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Conserved domains on  [gi|1263436545|gb|PGA03130.1|]
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alpha/beta hydrolase [Bacillus toyonensis]

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, ...
 5-299 3.23e-54

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: 175.96  E-value: 3.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545   5 ATMEFVSLsNGETIAYQEVGRrNTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIDSLQDFAEDV 84
Cdd:COG0596     2 STPRFVTV-DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  85 KLFIDQLKLEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVesvgmkgypifkkdingepivsslvktkeeiaqdpvqiA 164
Cdd:COG0596    80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV--------------------------------------D 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 165 PVLDAIKNMnklyyrtvwnlliythnqpepdryekYLDDMLTQRNFVDVNYALITFNISDehngvvegnkQIHRIKTPTL 244
Cdd:COG0596   122 EVLAALAEP--------------------------LRRPGLAPEALAALLRALARTDLRE----------RLARITVPTL 165

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1263436545 245 VIQGDRDYVVPQVVGEELAKHLPNAKLQVLEDCGHSPFIDCLDVFINHVENWLEQ 299
Cdd:COG0596   166 VIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 5-299 3.23e-54

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: 175.96  E-value: 3.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545   5 ATMEFVSLsNGETIAYQEVGRrNTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIDSLQDFAEDV 84
Cdd:COG0596     2 STPRFVTV-DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  85 KLFIDQLKLEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVesvgmkgypifkkdingepivsslvktkeeiaqdpvqiA 164
Cdd:COG0596    80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV--------------------------------------D 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 165 PVLDAIKNMnklyyrtvwnlliythnqpepdryekYLDDMLTQRNFVDVNYALITFNISDehngvvegnkQIHRIKTPTL 244
Cdd:COG0596   122 EVLAALAEP--------------------------LRRPGLAPEALAALLRALARTDLRE----------RLARITVPTL 165

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1263436545 245 VIQGDRDYVVPQVVGEELAKHLPNAKLQVLEDCGHSPFIDCLDVFINHVENWLEQ 299
Cdd:COG0596   166 VIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 30-284 2.64e-30

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 114.52  E-value: 2.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQ-NQYHIYALDLRGFGQSTYNKSIDSLQ--DFAEDVKLFIDQLKLEKFSLMGWSMGGG 106
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAQDDYRtdDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 107 VAMQFTANHPTFVEKLILVESVGMKGYPIFKKdingEPIVSSLVKTKEEIAQDPVQIAPVLDAIKNMNKLYYRtvWNLLI 186
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEAD----RFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLR--LRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 187 ythnqPEPDRYEKYLDDMLTQRNFVDVNYAL--ITFNISDEHngvvegnKQIHRIKTPTLVIQGDRDYVVPQVVGEELAK 264
Cdd:pfam00561 156 -----ALPLLNKRFPSGDYALAKSLVTGALLfiETWSTELRA-------KFLGRLDEPTLIIWGDQDPLVPPQALEKLAQ 223

                         250       260
                  ....*....|....*....|
gi 1263436545 265 HLPNAKLQVLEDCGHSPFID 284
Cdd:pfam00561 224 LFPNARLVVIPDAGHFAFLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 15-281 1.28e-26

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 107.34  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  15 GETIAYQEVGRRNTETLVLIHGnmtssqhF--DL-----VIEKLQNQYHIYALDLRGFGQSTYNKSIDSLQDFAEDVKLF 87
Cdd:PRK14875  118 GRTVRYLRLGEGDGTPVVLIHG-------FggDLnnwlfNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAF 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  88 IDQLKLEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVESVGMkGypifkKDINGEPIvSSLVKtkeeiAQDPVQIAPVL 167
Cdd:PRK14875  191 LDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGL-G-----PEINGDYI-DGFVA-----AESRRELKPVL 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 168 DaiknmnKLYyrtvwnlliytHNQPEPDRyeKYLDDMLTQRNFVDVNYAL--ITFNISDEHNGVVEGNKQIHRIKTPTLV 245
Cdd:PRK14875  259 E------LLF-----------ADPALVTR--QMVEDLLKYKRLDGVDDALraLADALFAGGRQRVDLRDRLASLAIPVLV 319

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1263436545 246 IQGDRDYVVPQVVGEELAkhlPNAKLQVLEDCGHSP 281
Cdd:PRK14875  320 IWGEQDRIIPAAHAQGLP---DGVAVHVLPGAGHMP 352
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 30-289 1.67e-17

