|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
5-265 |
5.43e-49 |
|
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: 161.32 E-value: 5.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 5 VTIRDCSIGYELKNGEGVTKLLLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGGYSLQNHADDTVQLMDHL 84
Cdd:COG0596 7 VTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 85 GIETADIIGTSYGSEVAMEFAIAYPRRTRSLVIIDGVseldpvltaaveswksaalsdprvfyrslipwnysagylethL 164
Cdd:COG0596 87 GLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV------------------------------------------L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 165 AQLREReelvAGLPQEYFQAFASLCDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEIIPSAGH 244
Cdd:COG0596 125 AALAEP----LRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGH 200
|
250 260
....*....|....*....|.
gi 609242772 245 AVVIEQPGEVARRTHDFLKQL 265
Cdd:COG0596 201 FPPLEQPEAFAAALRDFLARL 221
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
25-263 |
2.29e-38 |
|
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: 134.79 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGGYSLQNHADDTVQLMDHLGIETADIIGTSYGSEVAMEF 104
Cdd:TIGR02427 17 VFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 105 AIAYPRRTRSLVI------IDGVSELDPVLtAAVESWKSAALSDPrVFYRslipWnYSAGYLETHLAQLRE-REELVAGL 177
Cdd:TIGR02427 97 AARRPDRVRALVLsntaakIGTPESWNARI-AAVRAEGLAALADA-VLER----W-FTPGFREAHPARLDLyRNMLVRQP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 178 PQEYfqafASLCDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEIIPSAGHAVVIEQPGEVARR 257
Cdd:TIGR02427 170 PDGY----AGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAA 245
|
....*.
gi 609242772 258 THDFLK 263
Cdd:TIGR02427 246 LRDFLR 251
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-264 |
2.98e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 85.77 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 2 PDKVTIRDCSIGY-ELKNGEGVTKLLLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGGYSLQNHADDTVQL 80
Cdd:PRK14875 111 PRKARIGGRTVRYlRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 81 MDHLGIETADIIGTSYGSEVAMEFAIAYPRRTRSLVII--------------------DGVSELDPVLTAAVeswksaal 140
Cdd:PRK14875 191 LDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIapaglgpeingdyidgfvaaESRRELKPVLELLF-------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 141 SDPRVFYRSLIpwnysagylETHLAQLRErEELVAGLPQEYFQAFAslcDAFAEIDLTPRLEMIQCPSLVMVGENDilkh 220
Cdd:PRK14875 263 ADPALVTRQMV---------EDLLKYKRL-DGVDDALRALADALFA---GGRQRVDLRDRLASLAIPVLVIWGEQD---- 325
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 609242772 221 rgfaRII----ADNI-AGSRLEIIPSAGHAVVIEQPGEVARRTHDFLKQ 264
Cdd:PRK14875 326 ----RIIpaahAQGLpDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
25-251 |
1.03e-18 |
|
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: 82.55 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMSMNHWMPFVDA-YSQHAPFLLHDFRGQLFSEKPR--GGYSLQNHADDTVQLMDHLGIETADIIGTSYGSEVA 101
Cdd:pfam00561 4 LLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 102 MEFAIAYPRRTRSLVIIDGVSELDPVLTAavesWKSAALSDPRVFYRSLIP---------WNYSAGYLETHLAQLREREE 172
Cdd:pfam00561 84 LAYAAKYPDRVKALVLLGALDPPHELDEA----DRFILALFPGFFDGFVADfapnplgrlVAKLLALLLLRLRLLKALPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 173 LVAGLPQEYFQAFASL-------CDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEIIPSAGHA 245
Cdd:pfam00561 160 LNKRFPSGDYALAKSLvtgallfIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHF 239
|
....*.
gi 609242772 246 VVIEQP 251
Cdd:pfam00561 240 AFLEGP 245
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
5-265 |
5.43e-49 |
|
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: 161.32 E-value: 5.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 5 VTIRDCSIGYELKNGEGVTKLLLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGGYSLQNHADDTVQLMDHL 84
Cdd:COG0596 7 VTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 85 GIETADIIGTSYGSEVAMEFAIAYPRRTRSLVIIDGVseldpvltaaveswksaalsdprvfyrslipwnysagylethL 164
Cdd:COG0596 87 GLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV------------------------------------------L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 165 AQLREReelvAGLPQEYFQAFASLCDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEIIPSAGH 244
Cdd:COG0596 125 AALAEP----LRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGH 200
|
250 260
....*....|....*....|.
