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Conserved domains on  [gi|499315415|ref|WP_011005907|]
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alpha/beta fold hydrolase [Pseudomonas putida]

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, ...
 12-276 4.85e-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: 151.69  E-value: 4.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  12 REILAAGYRTNLHDQG-EGFPALLIHGsgpasppGPTGAGSFRS-----SQTRRVIAPDMLGFGYSERPADGkYSQARWV 85
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHG-------LPGSSYEWRPlipalAAGYRVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  86 EHAIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVlmgsvgvsfpitagletawgytpslanmrrlldlfahd 165
Cdd:COG0596   77 DDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV-------------------------------------- 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 166 rtLVNDELAELRYQASIRPGFQESFAAMFPPPRQNGVDDlasnetDIRALPNETLVIHGREDRIIPLQASLTLAQWIPNA 245
Cdd:COG0596  119 --LVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRE------RLARITVPTLVIWGEKDPIVPPALARRLAELLPNA 190

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499315415 246 QLHVFGQCGHWTQIEHAERFARLVENFLAEA 276
Cdd:COG0596  191 ELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 12-276 4.85e-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: 151.69  E-value: 4.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  12 REILAAGYRTNLHDQG-EGFPALLIHGsgpasppGPTGAGSFRS-----SQTRRVIAPDMLGFGYSERPADGkYSQARWV 85
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHG-------LPGSSYEWRPlipalAAGYRVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  86 EHAIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVlmgsvgvsfpitagletawgytpslanmrrlldlfahd 165
Cdd:COG0596   77 DDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV-------------------------------------- 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 166 rtLVNDELAELRYQASIRPGFQESFAAMFPPPRQNGVDDlasnetDIRALPNETLVIHGREDRIIPLQASLTLAQWIPNA 245
Cdd:COG0596  119 --LVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRE------RLARITVPTLVIWGEKDPIVPPALARRLAELLPNA 190

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499315415 246 QLHVFGQCGHWTQIEHAERFARLVENFLAEA 276
Cdd:COG0596  191 ELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 31-262 1.74e-42

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: 145.73  E-value: 1.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415   31 PALLIHGSGPASPPGPTGAGSFRSSQTRRVIAPDMLGFGYSERPAD----GKYSQARWVEHaigVLDALGIQQGDIVGNS 106
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAqddyRTDDLAEDLEY---ILEALGLEKVNLVGHS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  107 FGGGLALALAIRHPERVRRLVLMGSVGVSFPITAGLETAWGYTPSLANMRRLLDLFAHDRTLVNDELAELRYQASIR--- 183
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLkal 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  184 PGFQESFAAMFPPPRQNGVDDLASNETDIRALPNE---------TLVIHGREDRIIPLQASLTLAQWIPNAQLHVFGQCG 254
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAkflgrldepTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237


                  ....*...
gi 499315415  255 HWTQIEHA 262
Cdd:pfam00561 238 HFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 27-276 2.56e-30

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 116.58  E-value: 2.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  27 GEGFPALLIHGSG----------PASPPGptgagsfrssqtRRVIAPDMLGFGYSE-RPADGKYSQ-ARWVehaIGVLDA 94
Cdd:PRK14875 129 GDGTPVVLIHGFGgdlnnwlfnhAALAAG------------RPVIALDLPGHGASSkAVGAGSLDElAAAV---LAFLDA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  95 LGIQQGDIVGNSFGGGLALALAIRHPERVRRLVLMGSVGVSFPI----TAGLETAwgytPSLANMRRLLDLFAHDRTLVN 170
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEIngdyIDGFVAA----ESRRELKPVLELLFADPALVT 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 171 DELAE--LRY-QASIRPGFQESFA-AMFPPPRQngVDDLASnetDIRALPNETLVIHGREDRIIPLQASLTLAqwiPNAQ 246
Cdd:PRK14875 270 RQMVEdlLKYkRLDGVDDALRALAdALFAGGRQ--RVDLRD---RLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVA 341

