDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLNDK 255
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 1-121 1.90e-07

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 51.42  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   1 MGTVNITVSDGVRYAVADEGPNASEAVVCLHGFtgSKQSWTFlDEMLP----DSRLIKIDCLGHGETDAPL--NGKRYST 74
Cdd:PLN03084  104 MGAQSQASSDLFRWFCVESGSNNNPPVLLIHGF--PSQAYSY-RKVLPvlskNYHAIAFDWLGFGFSDKPQpgYGFNYTL 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2036720018  75 SRQVSDLAEIFDQLKLHKVKLIGYSMGGRLAYSFAMTYPERVSALVL 121
Cdd:PLN03084  181 DEYVSSLESLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLIL 227
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 25-120 1.60e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 48.45  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  25 EAVVCLHGFTGSKQSW-TFLDEMLPDSRLIKIDCLGHGETDAPLNGKRYSTsrQVSDLAEIFDQLKLHKVKLIGYSMGGR 103
Cdd:PRK03592   28 DPIVFLHGNPTSSYLWrNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFAD--HARYLDAWFDALGLDDVVLVGHDWGSA 105

                          90
                  ....*....|....*..
gi 2036720018 104 LAYSFAMTYPERVSALV 120
Cdd:PRK03592  106 LGFDWAARHPDRVRGIA 122
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
6-271 2.54e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 47.32  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   6 ITVSDGVR-----YAVADEGPNAseAVVCLHGFTGSkQSWTFLDE-----------MLPDSRlikidclGHGETDAPLNG 69
Cdd:COG1506     2 FKSADGTTlpgwlYLPADGKKYP--VVVYVHGGPGS-RDDSFLPLaqalasrgyavLAPDYR-------GYGESAGDWGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  70 KrystsrQVSDLAEIFDQLKLH------KVKLIGYSMGGRLAYSFAMTYPERVSALVLESTTPGLKTLGERRERIMRdrk 143
Cdd:COG1506    72 D------EVDDVLAAIDYLAARpyvdpdRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTE--- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 144 ladFILRDGLKAFVAYWENIPLFssqqrlaedirhrirsgrlrnnkiglansltgmgtgsqpslwsRVEEIDVPVLLICG 223
Cdd:COG1506   143 ---RLMGGPWEDPEAYAARSPLA-------------------------------------------YADKLKTPLLLIHG 176

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2036720018 224 EWDEkFCAINQ--EVHKMLPSSRIE----IVPKAGHTVHVEQPRLFGKIVSEFL 271
Cdd:COG1506   177 EADD-RVPPEQaeRLYEALKKAGKPvellVYPGEGHGFSGAGAPDYLERILDFL 229
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 20-121 1.02e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 46.34  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  20 GPNASEAVVCLHGFTGSKQSWT------FLDEMLPDSRLIKIDCLGHGETDAPlNGKRYsTSRQVSDLAE--IFDQLKLH 91
Cdd:PLN03087  197 DNKAKEDVLFIHGFISSSAFWTetlfpnFSDAAKSTYRLFAVDLLGFGRSPKP-ADSLY-TLREHLEMIErsVLERYKVK 274

                          90       100       110
                  ....*....|....*....|....*....|
gi 2036720018  92 KVKLIGYSMGGRLAYSFAMTYPERVSALVL 121
Cdd:PLN03087  275 SFHIVAHSLGCILALALAVKHPGAVKSLTL 304
PLN02578 PLN02578
hydrolase
 12-273 1.07e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.99  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  12 VRYAVADEGPnaseAVVCLHGFTGSKQSWTF-LDEMLPDSRLIKIDCLGHGETDAPLngKRYST---SRQVSDLAEifDQ 87
Cdd:PLN02578   78 IHYVVQGEGL----PIVLIHGFGASAFHWRYnIPELAKKYKVYALDLLGFGWSDKAL--IEYDAmvwRDQVADFVK--EV 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  88 LKLHKVkLIGYSMGGRLAYSFAMTYPERVSALVLESTTPGLKTLGERRERIMRD-----RKLADFILRDGLKAFV---AY 159
Cdd:PLN02578  150 VKEPAV-LVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIVVeetvlTRFVVKPLKEWFQRVVlgfLF 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018 160 WEniplfsSQQrlaediRHRIRSGrLRNNKIG-------LANSLTG------------------MGTGSQPSLWSRVEEI 214
Cdd:PLN02578  229 WQ------AKQ------PSRIESV-LKSVYKDksnvddyLVESITEpaadpnagevyyrlmsrfLFNQSRYTLDSLLSKL 295