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: 80.09  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIDSLQDFAEDVKLFIDQLKLEKFSLMGWSMGGGVAM 109
Cdd:TIGR02427  15 VLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 110 QFTANHPTFVEKLILVESVGMKGYPifkkdingEPIVSSLVKTKEEiaqdpvQIAPVLDAIknMNKLY---YRtvwnlli 186
Cdd:TIGR02427  95 GLAARRPDRVRALVLSNTAAKIGTP--------ESWNARIAAVRAE------GLAALADAV--LERWFtpgFR------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 187 ythnQPEPDRYEKYlDDMLTQRN---FVDVNYALITFNISDehngvvegnkQIHRIKTPTLVIQGDRDYVVPQVVGEELA 263
Cdd:TIGR02427 152 ----EAHPARLDLY-RNMLVRQPpdgYAGCCAAIRDADFRD----------RLGAIAVPTLCIAGDQDGSTPPELVREIA 216

                         250       260
                  ....*....|....*....|....*.
gi 1263436545 264 KHLPNAKLQVLEDCGHSPFIDCLDVF 289
Cdd:TIGR02427 217 DLVPGARFAEIRGAGHIPCVEQPEAF 242
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 5-299 3.23e-54

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: 175.96  E-value: 3.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545   5 ATMEFVSLsNGETIAYQEVGRrNTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIDSLQDFAEDV 84
Cdd:COG0596     2 STPRFVTV-DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  85 KLFIDQLKLEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVesvgmkgypifkkdingepivsslvktkeeiaqdpvqiA 164
Cdd:COG0596    80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV--------------------------------------D 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 165 PVLDAIKNMnklyyrtvwnlliythnqpepdryekYLDDMLTQRNFVDVNYALITFNISDehngvvegnkQIHRIKTPTL 244
Cdd:COG0596   122 EVLAALAEP--------------------------LRRPGLAPEALAALLRALARTDLRE----------RLARITVPTL 165

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1263436545 245 VIQGDRDYVVPQVVGEELAKHLPNAKLQVLEDCGHSPFIDCLDVFINHVENWLEQ 299
Cdd:COG0596   166 VIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 30-284 2.64e-30

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 114.52  E-value: 2.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQ-NQYHIYALDLRGFGQSTYNKSIDSLQ--DFAEDVKLFIDQLKLEKFSLMGWSMGGG 106
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAQDDYRtdDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 107 VAMQFTANHPTFVEKLILVESVGMKGYPIFKKdingEPIVSSLVKTKEEIAQDPVQIAPVLDAIKNMNKLYYRtvWNLLI 186
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEAD----RFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLR--LRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 187 ythnqPEPDRYEKYLDDMLTQRNFVDVNYAL--ITFNISDEHngvvegnKQIHRIKTPTLVIQGDRDYVVPQVVGEELAK 264
Cdd:pfam00561 156 -----ALPLLNKRFPSGDYALAKSLVTGALLfiETWSTELRA-------KFLGRLDEPTLIIWGDQDPLVPPQALEKLAQ 223

                         250       260
                  ....*....|....*....|
gi 1263436545 265 HLPNAKLQVLEDCGHSPFID 284
Cdd:pfam00561 224 LFPNARLVVIPDAGHFAFLE 243
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
4-299 1.09e-27

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 107.01  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545   4 PATMEFVSLSNGETIAYQEVGRRNTE--TLVLIHGNMTSSQHFDLVIEKLQNQ-YHIYALDLRGFGQSTYNKS-IDSLQD 79
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGhVDSFDD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  80 FAEDVKLFIDQLKLE---KFSLMGWSMGGGVAMQFTANHPTFVEKLILVESvgmkgypifkkdingepivsslvktkeEI 156
Cdd:COG2267    82 YVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP---------------------------AY 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 157 AQDPVQIAPVldaiknmnklyyrtvwnlliythnqpepdryeKYLDDMLTQRNfvdvnyalitfnisdehngvvegnkqI 236
Cdd:COG2267   135 RADPLLGPSA--------------------------------RWLRALRLAEA--------------------------L 156