                        250       260       270
                 ....*....|....*....|....*....|
gi 499315415 247 LHVFGQCGHWTQIEHAERFARLVENFLAEA 276
Cdd:PRK14875 342 VHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 83-128 2.65e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 38.76  E-value: 2.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499315415  83 RWVEHAIGVLDALG--IQQGD---IVGNSFGGGLALALAIRHPERVRRLVL 128
Cdd:cd12808  168 RWLGTDALTLAAYDalLDRVGpciVVAHSQGGGFAFEAARARPDLVRAVVA 218
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 12-276 4.85e-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: 151.69  E-value: 4.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  12 REILAAGYRTNLHDQG-EGFPALLIHGsgpasppGPTGAGSFRS-----SQTRRVIAPDMLGFGYSERPADGkYSQARWV 85
Cdd:COG0596    5 RFVTVDGVRLHYREAGpDGPPVVLLHG-------LPGSSYEWRPlipalAAGYRVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  86 EHAIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVlmgsvgvsfpitagletawgytpslanmrrlldlfahd 165
Cdd:COG0596   77 DDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV-------------------------------------- 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 166 rtLVNDELAELRYQASIRPGFQESFAAMFPPPRQNGVDDlasnetDIRALPNETLVIHGREDRIIPLQASLTLAQWIPNA 245
Cdd:COG0596  119 --LVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRE------RLARITVPTLVIWGEKDPIVPPALARRLAELLPNA 190

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499315415 246 QLHVFGQCGHWTQIEHAERFARLVENFLAEA 276
Cdd:COG0596  191 ELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 31-262 1.74e-42

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: 145.73  E-value: 1.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415   31 PALLIHGSGPASPPGPTGAGSFRSSQTRRVIAPDMLGFGYSERPAD----GKYSQARWVEHaigVLDALGIQQGDIVGNS 106
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAqddyRTDDLAEDLEY---ILEALGLEKVNLVGHS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  107 FGGGLALALAIRHPERVRRLVLMGSVGVSFPITAGLETAWGYTPSLANMRRLLDLFAHDRTLVNDELAELRYQASIR--- 183
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLkal 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  184 PGFQESFAAMFPPPRQNGVDDLASNETDIRALPNE---------TLVIHGREDRIIPLQASLTLAQWIPNAQLHVFGQCG 254
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAkflgrldepTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237


                  ....*...
gi 499315415  255 HWTQIEHA 262
Cdd:pfam00561 238 HFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 27-276 2.56e-30

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 116.58  E-value: 2.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  27 GEGFPALLIHGSG----------PASPPGptgagsfrssqtRRVIAPDMLGFGYSE-RPADGKYSQ-ARWVehaIGVLDA 94
Cdd:PRK14875 129 GDGTPVVLIHGFGgdlnnwlfnhAALAAG------------RPVIALDLPGHGASSkAVGAGSLDElAAAV---LAFLDA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  95 LGIQQGDIVGNSFGGGLALALAIRHPERVRRLVLMGSVGVSFPI----TAGLETAwgytPSLANMRRLLDLFAHDRTLVN 170
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEIngdyIDGFVAA----ESRRELKPVLELLFADPALVT 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 171 DELAE--LRY-QASIRPGFQESFA-AMFPPPRQngVDDLASnetDIRALPNETLVIHGREDRIIPLQASLTLAqwiPNAQ 246
Cdd:PRK14875 270 RQMVEdlLKYkRLDGVDDALRALAdALFAGGRQ--RVDLRD---RLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVA 341

                        250       260       270
                 ....*....|....*....|....*....|
gi 499315415 247 LHVFGQCGHWTQIEHAERFARLVENFLAEA 276
Cdd:PRK14875 342 VHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
19-275 5.85e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 71.96  E-value: 5.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  19 YRTNLHDQGEGFPALLIHGSGpasppgpTGAGSFRSSQTR------RVIAPDMLGFGYSERPADGKYSQARWVEHAIGVL 92
Cdd:COG2267   18 GRRWRPAGSPRGTVVLVHGLG-------EHSGRYAELAEAlaaagyAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAAL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  93 DALGIQQGD---IVGNSFGGGLALALAIRHPERVRRLVLMGSVGVSFPItagletaWGYTPSLanmrrLLDLFAHDRtlv 169
Cdd:COG2267   91 DALRARPGLpvvLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPL-------LGPSARW-----LRALRLAEA--- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 170 ndeLAELRyqasirpgfqesfaamfppprqngvddlasnetdiraLPneTLVIHGREDRIIPLQASLTLAQ-WIPNAQLH 248
Cdd:COG2267  156 ---LARID-------------------------------------VP--VLVLHGGADRVVPPEAARRLAArLSPDVELV 193

