|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
1-254 |
0e+00 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 532.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 1 MKLNTRAQTAQSPNNNSPIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRADEMTYAAMAQDLLDTLDAHNL 80
Cdd:PRK10673 1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 81 QKVTLIGHSMGGKAVMALTALAPERISGLVVIDVAPVDYDVRRHDEIFAAINAVTEAGVSTRQQAAAVMREHLDEEGVVQ 160
Cdd:PRK10673 81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 161 FLLKSFVEGQWRFNVPVLWDQYNNIVGWEAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
|
250
....*....|....
gi 504695916 241 PEAVLRAIRRYLTD 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
18-255 |
1.73e-43 |
|
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: 146.68 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRADE-MTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGKAVM 96
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 97 ALTALAPERISGLVVIDvapvdydvrrhdeifaainavteagvstrqQAAAVMREHLDEEGVVQFLLKSFVEGQWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504695916 177 vlwdqynnivgWEAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLTDT 255
Cdd:COG0596 154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
18-241 |
3.93e-26 |
|
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: 102.20 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDNLGVLARDL-VTDHDILQVDMRNHGLSGRA---DEMTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGK 93
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 94 AVMALTALAPERISGLVVIDVAPVDYDVRRHDEIFAAI-----------NAVTEAGVSTRQQAAAVMREHLDEEGVVQFL 162
Cdd:pfam00561 82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffdgfvadFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 163 LKSFVEGQWRFNVPVLWDQyNNIVGWEAVP------AWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWV 236
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGAL-LFIETWSTELrakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....*
gi 504695916 237 HAEKP 241
Cdd:pfam00561 241 FLEGP 245
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
39-253 |
3.38e-13 |
|
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: 67.38 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 39 LVTDHDILQVDMRNHGLS--GRADeMTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGKAVMALTALAPERISGLVVIDVAp 116
Cdd:TIGR02427 36 LTPDFRVLRYDKRGHGLSdaPEGP-YSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 117 vdydvrrhdeifAAINAVTeagvSTRQQAAAVMREHLdeEGVVQFLLKSFVEGQWRFNVPVLWDQYNN------------ 184
Cdd:TIGR02427 114 ------------AKIGTPE----SWNARIAAVRAEGL--AALADAVLERWFTPGFREAHPARLDLYRNmlvrqppdgyag 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504695916 185 ----IVGW---EAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLT 253
Cdd:TIGR02427 176 ccaaIRDAdfrDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
1-254 |
0e+00 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 532.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 1 MKLNTRAQTAQSPNNNSPIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRADEMTYAAMAQDLLDTLDAHNL 80
Cdd:PRK10673 1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 81 QKVTLIGHSMGGKAVMALTALAPERISGLVVIDVAPVDYDVRRHDEIFAAINAVTEAGVSTRQQAAAVMREHLDEEGVVQ 160
Cdd:PRK10673 81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 161 FLLKSFVEGQWRFNVPVLWDQYNNIVGWEAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
|
250
....*....|....