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263436545 237 HRIKTPTLVIQGDRDYVVPQVVGEELAKHL-PNAKLQVLEDCGHSPFID-CLDVFINHVENWLEQ 299
Cdd:COG2267   157 ARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLNEpAREEVLAAILAWLER 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 15-281 1.28e-26

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 107.34  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  15 GETIAYQEVGRRNTETLVLIHGnmtssqhF--DL-----VIEKLQNQYHIYALDLRGFGQSTYNKSIDSLQDFAEDVKLF 87
Cdd:PRK14875  118 GRTVRYLRLGEGDGTPVVLIHG-------FggDLnnwlfNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAF 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  88 IDQLKLEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVESVGMkGypifkKDINGEPIvSSLVKtkeeiAQDPVQIAPVL 167
Cdd:PRK14875  191 LDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGL-G-----PEINGDYI-DGFVA-----AESRRELKPVL 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 168 DaiknmnKLYyrtvwnlliytHNQPEPDRyeKYLDDMLTQRNFVDVNYAL--ITFNISDEHNGVVEGNKQIHRIKTPTLV 245
Cdd:PRK14875  259 E------LLF-----------ADPALVTR--QMVEDLLKYKRLDGVDDALraLADALFAGGRQRVDLRDRLASLAIPVLV 319

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1263436545 246 IQGDRDYVVPQVVGEELAkhlPNAKLQVLEDCGHSP 281
Cdd:PRK14875  320 IWGEQDRIIPAAHAQGLP---DGVAVHVLPGAGHMP 352
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 30-284 5.47e-24

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: 97.28  E-value: 5.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKL-QNQYHIYALDLRGFGQS----TYnksIDSLQDFAEDVKLFIDQLKLE----KFSLMG 100
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALaAQGFAVYAYDHRGHGRSdgkrGH---VPSFDDYVDDLDTFVDKIREEhpglPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 101 WSMGGGVAMQFTANHPTFVEKLILvesvgmkgypifkkdingepiVSSLVKTKEEIAQDPVQ-IAPVLDAIknMNKLYYR 179
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLIL---------------------SAPALKIKPYLAPPILKlLAKLLGKL--FPRLRVP 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 180 tvWNLLIY--THNQPEPDRYEKylDDMLTQRNFVDVNYALItfnisdehNGVVEGNKQIHRIKTPTLVIQGDRDYVVPQV 257
Cdd:pfam12146 140 --NNLLPDslSRDPEVVAAYAA--DPLVHGGISARTLYELL--------DAGERLLRRAAAITVPLLLLHGGADRVVDPA 207

                         250       260
                  ....*....|....*....|....*....
gi 1263436545 258 VGEELAKHLPNA--KLQVLEDCGHSPFID 284
Cdd:pfam12146 208 GSREFYERAGSTdkTLKLYPGLYHELLNE 236
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
32-299 5.51e-20

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 86.92  E-value: 5.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  32 VLIHGNMTSSQHFDLVIEKLQNQ-YHIYALDLRGFGQSTY--NKSidSLQDFAEDVKLFIDQLKL--EKFSLMGWSMGGG 106
Cdd:COG1647    19 LLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEdlLKT--TWEDWLEDVEEAYEILKAgyDKVIVIGLSMGGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 107 VAMQFTANHPTfVEKLILVESvgmkgyPIFKKDING--EPIVSSLVKTKEEIAQDPvqiapvldaiknmnklyyrtvwnl 184
Cdd:COG1647    97 LALLLAARYPD-VAGLVLLSP------ALKIDDPSAplLPLLKYLARSLRGIGSDI------------------------ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 185 liythnqPEPDRYEKYLDDMLTQrnfvdvnyALITFnisdeHNGVVEGNKQIHRIKTPTLVIQGDRDYVVPQVVGEELAK 264
Cdd:COG1647   146 -------EDPEVAEYAYDRTPLR--------ALAEL-----QRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYE 205

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1263436545 265 HL--PNAKLQVLEDCGHSPFIDC-LDVFINHVENWLEQ 299
Cdd:COG1647   206 RLgsPDKELVWLEDSGHVITLDKdREEVAEEILDFLER 243
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 30-289 1.67e-17