                        250       260
                 ....*....|....*....|....*...
gi 499315415 249 VFGQCGHWTQIEHA-ERFARLVENFLAE 275
Cdd:COG2267  194 LLPGARHELLNEPArEEVLAAILAWLER 221
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 24-129 1.14e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 66.56  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  24 HDQGEGFPALLIHGSgpasppgPTGAGSFRS-----SQTRRVIAPDMLGFGYSERPaDGKYS---QARWVEhaiGVLDAL 95
Cdd:PRK03592  22 IETGEGDPIVFLHGN-------PTSSYLWRNiiphlAGLGRCLAPDLIGMGASDKP-DIDYTfadHARYLD---AWFDAL 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499315415  96 GIQQGDIVGNSFGGGLALALAIRHPERVRRLVLM 129
Cdd:PRK03592  91 GLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFM 124
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
25-275 3.58e-12

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 64.65  E-value: 3.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  25 DQGEGFPA-LLIHGsgpasppGPTGAGSFRSSQTRR-------VIAPDMLGFGYSERPADGKysqarWVEHAIGVLDALg 96
Cdd:COG1506   18 ADGKKYPVvVYVHG-------GPGSRDDSFLPLAQAlasrgyaVLAPDYRGYGESAGDWGGD-----EVDDVLAAIDYL- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  97 IQQGD-------IVGNSFGGGLALALAIRHPERVRRLVLMGSVgvsfpitagletawgytpslANMRRLLDLFAHDRTLV 169
Cdd:COG1506   85 AARPYvdpdrigIYGHSYGGYMALLAAARHPDRFKAAVALAGV--------------------SDLRSYYGTTREYTERL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 170 NDELAELRyqasirpgfqESFAAMfppprqngvddlaSNETDIRALPNETLVIHGREDRIIPLQASLTLAQWI----PNA 245
Cdd:COG1506  145 MGGPWEDP----------EAYAAR-------------SPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALkkagKPV 201

                        250       260       270
                 ....*....|....*....|....*....|
gi 499315415 246 QLHVFGQCGHWTQIEHAERFARLVENFLAE 275
Cdd:COG1506  202 ELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PLN02578 PLN02578
hydrolase
 26-133 4.20e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 65.63  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  26 QGEGFPALLIHGsgpasppgpTGAGSF-------RSSQTRRVIAPDMLGFGYSERpADGKYSQARWVEHAIGVLDALGIQ 98
Cdd:PLN02578  83 QGEGLPIVLIHG---------FGASAFhwrynipELAKKYKVYALDLLGFGWSDK-ALIEYDAMVWRDQVADFVKEVVKE 152

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499315415  99 QGDIVGNSFGGGLALALAIRHPERVRRLVLMGSVG 133
Cdd:PLN02578 153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAG 187
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 33-268 1.04e-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: 62.88  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415   33 LLIHGSGpasppgpTGAGSFRSSQTRRV--IAPDMLGFGYSERPADGkYSQARWVEHAIGVLDALGiqQGDIVGNSFGGG 110
Cdd:pfam12697   2 VLVHGAG-------LSAAPLAALLAAGVavLAPDLPGHGSSSPPPLD-LADLADLAALLDELGAAR--PVVLVGHSLGGA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  111 LALALAIRHperVRRLVLMGSVGVSFPITAGLETAWGYTPSLANMRRLLDLFAHDRTLVNDELAELRYQASIRPGFQESF 190
Cdd:pfam12697  72 VALAAAAAA---LVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499315415  191 AAMFPPPRqngvddlasnetDIRALPNETLVIHGrEDRIIPLQASLTLAQWiPNAQLHVFGQCGHWTQiEHAERFARL 268
Cdd:pfam12697 149 ALALLPLA------------AWRDLPVPVLVLAE-EDRLVPELAQRLLAAL-AGARLVVLPGAGHLPL-DDPEEVAEA 211
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 26-129 1.54e-11