gi 504695916 241 PEAVLRAIRRYLTD 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
18-255 |
1.73e-43 |
|
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: 146.68 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRADE-MTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGKAVM 96
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 97 ALTALAPERISGLVVIDvapvdydvrrhdeifaainavteagvstrqQAAAVMREHLDEEGVVQFLLKSFVEGQWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504695916 177 vlwdqynnivgWEAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLTDT 255
Cdd:COG0596 154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
18-241 |
3.93e-26 |
|
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: 102.20 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDNLGVLARDL-VTDHDILQVDMRNHGLSGRA---DEMTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGK 93
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 94 AVMALTALAPERISGLVVIDVAPVDYDVRRHDEIFAAI-----------NAVTEAGVSTRQQAAAVMREHLDEEGVVQFL 162
Cdd:pfam00561 82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffdgfvadFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 163 LKSFVEGQWRFNVPVLWDQyNNIVGWEAVP------AWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWV 236
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGAL-LFIETWSTELrakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....*
gi 504695916 237 HAEKP 241
Cdd:pfam00561 241 FLEGP 245
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
18-254 |
1.65e-17 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 80.76 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDN-LGVLArDLVTDHDILQVDMRNHGLSG-RADEMTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGKAV 95
Cdd:PRK14875 133 PVVLIHGFGGDLNNwLFNHA-ALAAGRPVIALDLPGHGASSkAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 96 MALTALAPERISGLVVIDVAPVDYDVRRhDEIFAAINAVTEAGVS-------------TRQQAAAVMREHLDeEGVVQFL 162
Cdd:PRK14875 212 LRLAARAPQRVASLTLIAPAGLGPEING-DYIDGFVAAESRRELKpvlellfadpalvTRQMVEDLLKYKRL-DGVDDAL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 163 LK----SFVEGQWRFNVPvlwdqynnivgwEAVPAWPHPTLFIRGGNSPYVTDAYRDTLLaqfPQARAHVIAGAGHWVHA 238
Cdd:PRK14875 290 RAladaLFAGGRQRVDLR------------DRLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVHVLPGAGHMPQM 354
|
250
....*....|....*.
gi 504695916 239 EKPEAVLRAIRRYLTD 254
Cdd:PRK14875 355 EAAADVNRLLAEFLGK 370
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
18-252 |
1.10e-16 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 76.19 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDNLGVLARDLVT-DHDILQVDMRNHGLSGRA--DEMTYAAMAQDL---LDTLDAHNLQKVTLIGHSMG 91
Cdd:COG2267 30 TVVLVHGLGEHSGRYAELAEALAAaGYAVLAFDLRGHGRSDGPrgHVDSFDDYVDDLraaLDALRARPGLPVVLLGHSMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 92 GKAVMALTALAPERISGLVVIdvAPvdydvrrhdeifaAINAVTEAGVSTRQQAAAVMREHLdeegvvqfllksfvegqw 171
Cdd:COG2267 110 GLIALLYAARYPDRVAGLVLL--AP-------------AYRADPLLGPSARWLRALRLAEAL------------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 172 rfnvpvlwdqynnivgweavPAWPHPTLFIRGGNSPYV-TDAYRDTLLAQFPQARAHVIAGAGHWVHAEKP-EAVLRAIR 249
Cdd:COG2267 157 --------------------ARIDVPVLVLHGGADRVVpPEAARRLAARLSPDVELVLLPGARHELLNEPArEEVLAAIL 216
|
...
gi 504695916 250 RYL 252
Cdd:COG2267 217 AWL 219
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
19-247 |
6.71e-14 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 68.65 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 19 IVLVHGLFGSLDNLGVLARDLVTdhdILQVDMRNHGLSGRADEmTYAAMAqDLLDTLDAH-NLQKVTLIGHSMGGKAVMA 97
Cdd:pfam12697 1 VVLVHGAGLSAAPLAALLAAGVA---VLAPDLPGHGSSSPPPL-DLADLA-DLAALLDELgAARPVVLVGHSLGGAVALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 98 LTALAPerisgLVVIDVAPVDYDVRRHDEIFAAINAVTEAGVSTRQQAAAVMREHLDEEGVVQFLLKSFVEGQWRFNVPV 177
Cdd:pfam12697 76 AAAAAL-----VVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 178 LWDQYNNivgWEAVPAWphptLFIRGGNSPYVTDAYRDtLLAQFPQARAHVIAGAGHWVHaEKPEAVLRA 247
Cdd:pfam12697 151 ALLPLAA---WRDLPVP----VLVLAEEDRLVPELAQR-LLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
18-134 |
1.77e-13 |
|
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.