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: 80.09  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIDSLQDFAEDVKLFIDQLKLEKFSLMGWSMGGGVAM 109
Cdd:TIGR02427  15 VLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 110 QFTANHPTFVEKLILVESVGMKGYPifkkdingEPIVSSLVKTKEEiaqdpvQIAPVLDAIknMNKLY---YRtvwnlli 186
Cdd:TIGR02427  95 GLAARRPDRVRALVLSNTAAKIGTP--------ESWNARIAAVRAE------GLAALADAV--LERWFtpgFR------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 187 ythnQPEPDRYEKYlDDMLTQRN---FVDVNYALITFNISDehngvvegnkQIHRIKTPTLVIQGDRDYVVPQVVGEELA 263
Cdd:TIGR02427 152 ----EAHPARLDLY-RNMLVRQPpdgYAGCCAAIRDADFRD----------RLGAIAVPTLCIAGDQDGSTPPELVREIA 216

                         250       260
                  ....*....|....*....|....*.
gi 1263436545 264 KHLPNAKLQVLEDCGHSPFIDCLDVF 289
Cdd:TIGR02427 217 DLVPGARFAEIRGAGHIPCVEQPEAF 242
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
30-299 2.76e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.51  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTS-SQHFDLVIEKLQNQ-YHIYALDLRGFGQSTYNKSIDSLqdfaEDVKLFIDQLK------LEKFSLMGW 101
Cdd:COG1506    25 VVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDEV----DDVLAAIDYLAarpyvdPDRIGIYGH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 102 SMGGGVAMQFTANHPTFVEKLILvesvgmkgypifkkdingepivsslvktkeeiaqdpvqIAPVLDaiknmNKLYYRTV 181
Cdd:COG1506   101 SYGGYMALLAAARHPDRFKAAVA--------------------------------------LAGVSD-----LRSYYGTT 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 182 WNLLIYTHNQPE--PDRYEKylddmltqrnfvdvnYALITFnisdehngvvegnkqIHRIKTPTLVIQGDRDYVVPQVVG 259
Cdd:COG1506   138 REYTERLMGGPWedPEAYAA---------------RSPLAY---------------ADKLKTPLLLIHGEADDRVPPEQA 187

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1263436545 260 EELAKHL----PNAKLQVLEDCGHSPFIDCLDVFINHVENWLEQ 299
Cdd:COG1506   188 ERLYEALkkagKPVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 31-282 1.83e-12

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 65.19  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  31 LVLIHGnmtSSQHFDLVIEKLQNQYHIYALDLRGFGQS-TYNKSIDSLQDFAEDVKLFIDQlklEKFSLMGWSMGGGVAM 109
Cdd:pfam12697   1 VVLVHG---AGLSAAPLAALLAAGVAVLAPDLPGHGSSsPPPLDLADLADLAALLDELGAA---RPVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 110 QFTANHPTFVeklILVESVGMkgypifkkdingepivsslvktkeeiaqDPVQIAPVLDAIKNMNKLYYRTVWNLLI--- 186
Cdd:pfam12697  75 AAAAAALVVG---VLVAPLAA----------------------------PPGLLAALLALLARLGAALAAPAWLAAEsla 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 187 --YTHNQPEPDRYEKYLDDMLTQRNFVDvnyaliTFNISDehngvvegnkqIHRIKTPTLVIqGDRDYVVPQVVGEELAK 264
Cdd:pfam12697 124 rgFLDDLPADAEWAAALARLAALLAALA------LLPLAA-----------WRDLPVPVLVL-AEEDRLVPELAQRLLAA 185

                         250
                  ....*....|....*...
gi 1263436545 265 hLPNAKLQVLEDCGHSPF 282
Cdd:pfam12697 186 -LAGARLVVLPGAGHLPL 202
PLN02578 PLN02578
hydrolase
 31-281 4.47e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 65.63  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  31 LVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQS-----TYNKSI--DSLQDFAEDVklfidqLKlEKFSLMGWSM 103
Cdd:PLN02578   89 IVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSdkaliEYDAMVwrDQVADFVKEV------VK-EPAVLVGNSL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 104 GGGVAMQFTANHPTFVEKLILVESVGMKGypifkkDINGEPIVSSLVktKEEIAQDPVqiapvldaIKNMNKLYYRTVWN 183
Cdd:PLN02578  162 GGFTALSTAVGYPELVAGVALLNSAGQFG------SESREKEEAIVV--EETVLTRFV--------VKPLKEWFQRVVLG 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 184 LLIYTHNQPEpdRYEKYL----------DDML--------TQRNFVDVNYALIT---FNISDehngvVEGNKQIHRIKTP 242
Cdd:PLN02578  226 FLFWQAKQPS--RIESVLksvykdksnvDDYLvesitepaADPNAGEVYYRLMSrflFNQSR-----YTLDSLLSKLSCP 298

