|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
1-254 |
0e+00 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 531.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 1 MKLNTRAQTAQSPNNNSPIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRSDEMTYAAMAQDLLDTLDAHDL 80
Cdd:PRK10673 1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 81 QKVTLIGHSMGGKAVMALTALAPDRISGLVVIDVAPVDYDVRRHDEIFAAINAVTEAGVATRQQAAAVMREHLNEEGVVQ 160
Cdd:PRK10673 81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 161 FLLKSFVDGQWRFNVPVLWDQYNNIVGWETVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
|
250
....*....|....
gi 556425846 241 PDAVLRAIRRYLAD 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
18-255 |
3.16e-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: 145.91 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRSDE-MTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGKAVM 96
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 97 ALTALAPDRISGLVVIDvapvdydvrrhdeifaainavteagvatrqQAAAVMREHLNEEGVVQFLLKSFVDGQWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556425846 177 vlwdqynnivgWETVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLADT 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 |
3.77e-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: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDNLGVLARDL-VTDHDILQVDMRNHGLSGRS---DEMTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGK 93
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 94 AVMALTALAPDRISGLVVIDVAPVDYDVRRHDEIFAAI-----NAVTEAGVATR--QQAAAVMREHLNEEGVV----QFL 162
Cdd:pfam00561 82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPlgRLVAKLLALLLLRLRLLkalpLLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 163 LKSFVDGQWRFNVPVLWDQyNNIVGWETVP------AWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWV 236
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGAL-LFIETWSTELrakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....*
gi 556425846 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 |
7.50e-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: 66.23 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 39 LVTDHDILQVDMRNHGLSGRSD-EMTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGKAVMALTALAPDRISGLVVIDVApv 117
Cdd:TIGR02427 36 LTPDFRVLRYDKRGHGLSDAPEgPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTA-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 118 dydvrrhdeifAAINavTEAGVATRqqAAAVMREHLneEGVVQFLLKSFVDGQWRFNVPVLWDQYNN------------- 184
Cdd:TIGR02427 114 -----------AKIG--TPESWNAR--IAAVRAEGL--AALADAVLERWFTPGFREAHPARLDLYRNmlvrqppdgyagc 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425846 185 ---IVGW---ETVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLA 253
Cdd:TIGR02427 177 caaIRDAdfrDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 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: 531.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 1 MKLNTRAQTAQSPNNNSPIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRSDEMTYAAMAQDLLDTLDAHDL 80
Cdd:PRK10673 1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 81 QKVTLIGHSMGGKAVMALTALAPDRISGLVVIDVAPVDYDVRRHDEIFAAINAVTEAGVATRQQAAAVMREHLNEEGVVQ 160
Cdd:PRK10673 81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 161 FLLKSFVDGQWRFNVPVLWDQYNNIVGWETVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
|
250
....*....|....
gi 556425846 241 PDAVLRAIRRYLAD 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
18-255 |
3.16e-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: 145.91 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLSGRSDE-MTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGKAVM 96
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 97 ALTALAPDRISGLVVIDvapvdydvrrhdeifaainavteagvatrqQAAAVMREHLNEEGVVQFLLKSFVDGQWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556425846 177 vlwdqynnivgWETVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLADT 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 |
3.77e-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: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDNLGVLARDL-VTDHDILQVDMRNHGLSGRS---DEMTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGK 93
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 94 AVMALTALAPDRISGLVVIDVAPVDYDVRRHDEIFAAI-----NAVTEAGVATR--QQAAAVMREHLNEEGVV----QFL 162
Cdd:pfam00561 82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPlgRLVAKLLALLLLRLRLLkalpLLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 163 LKSFVDGQWRFNVPVLWDQyNNIVGWETVP------AWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWV 236
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGAL-LFIETWSTELrakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....*
gi 556425846 237 HAEKP 241
Cdd:pfam00561 241 FLEGP 245
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
18-254 |
7.22e-18 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 81.91 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDN-LGVLArDLVTDHDILQVDMRNHGLSG-RSDEMTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGKAV 95
Cdd:PRK14875 133 PVVLIHGFGGDLNNwLFNHA-ALAAGRPVIALDLPGHGASSkAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 96 MALTALAPDRISGLVVIDVAPVDYDVRRhDEIFAAINAVTEAGVA-------------TRQQAAAVMREhLNEEGVVQFL 162
Cdd:PRK14875 212 LRLAARAPQRVASLTLIAPAGLGPEING-DYIDGFVAAESRRELKpvlellfadpalvTRQMVEDLLKY-KRLDGVDDAL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 163 LK----SFVDGQWRFNV-PVLwdqynnivgwetvPAWPHPTLFIRGGNSPYVTDAYRDTLLaqfPQARAHVIAGAGHWVH 237
Cdd:PRK14875 290 RAladaLFAGGRQRVDLrDRL-------------ASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVHVLPGAGHMPQ 353
|
250
....*....|....*..