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 63.45  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  26 QGEGFPALLIHGSgpasppgPTGAGSFR------SSQTRRVIAPDMLGFGYSERPAD-GKYSQARWVEHAIGVLDALGIQ 98
Cdd:PRK00870  43 PADGPPVLLLHGE-------PSWSYLYRkmipilAAAGHRVIAPDLIGFGRSDKPTRrEDYTYARHVEWMRSWFEQLDLT 115

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499315415  99 QGDIVGNSFGGGLALALAIRHPERVRRLVLM 129
Cdd:PRK00870 116 DVTLVCQDWGGLIGLRLAAEHPDRFARLVVA 146
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 51-270 7.26e-11

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 62.13  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  51 SFRSSQTRRVIAPDMLGFGYSERPADGKYSQARWVEH-AIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVLM 129
Cdd:PLN03087 226 SDAAKSTYRLFAVDLLGFGRSPKPADSLYTLREHLEMiERSVLERYKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLL 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 130 ---------GSVGVSF------------PITAGLETAWGYtpslANMRRL--LDLFAHDRTLvnDELAELRYQASIRPGF 186
Cdd:PLN03087 306 appyypvpkGVQATQYvmrkvaprrvwpPIAFGASVACWY----EHISRTicLVICKNHRLW--EFLTRLLTRNRMRTFL 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 187 QESF------AAMFppPRQNGVDDLASN-----ETDIRALPNETLVIHGREDRIIPLQASLTLAQWIPNAQLHVFGQCGH 255
Cdd:PLN03087 380 IEGFfchthnAAWH--TLHNIICGSGSKldgylDHVRDQLKCDVAIFHGGDDELIPVECSYAVKAKVPRARVKVIDDKDH 457

                        250
                 ....*....|....*.
gi 499315415 256 WTQIEHAER-FARLVE 270
Cdd:PLN03087 458 ITIVVGRQKeFARELE 473
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
60-278 2.51e-10

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 59.18  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  60 VIAPDMLGFGysERPAD-GKYSQARWVEHAIGVLDALGiQQGD---IVGNSFGGGLALALAIRHPErVRRLVLMGsvgvs 135
Cdd:COG1647   45 VYAPRLPGHG--TSPEDlLKTTWEDWLEDVEEAYEILK-AGYDkviVIGLSMGGLLALLLAARYPD-VAGLVLLS----- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 136 fpitagleTAWGYTPSLANMRRLLDLFAHD-RTLVNDELAELRYQASIRPGFQESFAAMfppprQNGVDDLASNETDIRA 214
Cdd:COG1647  116 --------PALKIDDPSAPLLPLLKYLARSlRGIGSDIEDPEVAEYAYDRTPLRALAEL-----QRLIREVRRDLPKITA 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499315415 215 lPneTLVIHGREDRIIPLQASLTLAQWI--PNAQLHVFGQCGHW-TQIEHAERFARLVENFLAEADA 278
Cdd:COG1647  183 -P--TLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHViTLDKDREEVAEEILDFLERLAA 246
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 20-128 1.44e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 54.48  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  20 RTNLHDQGEGFPALLIHGSgpasppgPTGAGSFRSSQTR-----RVIAPDMLGFGYSERPADGKYSQArwvEHA--IG-V 91
Cdd:PRK03204  25 RIHYIDEGTGPPILLCHGN-------PTWSFLYRDIIVAlrdrfRCVAPDYLGFGLSERPSGFGYQID---EHArvIGeF 94

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499315415  92 LDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVL 128
Cdd:PRK03204  95 VDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVL 131
PRK10673 PRK10673
esterase;
56-275 3.08e-08