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1263436545 243 TLVIQGDRDYVVPQVVGEELAKHLPNAKLQVLEdCGHSP 281
Cdd:PLN02578  299 LLLLWGDLDPWVGPAKAEKIKAFYPDTTLVNLQ-AGHCP 336
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
18-283 6.15e-12

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 64.27  E-value: 6.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  18 IAYQEVGRRNTEtLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIdSLQDFAEDVKlfidQLKLEKFS 97
Cdd:PRK10349    4 IWWQTKGQGNVH-LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGAL-SLADMAEAVL----QQAPDKAI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  98 LMGWSMGGGVAMQFTANHPTFVEKLILVES----VGMKGYPIFKKDIngepivssLVKTKEEIAQDPVQIAPVLDAIKNM 173
Cdd:PRK10349   78 WLGWSLGGLVASQIALTHPERVQALVTVASspcfSARDEWPGIKPDV--------LAGFQQQLSDDFQRTVERFLALQTM 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 174 NKLYYRTVWNLLIYT-HNQPEPDryekylddmltqrnfVDVnyalitFNISDEHNGVVEGNKQIHRIKTPTLVIQGDRDY 252
Cdd:PRK10349  150 GTETARQDARALKKTvLALPMPE---------------VDV------LNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDG 208

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1263436545 253 VVPQVVGEELAKHLPNAKLQVLEDCGHSPFI 283
Cdd:PRK10349  209 LVPRKVVPMLDKLWPHSESYIFAKAAHAPFI 239
PRK10673 PRK10673
esterase;
27-126 1.42e-11

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 63.21  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  27 NTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIDsLQDFAEDVKLFIDQLKLEKFSLMGWSMGGG 106
Cdd:PRK10673   15 NNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMN-YPAMAQDLLDTLDALQIEKATFIGHSMGGK 93

                          90       100
                  ....*....|....*....|
gi 1263436545 107 VAMQFTANHPTFVEKLILVE 126
Cdd:PRK10673   94 AVMALTALAPDRIDKLVAID 113
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 30-279 2.56e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 59.54  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQNQ-YHIYALDLRGFGQSTYNKSIDSLQDfAEDVKLFIDQLKLEKFS------LMGWS 102
Cdd:COG1073    39 AVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESEGEPREEGSPE-RRDARAAVDYLRTLPGVdperigLLGIS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 103 MGGGVAMQFTANHPTFveKLILVESvgmkGYpifkkdingepivSSLVktkeeiaqdpvqiapvlDAIKNMNKLYYRTVW 182
Cdd:COG1073   118 LGGGYALNAAATDPRV--KAVILDS----PF-------------TSLE-----------------DLAAQRAKEARGAYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 183 NLLIYTHNqpepdryekylddmLTQRNFVDVNYALItfnisdehngvvegnKQIHRIKTPTLVIQGDRDYVVPQVVGEEL 262
Cdd:COG1073   162 PGVPYLPN--------------VRLASLLNDEFDPL---------------AKIEKISRPLLFIHGEKDEAVPFYMSEDL 212

                         250
                  ....*....|....*...
gi 1263436545 263 AKHLPNAK-LQVLEDCGH 279
Cdd:COG1073   213 YEAAAEPKeLLIVPGAGH 230
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 4-128 3.19e-10

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 59.62  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545   4 PATMEFVSLsNGETIAYQEVGrrNTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQS-----TYnksidSLQ 78
Cdd:PRK03592    6 PGEMRRVEV-LGSRMAYIETG--EGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASdkpdiDY-----TFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1263436545  79 DFAEDVKLFIDQLKLEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVESV 128
Cdd:PRK03592   78 DHARYLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAI 127
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 20-125 9.05e-09

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 56.04  E-value: 9.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  20 YQEVGRRNTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQS---TYNKSID-SLQDFAEDVKLFIDQLKLEK 95
Cdd:PLN03084  119 CVESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSdkpQPGYGFNyTLDEYVSSLESLIDELKSDK 198