Pssm-ID: 369540 Cd Length: 233 Bit Score: 67.77 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHG---LSGRADEMTYAAMAQD---LLDTLDAHNL----------- 80
Cdd:pfam07819 6 PVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNgfhLDFFSVDFNEELSAFHgrtLLDQAEYLNDairyilslyas 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504695916 81 -----QKVTLIGHSMGGK---AVMALTALAPERISGLVVIDvAPVDYDVRRHD----EIFAAINAV 134
Cdd:pfam07819 86 grpgpTSVILIGHSMGGIvarAALTLPNYIPQSVNTIITLS-SPHAKPPLTFDgdilKFYERLNAF 150
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
39-253 |
3.38e-13 |
|
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: 67.38 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 39 LVTDHDILQVDMRNHGLS--GRADeMTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGKAVMALTALAPERISGLVVIDVAp 116
Cdd:TIGR02427 36 LTPDFRVLRYDKRGHGLSdaPEGP-YSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 117 vdydvrrhdeifAAINAVTeagvSTRQQAAAVMREHLdeEGVVQFLLKSFVEGQWRFNVPVLWDQYNN------------ 184
Cdd:TIGR02427 114 ------------AKIGTPE----SWNARIAAVRAEGL--AALADAVLERWFTPGFREAHPARLDLYRNmlvrqppdgyag 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504695916 185 ----IVGW---EAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLT 253
Cdd:TIGR02427 176 ccaaIRDAdfrDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
19-252 |
1.49e-09 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 56.56 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 19 IVLVHGLFGSLDNLGVLARDLVTDHDI--LQVDMRNHGLSGRAdemTYAAMAQDLLDTLDA------HNLQKVTLIGHSM 90
Cdd:COG1506 26 VVYVHGGPGSRDDSFLPLAQALASRGYavLAPDYRGYGESAGD---WGGDEVDDVLAAIDYlaarpyVDPDRIGIYGHSY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 91 GGkaVMALTALAperisglvvidvapvdydvrRHDEIFAAinAVTEAGVSTRQQAAAVMREhldeegvvqfLLKSFVEGQ 170
Cdd:COG1506 103 GG--YMALLAAA--------------------RHPDRFKA--AVALAGVSDLRSYYGTTRE----------YTERLMGGP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 171 WRFnvPVLWDQYNNIvgwEAVPAWPHPTLFIRGGNSPYV----TDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLR 246
Cdd:COG1506 149 WED--PEAYAARSPL---AYADKLKTPLLLIHGEADDRVppeqAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLE 223
|
....*.
gi 504695916 247 AIRRYL 252
Cdd:COG1506 224 RILDFL 229
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
19-110 |
1.32e-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: 53.76 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 19 IVLVHGLFGSLDNLGVLARDLVT-DHDILQVDMRNHGLSG--RADEMTYAAMAQDLLDTLDA----HNLQKVTLIGHSMG 91
Cdd:pfam12146 7 VVLVHGLGEHSGRYAHLADALAAqGFAVYAYDHRGHGRSDgkRGHVPSFDDYVDDLDTFVDKireeHPGLPLFLLGHSMG 86
|
90
....*....|....*....
gi 504695916 92 GKAVMALTALAPERISGLV 110
Cdd:pfam12146 87 GLIAALYALRYPDKVDGLI 105
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
18-110 |
1.38e-07 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 48.67 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLVHGLFGSLDNLGVLARDLVTDH---DILQVDMRNHGLSGRADEMtyaamAQDLLDTLDAHNLQKVTLIGHSMGGka 94
Cdd:COG1075 7 PVVLVHGLGGSAASWAPLAPRLRAAGypvYALNYPSTNGSIEDSAEQL-----AAFVDAVLAATGAEKVDLVGHSMGG-- 79
|
90 100
....*....|....*....|
gi 504695916 95 VMALTALA----PERISGLV 110
Cdd:COG1075 80 LVARYYLKrlggAAKVARVV 99
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
18-98 |
2.70e-06 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 47.79 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 18 PIVLV-HGLFGSLDNLGVLARDLV-----------TDHDILQVDMRNHGLSGRADEMTYAAMAQDL---LDTLDAHN--- 79
Cdd:COG4188 63 PLVVLsHGLGGSREGYAYLAEHLAshgyvvaapdhPGSNAADLSAALDGLADALDPEELWERPLDLsfvLDQLLALNksd 142
|
90 100
....*....|....*....|....*..