gi 556425846 238 AEKPDAVLRAIRRYLAD 254
Cdd:PRK14875 354 MEAAADVNRLLAEFLGK 370
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
18-254 |
4.09e-16 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 74.65 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDNLGVLARDLVT-DHDILQVDMRNHGLSGRS--DEMTYAAMAQDL---LDTLDAHDLQKVTLIGHSMG 91
Cdd:COG2267 30 TVVLVHGLGEHSGRYAELAEALAAaGYAVLAFDLRGHGRSDGPrgHVDSFDDYVDDLraaLDALRARPGLPVVLLGHSMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 92 GKAVMALTALAPDRISGLVVIdvAPvdydvrrhdeifaAINAVTEAGVATRQQAAAVMREHLneegvvqfllksfvdgqw 171
Cdd:COG2267 110 GLIALLYAARYPDRVAGLVLL--AP-------------AYRADPLLGPSARWLRALRLAEAL------------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 172 rfnvpvlwdqynnivgwetvPAWPHPTLFIRGGNSPYV-TDAYRDTLLAQFPQARAHVIAGAGHWVHAEKP-DAVLRAIR 249
Cdd:COG2267 157 --------------------ARIDVPVLVLHGGADRVVpPEAARRLAARLSPDVELVLLPGARHELLNEPArEEVLAAIL 216
|
....*
gi 556425846 250 RYLAD 254
Cdd:COG2267 217 AWLER 221
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
19-247 |
6.99e-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: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 19 IVLVHGLFGSLDNLGVLARDLVTdhdILQVDMRNHGLSGRSDEmTYAAMAqDLLDTLDAH-DLQKVTLIGHSMGGKAVMA 97
Cdd:pfam12697 1 VVLVHGAGLSAAPLAALLAAGVA---VLAPDLPGHGSSSPPPL-DLADLA-DLAALLDELgAARPVVLVGHSLGGAVALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 98 LTALAPdrisgLVVIDVAPVDYDVRRHDEIFAAINAVTEAGVATRQQAAAVMREHlneegvvqFLLKSFVDGQWRFNVPV 177
Cdd:pfam12697 76 AAAAAL-----VVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARG--------FLDDLPADAEWAAALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556425846 178 LwDQYNNIVGWETVPAWPH--PTLFIRGGNSPYVTDAYRDtLLAQFPQARAHVIAGAGHWVHaEKPDAVLRA 247
Cdd:pfam12697 143 L-AALLAALALLPLAAWRDlpVPVLVLAEEDRLVPELAQR-LLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
18-134 |
2.15e-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: 67.39 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHG---LSGRSDEMTYAAMAQD---LLDTLD--------------- 76
Cdd:pfam07819 6 PVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNgfhLDFFSVDFNEELSAFHgrtLLDQAEylndairyilslyas 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556425846 77 -AHDLQKVTLIGHSMGGK---AVMALTALAPDRISGLVVIDvAPVDYDVRRHD----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 |
7.50e-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: 66.23 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 39 LVTDHDILQVDMRNHGLSGRSD-EMTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGKAVMALTALAPDRISGLVVIDVApv 117
Cdd:TIGR02427 36 LTPDFRVLRYDKRGHGLSDAPEgPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTA-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 118 dydvrrhdeifAAINavTEAGVATRqqAAAVMREHLneEGVVQFLLKSFVDGQWRFNVPVLWDQYNN------------- 184
Cdd:TIGR02427 114 -----------AKIG--TPESWNAR--IAAVRAEGL--AALADAVLERWFTPGFREAHPARLDLYRNmlvrqppdgyagc 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425846 185 ---IVGW---ETVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLA 253
Cdd:TIGR02427 177 caaIRDAdfrDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
19-253 |
7.15e-10 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 57.72 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 19 IVLVHGLFGSLDNLGVLARDLVTDHDI--LQVDMRNHGlsgRSDEMTYAAMAQDLLDTLDA------HDLQKVTLIGHSM 90
Cdd:COG1506 26 VVYVHGGPGSRDDSFLPLAQALASRGYavLAPDYRGYG---ESAGDWGGDEVDDVLAAIDYlaarpyVDPDRIGIYGHSY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 91 GGkaVMALTALApdrisglvvidvapvdydvrRHDEIFAAinAVTEAGVATRQQAAAVMREhlneegvvqfLLKSFVDGQ 170
Cdd:COG1506 103 GG--YMALLAAA--------------------RHPDRFKA--AVALAGVSDLRSYYGTTRE----------YTERLMGGP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 171 WRFnvPVLWDQYNNIvgwETVPAWPHPTLFIRGGNSPYV----TDAYRDTLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246
Cdd:COG1506 149 WED--PEAYAARSPL---AYADKLKTPLLLIHGEADDRVppeqAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLE 223
|
....*..