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 53.20  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  56 QTRRVIAPDMLGFGYSERPADGKYSQArwVEHAIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVLMGSVGVS 135
Cdd:PRK10673  41 NDHDIIQVDMRNHGLSPRDPVMNYPAM--AQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVD 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 136 FPItagletawgytpslanmRRLLDLFAHDRTlVNDELAELRYQAS--IRPGFQESFAAMF-------------PPPRQN 200
Cdd:PRK10673 119 YHV-----------------RRHDEIFAAINA-VSEAGATTRQQAAaiMRQHLNEEGVIQFllksfvdgewrfnVPVLWD 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499315415 201 GVDDLASNETdIRALPNETLVIHGREDRIIPLQASLTLAQWIPNAQLHVFGQCGHWTQIEHAERFARLVENFLAE 275
Cdd:PRK10673 181 QYPHIVGWEK-IPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLND 254
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 60-255 6.08e-08

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: 52.22  E-value: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415   60 VIAPDMLGFGYSerpaDGKY----SQARWVEHAIGVLDALGIQQGD----IVGNSFGGGLALALAIRHPERVRRLVL--- 128
Cdd:pfam12146  34 VYAYDHRGHGRS----DGKRghvpSFDDYVDDLDTFVDKIREEHPGlplfLLGHSMGGLIAALYALRYPDKVDGLILsap 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  129 MGSVGVSFPITAGLETAWGYTPSLANMR----RLLDLFAHDRTLV----NDELaelrYQASIRPGFqesFAAMFppprqN 200
Cdd:pfam12146 110 ALKIKPYLAPPILKLLAKLLGKLFPRLRvpnnLLPDSLSRDPEVVaayaADPL----VHGGISART---LYELL-----D 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499315415  201 GVDDLASNETDIRaLPneTLVIHGREDRIIPLQASLTLAQWIPNA--QLHVFGQCGH 255
Cdd:pfam12146 178 AGERLLRRAAAIT-VP--LLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPGLYH 231
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 59-135 1.56e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 51.83  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  59 RVIAPDMLGFGYSERP----ADGKYSQARWVEHAIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVLMGSVGV 134
Cdd:PLN02894 133 RVIAIDQLGWGGSSRPdftcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGF 212


                 .
gi 499315415 135 S 135
Cdd:PLN02894 213 S 213
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 31-255 1.64e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 51.76  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  31 PALLIHGSGPASPPGPTGAGSFRSSQTrrVIAPDMLGFGYSERPADGKYSQARWVEHAIGVLDALGIQQGDIVGNSFgGG 110
Cdd:PLN02679  90 PVLLVHGFGASIPHWRRNIGVLAKNYT--VYAIDLLGFGASDKPPGFSYTMETWAELILDFLEEVVQKPTVLIGNSV-GS 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 111 LA--LALAIRHPERVRRLVLMGSVG----------------------VSF-----PITAGLetaWGYTPSLANMRRLLDL 161
Cdd:PLN02679 167 LAcvIAASESTRDLVRGLVLLNCAGgmnnkavvddwriklllpllwlIDFllkqrGIASAL---FNRVKQRDNLKNILLS 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 162 FAHDRTLVNDELAELRYQASIRPGFQESFAAMFP-PPRQNGVddlasneTDIRALPNETLVIHGREDRIIPLQASL---- 236
Cdd:PLN02679 244 VYGNKEAVDDELVEIIRGPADDEGALDAFVSIVTgPPGPNPI-------KLIPRISLPILVLWGDQDPFTPLDGPVgkyf 316

                        250       260
                 ....*....|....*....|
gi 499315415 237 -TLAQWIPNAQLHVFGQCGH 255
Cdd:PLN02679 317 sSLPSQLPNVTLYVLEGVGH 336
metX PRK00175
homoserine O-acetyltransferase; Provisional
 57-131 1.82e-07

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 51.73  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  57 TRR--VIAPDMLG--FGY----SERPADGKYSQAR--------WVEHAIGVLDALGIQQ-GDIVGNSFGGGLALALAIRH 119
Cdd:PRK00175  89 TDRyfVICSNVLGgcKGStgpsSINPDTGKPYGSDfpvitirdWVRAQARLLDALGITRlAAVVGGSMGGMQALEWAIDY 168

                         90
                 ....*....|..
gi 499315415 120 PERVRRLVLMGS 131
Cdd:PRK00175 169 PDRVRSALVIAS 180
PRK08775 PRK08775
homoserine O-succinyltransferase;
45-128 1.83e-07