                          90       100       110
                  ....*....|....*....|....*....|
gi 1263436545  96 FSLMGWSMGGGVAMQFTANHPTFVEKLILV 125
Cdd:PLN03084  199 VSLVVQGYFSPPVVKYASAHPDKIKKLILL 228
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 24-129 1.19e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 55.69  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  24 GRRNTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYN----KSIDSLQDFaedvklFIDQLK------- 92
Cdd:PLN02894  101 SKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPdftcKSTEETEAW------FIDSFEewrkakn 174

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1263436545  93 LEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVESVG 129
Cdd:PLN02894  175 LSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAG 211
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 31-125 7.62e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.83  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  31 LVLIHGNMTSSQHFDLVIEKLQNQ-YHIYALDLrgfgqSTYNKSIDSLqdfAEDVKLFIDQLK----LEKFSLMGWSMGG 105
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNY-----PSTNGSIEDS---AEQLAAFVDAVLaatgAEKVDLVGHSMGG 79

                          90       100
                  ....*....|....*....|..
gi 1263436545 106 GVAMQFTANH--PTFVEKLILV 125
Cdd:COG1075    80 LVARYYLKRLggAAKVARVVTL 101
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 30-126 2.01e-07

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 50.99  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQnQYHIYALDLRGFGQStynKSIdSLQDFAEDVKLFIDQLKL---EKFSLMGWSMGGG 106
Cdd:PRK11126    4 WLVFLHGLLGSGQDWQPVGEALP-DYPRLYIDLPGHGGS---AAI-SVDGFADVSRLLSQTLQSyniLPYWLVGYSLGGR 78

                          90       100
                  ....*....|....*....|..
gi 1263436545 107 VAMQFTANHPTfvEKL--ILVE 126
Cdd:PRK11126   79 IAMYYACQGLA--GGLcgLIVE 98
PRK05855 PRK05855
SDR family oxidoreductase;
8-91 4.42e-07

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 51.13  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545   8 EFVSLSNGETIAYQEVGRRNTETLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSIDS--LQDFAEDVK 85
Cdd:PRK05855    5 RTVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAytLARLADDFA 84


                  ....*.
gi 1263436545  86 LFIDQL 91
Cdd:PRK05855   85 AVIDAV 90
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 30-299 9.01e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 49.84  E-value: 9.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTYNKSID-SLQDFAEDVKLFIDQLKLEKFSLMGWSMGGGVA 108
Cdd:PLN02679   90 PVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFSyTMETWAELILDFLEEVVQKPTVLIGNSVGSLAC 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 109 MQFTANHP-TFVEKLILVE-SVGMKGYPIFkkDINGEPIVSSLVKTKEEIAQDPVQIAPVLDAIKNMNKLYyrtvwNLLI 186
Cdd:PLN02679  170 VIAASESTrDLVRGLVLLNcAGGMNNKAVV--DDWRIKLLLPLLWLIDFLLKQRGIASALFNRVKQRDNLK-----NILL 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545 187 YTHNQPEPdryekyLDDMLTQ--RNFVDVNYALITFnISdehngVVEGN------KQIHRIKTPTLVIQGDRDYVVP--Q 256
Cdd:PLN02679  243 SVYGNKEA------VDDELVEiiRGPADDEGALDAF-VS-----IVTGPpgpnpiKLIPRISLPILVLWGDQDPFTPldG 310

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1263436545 257 VVGE---ELAKHLPNAKLQVLEDCGHSPFIDCLDVFINHVENWLEQ 299
Cdd:PLN02679  311 PVGKyfsSLPSQLPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLAQ 356
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 15-149 4.58e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 47.43  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  15 GETIAYQEVGRRNTeTLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQSTY-------NKSIDSLQDFAEDVKLF 87
Cdd:PLN02824   17 GYNIRYQRAGTSGP-ALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKpnprsapPNSFYTFETWGEQLNDF 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263436545  88 IDQLKLEKFSLMGWSMGGGVAMQFTANHPTFVEKLILVeSVGMKGYPIFKKDINGEPIVSSL 149
Cdd:PLN02824   96 CSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLI-NISLRGLHIKKQPWLGRPFIKAF 156
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 29-125 1.23e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 46.34  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  29 ETLVLIHGNMTSSQH-----FDLVIEKLQNQYHIYALDLRGFGQSTynKSIDSLQDFAEDVKLF----IDQLKLEKFSLM 99
Cdd:PLN03087  202 EDVLFIHGFISSSAFwtetlFPNFSDAAKSTYRLFAVDLLGFGRSP--KPADSLYTLREHLEMIersvLERYKVKSFHIV 279