gi 556425846 247 AIRRYLA 253
Cdd:COG1506 224 RILDFLD 230
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
19-110 |
4.16e-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: 52.60 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 19 IVLVHGLFGSLDNLGVLARDLVT-DHDILQVDMRNHGLSG--RSDEMTYAAMAQDLLDTLDA----HDLQKVTLIGHSMG 91
Cdd:pfam12146 7 VVLVHGLGEHSGRYAHLADALAAqGFAVYAYDHRGHGRSDgkRGHVPSFDDYVDDLDTFVDKireeHPGLPLFLLGHSMG 86
|
90
....*....|....*....
gi 556425846 92 GKAVMALTALAPDRISGLV 110
Cdd:pfam12146 87 GLIAALYALRYPDKVDGLI 105
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
18-110 |
7.91e-08 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 49.44 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 18 PIVLVHGLFGSLDNLGVLARDLvtdhdilqvdmRNHG-----LSGRSDEMTYAAMAQDLLDTLDA----HDLQKVTLIGH 88
Cdd:COG1075 7 PVVLVHGLGGSAASWAPLAPRL-----------RAAGypvyaLNYPSTNGSIEDSAEQLAAFVDAvlaaTGAEKVDLVGH 75
|
90 100
....*....|....*....|....*.
gi 556425846 89 SMGGkaVMALTALA----PDRISGLV 110
Cdd:COG1075 76 SMGG--LVARYYLKrlggAAKVARVV 99
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
19-98 |
2.68e-06 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 47.79 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 19 IVLVHGLFGSLDNLGVLARDLV-----------TDHDILQVDMRNHGLSGRSDEMTYAAMAQDL---LDTLDAH------ 78
Cdd:COG4188 65 VVLSHGLGGSREGYAYLAEHLAshgyvvaapdhPGSNAADLSAALDGLADALDPEELWERPLDLsfvLDQLLALnksdpp 144
|
90 100
....*....|....*....|....*
gi 556425846 79 -----DLQKVTLIGHSMGGKAVMAL 98
Cdd:COG4188 145 lagrlDLDRIGVIGHSLGGYTALAL 169
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
19-252 |
6.61e-05 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 42.98 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 19 IVLVHGLFGSLDNLGVLARDLvTDH--DILQVDMRNHGLS-GRSDEMTYAAM-----AQDLLDTLDAHDLQKVTLIGHSM 90
Cdd:COG1073 40 VVVAHGNGGVKEQRALYAQRL-AELgfNVLAFDYRGYGESeGEPREEGSPERrdaraAVDYLRTLPGVDPERIGLLGISL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 91 GGkaVMALTALAPD-RISGLvvidvapvdydvrrhdeifaainaVTEAGVATRQQAAAVMREHLNEEGVVQFLLKSFVDG 169
Cdd:COG1073 119 GG--GYALNAAATDpRVKAV------------------------ILDSPFTSLEDLAAQRAKEARGAYLPGVPYLPNVRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 170 QWRFNvpvlwDQYNNIvgwETVPAWPHPTLFIRGGNSPYVTDAYRDTLLAQFPQARA-HVIAGAGH----WVHAEKPDAV 244
Cdd:COG1073 173 ASLLN-----DEFDPL---AKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKElLIVPGAGHvdlyDRPEEEYFDK 244
|
....*....
gi 556425846 245 LRA-IRRYL 252
Cdd:COG1073 245 LAEfFKKNL 253
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
19-120 |
1.62e-04 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 41.85 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 19 IVLVHGLFGSLDNLGVLARDLV-TDHDILQVDMRNHGLSGRSDE-MTYAAMAQDLLDTLD--AHDLQKVTLIGHSMGGKA 94
Cdd:COG1647 18 VLLLHGFTGSPAEMRPLAEALAkAGYTVYAPRLPGHGTSPEDLLkTTWEDWLEDVEEAYEilKAGYDKVIVIGLSMGGLL 97
|
90 100
....*....|....*....|....*.