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2036720018 215 DVPVLLICGEWDEKFCAINQEVHKMLPSSRIEIVPKAGHTVHVEQPRLFGKIVSEFLTS 273
Cdd:PLN02578  296 SCPLLLLWGDLDPWVGPAKAEKIKAFYPDTTLVNLQAGHCPHDEVPEQVNKALLEWLSS 354
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
27-126 1.57e-05

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 45.01  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  27 VVCLHGFTGSKQSWTFLDEMLPDS-RLIKIDCLGHGETdaplngkRYSTSRQVSDLAEIFDQLKLHKVKLIGYSMGGRLA 105
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEELSSHfTLHLVDLPGFGRS-------RGFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVA 88

                          90       100
                  ....*....|....*....|.
gi 2036720018 106 YSFAMTYPERVSALVLESTTP 126
Cdd:PRK10349   89 SQIALTHPERVQALVTVASSP 109
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
27-159 5.63e-05

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 43.69  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  27 VVCLHGFTGSKQSW-------TFLDEM-----LPDSRLIKIDCLGHGETDAPLNG-----------------KRYSTSRQ 77
Cdd:COG2382   115 LYLLDGGGGDEQDWfdqgrlpTILDNLiaagkIPPMIVVMPDGGDGGDRGTEGPGndaferflaeelipfveKNYRVSAD 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  78 VSDLAeifdqlklhkvkLIGYSMGGRLAYSFAMTYPERVSALVLESttPGLKTLGERRERIMRDRKLADFILRDGLKAFV 157
Cdd:COG2382   195 PEHRA------------IAGLSMGGLAALYAALRHPDLFGYVGSFS--GSFWWPPGDADRGGWAELLAAGAPKKPLRFYL 260


                  ..
gi 2036720018 158 AY 159
Cdd:COG2382   261 DV 262
PRK08775 PRK08775
homoserine O-succinyltransferase;
51-123 1.26e-04

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 42.85  E-value: 1.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2036720018  51 RLIKIDCLG-HGETDAPLngkrySTSRQVSDLAEIFDQLKLHKVK-LIGYSMGGRLAYSFAMTYPERVSALVLES 123
Cdd:PRK08775  101 RLLAFDFIGaDGSLDVPI-----DTADQADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPARVRTLVVVS 170
YpfH COG0400
Predicted esterase [General function prediction only];
20-121 2.73e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  20 GPNASEAVVCLHGFTGSKQSWTFLDEML--PDSRLI----------------KIDCLGHGETDAPLNgkrySTSRQVSD- 80
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELalPGAAVLaprapvpegpggrawfDLSFLEGREDEEGLA----AAAEALAAf 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2036720018  81 LAEIFDQLKLH--KVKLIGYSMGGRLAYSFAMTYPERVSALVL 121
Cdd:COG0400    77 IDELEARYGIDpeRIVLAGFSQGAAMALSLALRRPELLAGVVA 119
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 27-120 4.18e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 39.04  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  27 VVCLHGFTGSKQSWTFLDEMLPDSRlIKIDCLGHGETDAPLNgkrySTSRQVSD-LAEIFDQLKLHKVKLIGYSMGGRLA 105
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAG-YPVYALNYPSTNGSIE----DSAEQLAAfVDAVLAATGAEKVDLVGHSMGGLVA 82

                          90
                  ....*....|....*..
gi 2036720018 106 YSFA--MTYPERVSALV 120
Cdd:COG1075    83 RYYLkrLGGAAKVARVV 99
PRK06489 PRK06489
hypothetical protein; Provisional
 6-151 5.13e-04

hypothetical protein; Provisional


Pssm-ID: 235815 [Multi-domain]  Cd Length: 360  Bit Score: 40.73  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018   6 ITVSDGVRYAVADEGPnaseAVVCLHGFTGSKQSW---TFLDEML-PDSRL-------IKIDCLGHGETDAPLNG----- 69
Cdd:PRK06489   55 TTLGTPHRNADGEIDN----AVLVLHGTGGSGKSFlspTFAGELFgPGQPLdaskyfiILPDGIGHGKSSKPSDGlraaf 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  70 KRYSTSRQVsdLAE---IFDQLKLHKVKLI-GYSMGGRLAYSFAMTYPERVSALVLESTTPglkTLGERRERIMRdRKLA 145
Cdd:PRK06489  131 PRYDYDDMV--EAQyrlVTEGLGVKHLRLIlGTSMGGMHAWMWGEKYPDFMDALMPMASQP---TEMSGRNWMWR-RMLI 204