gi 504695916 80 --------LQKVTLIGHSMGGKAVMAL 98
Cdd:COG4188 143 pplagrldLDRIGVIGHSLGGYTALAL 169
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
19-257 |
4.65e-06 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 46.47 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 19 IVLVHGLFGSLDNLGVLARDLV-TDHDILQVDMRNHGLSGRADE-MTYAAMAQDLLDTLD--AHNLQKVTLIGHSMGGKA 94
Cdd:COG1647 18 VLLLHGFTGSPAEMRPLAEALAkAGYTVYAPRLPGHGTSPEDLLkTTWEDWLEDVEEAYEilKAGYDKVIVIGLSMGGLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 95 VMALTALAPErISGLVVIDvAPVDYDvrrhDEIFAAINAVTEAGVSTRQQAAAVMREHLDEEGVVQFLLKSFVEGQWrfn 174
Cdd:COG1647 98 ALLLAARYPD-VAGLVLLS-PALKID----DPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLRALAELQR--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 175 vpvLWDQYNnivgwEAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIA--GAGHWVHAEK-PEAVLRAIRRY 251
Cdd:COG1647 169 ---LIREVR-----RDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWleDSGHVITLDKdREEVAEEILDF 240
|
....*.
gi 504695916 252 LTDTAN 257
Cdd:COG1647 241 LERLAA 246
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
19-252 |
6.27e-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: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 19 IVLVHGLFGSLDNLGVLARDLvTDH--DILQVDMRNHGLS-GRADEMTYAAM-----AQDLLDTLDAHNLQKVTLIGHSM 90
Cdd:COG1073 40 VVVAHGNGGVKEQRALYAQRL-AELgfNVLAFDYRGYGESeGEPREEGSPERrdaraAVDYLRTLPGVDPERIGLLGISL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 91 GGKAVMALTALAPeRISGLvvidvapvdydvrrhdeifaainaVTEAGVSTRQQAAAVMREHLDEEGVVQFLLKSFVEGQ 170
Cdd:COG1073 119 GGGYALNAAATDP-RVKAV------------------------ILDSPFTSLEDLAAQRAKEARGAYLPGVPYLPNVRLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 171 WRFNvpvlwDQYNNIvgwEAVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARA-HVIAGAGH----WVHAEKPEAVL 245
Cdd:COG1073 174 SLLN-----DEFDPL---AKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKElLIVPGAGHvdlyDRPEEEYFDKL 245
|
....*...