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 51.33  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  45 GPTGAGSFRSSQTRRVIAPDMLGFGYSERPADGKYSQARwvehAIG-VLDALGIQQGD-IVGNSFGGGLALALAIRHPER 122
Cdd:PRK08775  87 GLVGSGRALDPARFRLLAFDFIGADGSLDVPIDTADQAD----AIAlLLDALGIARLHaFVGYSYGALVGLQFASRHPAR 162


                 ....*.
gi 499315415 123 VRRLVL 128
Cdd:PRK08775 163 VRTLVV 168
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 31-140 6.33e-06

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 46.80  E-value: 6.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  31 PALLIHGSgpasppgPTGAGSFRS-----SQTRRVIAPDMLGFGYSERPADG---KYSQARWVEHAIGVLDALGIQQGDI 102
Cdd:PLN03084 129 PVLLIHGF-------PSQAYSYRKvlpvlSKNYHAIAFDWLGFGFSDKPQPGygfNYTLDEYVSSLESLIDELKSDKVSL 201

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499315415 103 VGNSFGGGLALALAIRHPERVRRLVLMGSvgvsfPITA 140
Cdd:PLN03084 202 VVQGYFSPPVVKYASAHPDKIKKLILLNP-----PLTK 234
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 60-245 9.20e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 46.06  E-value: 9.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  60 VIAPDMLGFGYSErpadGKYSQARWVEH--AIGVLDAL----GIQQGDIV--GNSFGGGLALALAIRHPeRVRRLVLMGs 131
Cdd:COG1073   67 VLAFDYRGYGESE----GEPREEGSPERrdARAAVDYLrtlpGVDPERIGllGISLGGGYALNAAATDP-RVKAVILDS- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415 132 vgvsfpitagletawGYTpSLANM-RRLLDLFAHDRTLVNDELAELRYQASIRPGFqesfaamfppprqngvddlaSNET 210
Cdd:COG1073  141 ---------------PFT-SLEDLaAQRAKEARGAYLPGVPYLPNVRLASLLNDEF--------------------DPLA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 499315415 211 DIRALPNETLVIHGREDRIIPLQASLTLAQ---------WIPNA 245
Cdd:COG1073  185 KIEKISRPLLFIHGEKDEAVPFYMSEDLYEaaaepkellIVPGA 228
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 27-194 7.42e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 43.57  E-value: 7.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  27 GEGFPALLIHGSGpasppgpTGAGSFRS-----SQTRRVIAPDMLGFGYSERP------ADGKYSQARWVEHAIGVLDAL 95
Cdd:PLN02824  27 TSGPALVLVHGFG-------GNADHWRKntpvlAKSHRVYAIDLLGYGYSDKPnprsapPNSFYTFETWGEQLNDFCSDV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315415  96 GIQQGDIVGNSFGGGLALALAIRHPERVRRLVLMgsvGVSFPITAGLETAWGYTPSLANMRRLL-------DLFA----- 163
Cdd:PLN02824 100 VGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLI---NISLRGLHIKKQPWLGRPFIKAFQNLLretavgkAFFKsvatp 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 499315415 164 -----------HDRTLVNDELAelryQASIRPGFQESFAAMF 194
Cdd:PLN02824 177 etvknilcqcyHDDSAVTDELV----EAILRPGLEPGAVDVF 214
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 83-128 2.65e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 38.76  E-value: 2.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499315415  83 RWVEHAIGVLDALG--IQQGD---IVGNSFGGGLALALAIRHPERVRRLVL 128
Cdd:cd12808  168 RWLGTDALTLAAYDalLDRVGpciVVAHSQGGGFAFEAARARPDLVRAVVA 218
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
60-121 8.10e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 36.87  E-value: 8.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499315415  60 VIAPDMLGFGYSERPAD------GKYSQARWVEHAIGVLDALGiQQGD-------IVGNSFGGGLALALAIRHPE 121
Cdd:COG0412   59 VLAPDLYGRGGPGDDPDearalmGALDPELLAADLRAALDWLK-AQPEvdagrvgVVGFCFGGGLALLAAARGPD 132
 
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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