                          90       100
                  ....*....|....*....|....*.
gi 1263436545 100 GWSMGGGVAMQFTANHPTFVEKLILV 125
Cdd:PLN03087  280 AHSLGCILALALAVKHPGAVKSLTLL 305
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
242-299 2.21e-05

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 44.38  E-value: 2.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1263436545 242 PTLVIQGDRDYVVP-QVVGEELAKHLPNAKLQVLEDCGHSpFIDCLDVFINHVENWLEQ 299
Cdd:COG2945   144 PTLVIHGEQDEVVPpAEVLDWARPLSPPLPVVVVPGADHF-FHGKLDELKELVARYLPR 201
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 30-109 1.68e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 42.54  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  30 TLVLIHGNMTSSQHFDLVIEKLQNQYHIYALDLRGFGQS----TYNKSIDslqDFAEDVKLFIDQLKLEKFSLMGWSMGG 105
Cdd:PRK03204   36 PILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSerpsGFGYQID---EHARVIGEFVDHLGLDRYLSMGQDWGG 112


                  ....
gi 1263436545 106 GVAM 109
Cdd:PRK03204  113 PISM 116
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
239-280 3.02e-03

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 37.94  E-value: 3.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1263436545 239 IKTPTLVIQGDRDyvvPQVVGEELAKHL--PNAKLQVLEDCGHS 280
Cdd:COG3571   131 LTVPTLIVQGERD---PFGTPEEVAGYPlpPAIELVWLPGGDHD 171
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
31-118 3.91e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.02  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263436545  31 LVLIHGNMTSSQHFDLVIEKLQNQ-YHIYALDLRGFGQSTYNKSIDS-------LQDFAEDVKLFIDQLK------LEKF 96
Cdd:COG0412    32 VVVLHEIFGLNPHIRDVARRLAAAgYVVLAPDLYGRGGPGDDPDEARalmgaldPELLAADLRAALDWLKaqpevdAGRV 111

                          90       100
                  ....*....|....*....|..
gi 1263436545  97 SLMGWSMGGGVAMQFTANHPTF 118
Cdd:COG0412   112 GVVGFCFGGGLALLAAARGPDL 133
PRK08775 PRK08775
homoserine O-succinyltransferase;
53-125 5.30e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 37.85  E-value: 5.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263436545  53 NQYHIYALDLrgFGQSTYNKSIDSLQDFAEDVKLFIDQLKLEK-FSLMGWSMGGGVAMQFTANHPTFVEKLILV 125
Cdd:PRK08775   98 ARFRLLAFDF--IGADGSLDVPIDTADQADAIALLLDALGIARlHAFVGYSYGALVGLQFASRHPARVRTLVVV 169
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
 241-279 6.29e-03

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 35.39  E-value: 6.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1263436545 241 TPTLVIQGDRDYVVPQVVGEELAKHLPNAKLQVLEDCGH 279
Cdd:pfam08386  34 PPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGH 72
PRK06765 PRK06765
homoserine O-acetyltransferase; Provisional
 76-125 7.63e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 235859 [Multi-domain]  Cd Length: 389  Bit Score: 37.76  E-value: 7.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1263436545  76 SLQDFAEDVKLFIDQLKLEKF-SLMGWSMGGGVAMQFTANHPTFVEKLILV 125
Cdd:PRK06765  142 TILDFVRVQKELIKSLGIARLhAVMGPSMGGMQAQEWAVHYPHMVERMIGV 192
YpfH COG0400
Predicted esterase [General function prediction only];
240-299 9.53e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 36.42  E-value: 9.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263436545 240 KTPTLVIQGDRDYVVPQVVGEELAKHLPNAKLQV---LEDCGHSpfIdCLDVfINHVENWLEQ 299
Cdd:COG0400   139 GTPVFLAHGTQDPVIPVERAREAAEALEAAGADVtyrEYPGGHE--I-SPEE-LADARAWLAE 197
 
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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