gi 504695916 246 RA-IRRYL 252
Cdd:COG1073 246 AEfFKKNL 253
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
9-252 |
2.05e-05 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 45.29 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 9 TAQSPNNNSPIVLVHGLFGS----LDNLGVLARDLvtdhDILQVDMRNHGLSGRAD------EMTYAAMAQDLLDTLDAH 78
Cdd:PLN02894 98 TFDSKEDAPTLVMVHGYGASqgffFRNFDALASRF----RVIAIDQLGWGGSSRPDftckstEETEAWFIDSFEEWRKAK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 79 NLQKVTLIGHSMGGkAVMALTALA-PERISGLVVIDVAPVDYDVRRHDEIF---------AAINAVTEAGVS-------- 140
Cdd:PLN02894 174 NLSNFILLGHSFGG-YVAAKYALKhPEHVQHLILVGPAGFSSESDDKSEWLtkfratwkgAVLNHLWESNFTpqkiirgl 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 141 -------TRQQAAAVMREHLDEEGVVQF---LLKSFV--------EGQWRFNVPVLWDQYNNIVGWEAVPAWPHPTLFIr 202
Cdd:PLN02894 253 gpwgpnlVRRYTTARFGAHSTGDILSEEeskLLTDYVyhtlaakaSGELCLKYIFSFGAFARKPLLESASEWKVPTTFI- 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695916 203 ggnspYVTDAYRDTLLAQfpQARAHV--------IAGAGHWVHAEKPE----AVLRAIRRYL 252
Cdd:PLN02894 332 -----YGRHDWMNYEGAV--EARKRMkvpceiirVPQGGHFVFLDNPSgfhsAVLYACRKYL 386
|
|
| COG4814 |
COG4814 |
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown]; |
1-97 |
5.78e-05 |
|
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];
Pssm-ID: 443842 Cd Length: 286 Bit Score: 43.39 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 1 MKLNTRAQTAQSPNNNSPIVLVHGLFGSLDNLGVLARDLVTD----HDILQVDMRNHG---LSG---------------- 57
Cdd:COG4814 28 TKSTVKSLKSKYNSKQTPTIFIHGSGGTANSFNTMINRLNEKygvgHKVLTVTVSKDGkitYSGkirknaknpiiqvgfe 107
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 504695916 58 --RADEMTYAAMAQDLLDTLDAH-NLQKVTLIGHSMGGKAVMA 97
Cdd:COG4814 108 dnRDSIKKQAKWLKKVLKYLKKKyGFKKFNAVGHSMGGLALTY 150
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
19-111 |
8.03e-05 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 42.90 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 19 IVLVHGLFGSLDN-LGVLarDLVTDHDILQVDMRNHGLSGRADEMTYAAMAQDLLDTLDAHNLQKVTLIGHSMGGKAVM- 96
Cdd:PRK11126 5 LVFLHGLLGSGQDwQPVG--EALPDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAMy 82
|
90
....*....|....*.
gi 504695916 97 -ALTALaPERISGLVV 111
Cdd:PRK11126 83 yACQGL-AGGLCGLIV 97
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
11-115 |
2.12e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 39.05 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 11 QSPNNNSPIVLVHGLFGSLD----NLGVLARDlvtdHDILQVDMRNHGLSGRADEMTYA--AMAQDLLDTLDAHNLQKVT 84
Cdd:PLN02679 83 EVTSSGPPVLLVHGFGASIPhwrrNIGVLAKN----YTVYAIDLLGFGASDKPPGFSYTmeTWAELILDFLEEVVQKPTV 158
|
90 100 110
....*....|....*....|....*....|..
gi 504695916 85 LIGHSMGGKA-VMALTALAPERISGLVVIDVA 115
Cdd:PLN02679 159 LIGNSVGSLAcVIAASESTRDLVRGLVLLNCA 190
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
4-115 |
3.61e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 38.18 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 4 NTRAQTAQspNNNSPIVLVHGLFGSLD----NLGVLARDlvtdHDILQVDMRNHGLSGRADEM--------TYAAMAQDL 71
Cdd:PLN02824 19 NIRYQRAG--TSGPALVLVHGFGGNADhwrkNTPVLAKS----HRVYAIDLLGYGYSDKPNPRsappnsfyTFETWGEQL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 504695916 72 LDTLDAHNLQKVTLIGHSMGGKAVMALTALAPERISGLVVIDVA 115
Cdd:PLN02824 93 NDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLINIS 136
|
|
| PLN02578 |
PLN02578 |
hydrolase |
17-115 |
5.71e-03 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 37.51 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695916 17 SPIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRA----DEMTYAAMAQDLLDTLDAhnlQKVTLIGHSMGG 92
Cdd:PLN02578 87 LPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKAlieyDAMVWRDQVADFVKEVVK---EPAVLVGNSLGG 163
|
90 100
....*....|....*....|...
gi 504695916 93 KAVMALTALAPERISGLVVIDVA 115
Cdd:PLN02578 164 FTALSTAVGYPELVAGVALLNSA 186
|
|
| |