                  ....*.
gi 2036720018 146 DFILRD 151
Cdd:PRK06489  205 ESIRND 210
COG4099 COG4099
Predicted peptidase [General function prediction only];
69-120 9.08e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.57  E-value: 9.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2036720018  69 GKRYSTSRQVSDLAEIFDQLKLH------KVKLIGYSMGGRLAYSFAMTYPERVSALV 120
Cdd:COG4099    97 DDYWSDTKALDAVLALLDDLIAEyridpdRIYLTGLSMGGYGTWDLAARYPDLFAAAV 154
homoserO_Ac_trn TIGR01392
homoserine O-acetyltransferase; This family describes homoserine-O-acetyltransferase, an ...
 82-126 1.66e-03

homoserine O-acetyltransferase; This family describes homoserine-O-acetyltransferase, an enzyme of methionine biosynthesis. This model has been rebuilt to identify sequences more broadly, including a number of sequences suggested to be homoserine O-acetyltransferase based on proximity to other Met biosynthesis genes. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273596 [Multi-domain]  Cd Length: 351  Bit Score: 39.21  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2036720018  82 AEIFDQLKLHKVKL-IGYSMGGRLAYSFAMTYPERVSALVLESTTP 126
Cdd:TIGR01392 117 KLLLDHLGIEQIAAvVGGSMGGMQALEWAIDYPERVRAIVVLATSA 162
metX PRK00175
homoserine O-acetyltransferase; Provisional
 82-125 1.78e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 39.40  E-value: 1.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2036720018  82 AEIFDQL---KLHKVklIGYSMGGRLAYSFAMTYPERV-SALVLESTT 125
Cdd:PRK00175  137 ARLLDALgitRLAAV--VGGSMGGMQALEWAIDYPDRVrSALVIASSA 182
MET2 COG2021
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ...
 65-126 3.24e-03

Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441624 [Multi-domain]  Cd Length: 355  Bit Score: 38.53  E-value: 3.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2036720018  65 APLNGKRYSTS------R-QVSDLAEIFDQL---KLHKVklIGYSMGGRLAYSFAMTYPERVSALVLESTTP 126
Cdd:COG2021    94 NPATGKPYGLDfpvvtiRdMVRAQKRLLDHLgieRLAAV--IGGSMGGMQALEWAVSYPDRVRRAIVIATAA 163
C80_toxinA_B-like cd20502
Peptidase C80 cysteine binding domain of Clostridium difficile toxins A and B, and related ...
 21-138 3.53e-03

Peptidase C80 cysteine binding domain of Clostridium difficile toxins A and B, and related proteins; This peptidase C80 family includes the major virulence factors of Clostridium difficile multidomain toxins TcdA and TcdB. These large homologous toxins contain several distinct domains including a cysteine protease domain (CPD) that autoproteolytically releases a cytotoxic effector domain upon binding of intracellular inositol hexakisphosphate. C. difficile is a major cause of intestinal tissue damage and inflammation, and TcdA is generally more inflammatory whereas TcdB is more cytotoxic; studies show that the CPD is an internal regulator of the proinflammatory activity. Site-directed mutagenesis has identified functional residues Asp/His/Cys in Clostridium toxin B.


Pssm-ID: 410975  Cd Length: 209  Bit Score: 37.69  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  21 PNASEAVVCLHGFTGSKQSW---TFLDEMLPDSRL-----IKIDCLGHGETD------APLNGKRYSTSrqvsdLAEIFD 86
Cdd:cd20502    26 PKNSEWLQLNDGEIADVLTWdggSIQEVYTIPLRLddegkVKLTLVGHGEDEfgtttfGGLNAEQLSTE-----LSSLFD 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  87 QLKLH------KVKLIGYSMggrLAYSFAM--TYPERVsALVLESTTPglkTLGERRERI 138
Cdd:cd20502   101 QIKLDikpksiKINLLGCNL---FDYSQNLeeTLPGQL-ALWLKSKSD---ALGISKEQI 153
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 55-159 4.28e-03

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 37.72  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036720018  55 IDCLGHGETDAPL-NGKRYSTSRQVSD-LAEIFDQLKLHKVKLIGYSMGGRLAYSFAMTYPERVSALVLESTTPGLKTLG 132
Cdd:pfam03096  61 VDAPGQEDGAASFpGGYPYPSMDDLADmLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWI 140

                          90       100
                  ....*....|....*....|....*...
gi 2036720018 133 ER-RERIMrDRKLADFILRDGLKAFVAY 159
Cdd:pfam03096 141 EWfYNKLS-SKLLYYYGMTDSAKDYLLA 167
 
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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