gi 556425846 95 VMALTALAPDrISGLVVIDvAPVDYD 120
Cdd:COG1647 98 ALLLAARYPD-VAGLVLLS-PALKID 121
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
19-111 |
3.03e-04 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 40.98 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 19 IVLVHGLFGSLDN-LGVLarDLVTDHDILQVDMRNHGLSGRSDEMTYAAMAQDLLDTLDAHDLQKVTLIGHSMGGKAVM- 96
Cdd:PRK11126 5 LVFLHGLLGSGQDwQPVG--EALPDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAMy 82
|
90
....*....|....*.
gi 556425846 97 -ALTALAPDrISGLVV 111
Cdd:PRK11126 83 yACQGLAGG-LCGLIV 97
|
|
| COG4814 |
COG4814 |
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown]; |
1-97 |
3.21e-04 |
|
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];
Pssm-ID: 443842 Cd Length: 286 Bit Score: 41.08 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 1 MKLNTRAQTAQSPNNNSPIVLVHGLFGSLDNLGVLARDLVTD----HDILQVDMRNHG---LSG---------------- 57
Cdd:COG4814 28 TKSTVKSLKSKYNSKQTPTIFIHGSGGTANSFNTMINRLNEKygvgHKVLTVTVSKDGkitYSGkirknaknpiiqvgfe 107
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 556425846 58 --RSDEMTYAAMAQDLLDTLDAH-DLQKVTLIGHSMGGKAVMA 97
Cdd:COG4814 108 dnRDSIKKQAKWLKKVLKYLKKKyGFKKFNAVGHSMGGLALTY 150
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
63-112 |
1.21e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 39.18 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 556425846 63 TYAAMAQDLLDTLDAH---DLQKVTLIGHSMGGKAVMALTALAPDRISGLVVI 112
Cdd:COG4099 104 KALDAVLALLDDLIAEyriDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPI 156
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
11-115 |
1.26e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 39.44 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 11 QSPNNNSPIVLVHGLFGSLD----NLGVLARDlvtdHDILQVDMRNHGLSGRSDEMTYA--AMAQDLLDTLDAHDLQKVT 84
Cdd:PLN02679 83 EVTSSGPPVLLVHGFGASIPhwrrNIGVLAKN----YTVYAIDLLGFGASDKPPGFSYTmeTWAELILDFLEEVVQKPTV 158
|
90 100 110
....*....|....*....|....*....|..
gi 556425846 85 LIGHSMGGKA-VMALTALAPDRISGLVVIDVA 115
Cdd:PLN02679 159 LIGNSVGSLAcVIAASESTRDLVRGLVLLNCA 190
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
6-116 |
4.11e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 38.30 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 6 RAQTAQSPNNNSPIVLVHGLFGSLDNLGVLARDLVTDHDILQVDMRNHGLS-----GRSDEMTYA---AMAQDLLDTLDA 77
Cdd:PLN02980 1361 KVHEVGQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhAKETQTEPTlsvELVADLLYKLIE 1440
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 556425846 78 HDLQ-KVTLIGHSMGGKAVMALTALAPDRISGLVVIDVAP 116
Cdd:PLN02980 1441 HITPgKVTLVGYSMGARIALYMALRFSDKIEGAVIISGSP 1480
|
|
| DUF676 |
pfam05057 |
Putative serine esterase (DUF676); This family of proteins are probably serine esterase type ... |
12-105 |
6.81e-03 |
|
Putative serine esterase (DUF676); This family of proteins are probably serine esterase type enzymes with an alpha/beta hydrolase fold.
Pssm-ID: 309968 Cd Length: 212 Bit Score: 36.70 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 12 SPNNNSPIVLVHGLFGSLDNLGVLARDLVTDHD----ILQVDMRNHGLSGRS-DEMTYaAMAQDLLDTL-DAHDLQKVTL 85
Cdd:pfam05057 1 SSKKDHLVVLVHGLWGNSADMEYVAEQLEKKLPdeliVFLMSSNNVSKTFKGiDVMGE-RLANEVLEFVqDGSDGKKISF 79
|
90 100
....*....|....*....|
gi 556425846 86 IGHSMGGKAVMALTALAPDR 105
Cdd:pfam05057 80 VGHSLGGLIARYAIGKLYDK 99
|
|
| PhaC |
COG3243 |
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
71-120 |
9.80e-03 |
|
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 36.86 E-value: 9.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425846 71 LLDTLDA----HDLQKVTLIGHSMGGkaVMALTALA------PDRISGLVVIdVAPVDYD 120
Cdd:COG3243 263 ILAAVDAvreiTGEDKVNLLGYCLGG--TLLAIYAAllaargPDRVASLTLL-ATPLDFS 319
|
|
| |