gi 609242772 245 AVVIEQPGEVARRTHDFLKQL 265
Cdd:COG0596 201 FPPLEQPEAFAAALRDFLARL 221
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
25-263 |
2.29e-38 |
|
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: 134.79 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGGYSLQNHADDTVQLMDHLGIETADIIGTSYGSEVAMEF 104
Cdd:TIGR02427 17 VFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 105 AIAYPRRTRSLVI------IDGVSELDPVLtAAVESWKSAALSDPrVFYRslipWnYSAGYLETHLAQLRE-REELVAGL 177
Cdd:TIGR02427 97 AARRPDRVRALVLsntaakIGTPESWNARI-AAVRAEGLAALADA-VLER----W-FTPGFREAHPARLDLyRNMLVRQP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 178 PQEYfqafASLCDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEIIPSAGHAVVIEQPGEVARR 257
Cdd:TIGR02427 170 PDGY----AGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAA 245
|
....*.
gi 609242772 258 THDFLK 263
Cdd:TIGR02427 246 LRDFLR 251
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-264 |
2.98e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 85.77 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 2 PDKVTIRDCSIGY-ELKNGEGVTKLLLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGGYSLQNHADDTVQL 80
Cdd:PRK14875 111 PRKARIGGRTVRYlRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 81 MDHLGIETADIIGTSYGSEVAMEFAIAYPRRTRSLVII--------------------DGVSELDPVLTAAVeswksaal 140
Cdd:PRK14875 191 LDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIapaglgpeingdyidgfvaaESRRELKPVLELLF-------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 141 SDPRVFYRSLIpwnysagylETHLAQLRErEELVAGLPQEYFQAFAslcDAFAEIDLTPRLEMIQCPSLVMVGENDilkh 220
Cdd:PRK14875 263 ADPALVTRQMV---------EDLLKYKRL-DGVDDALRALADALFA---GGRQRVDLRDRLASLAIPVLVIWGEQD---- 325
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 609242772 221 rgfaRII----ADNI-AGSRLEIIPSAGHAVVIEQPGEVARRTHDFLKQ 264
Cdd:PRK14875 326 ----RIIpaahAQGLpDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
25-251 |
1.03e-18 |
|
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: 82.55 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMSMNHWMPFVDA-YSQHAPFLLHDFRGQLFSEKPR--GGYSLQNHADDTVQLMDHLGIETADIIGTSYGSEVA 101
Cdd:pfam00561 4 LLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 102 MEFAIAYPRRTRSLVIIDGVSELDPVLTAavesWKSAALSDPRVFYRSLIP---------WNYSAGYLETHLAQLREREE 172
Cdd:pfam00561 84 LAYAAKYPDRVKALVLLGALDPPHELDEA----DRFILALFPGFFDGFVADfapnplgrlVAKLLALLLLRLRLLKALPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 173 LVAGLPQEYFQAFASL-------CDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEIIPSAGHA 245
Cdd:pfam00561 160 LNKRFPSGDYALAKSLvtgallfIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHF 239
|
....*.
gi 609242772 246 VVIEQP 251
Cdd:pfam00561 240 AFLEGP 245
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
25-263 |
1.60e-14 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 274729 [Multi-domain] Cd Length: 252 Bit Score: 71.09 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGG--YSLQNHADD-TVQLMDHLGIETADIIGTSYGSEVA 101
Cdd:TIGR03695 6 VFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIerYDFEEAAQLlLATLLDQLGIEPFFLVGYSMGGRIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 102 MEFAIAYPRRTRSLvIIDGVSeldPVLTAAVESwKSAALSDPR---VFYRSLIPW--NY-------SAGYLETHLAQLRE 169
Cdd:TIGR03695 86 LYYALQYPERVQGL-ILESGS---PGLQTEEER-AARRQNDEQlaqRFEQEGLEAflDDwyqqplfASQKNLPPEQRQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 170 REELVAGLPQEYFQAFASLCDAfAEIDLTPRLEMIQCPSLVMVGENDiLKHRGFARIIADNIAGSRLEIIPSAGHAVVIE 249
Cdd:TIGR03695 161 RAERLANNPEGLAKMLRATGLG-KQPSLWPKLQALKIPVLYLCGERD-EKFVQIAKEMQKLIPNLTLHIIPNAGHNIHLE 238
|
250
....*....|....
gi 609242772 250 QPGEVARRTHDFLK 263
Cdd:TIGR03695 239 NPEAFAKILLAFLE 252
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
25-257 |
5.12e-11 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMsmnHWMPFVDAYSQHAPFLLHDFRGQLFSEKPRGGYSlqnHADDTVQLMDHLGIET-ADIIGTSYGSEVAME 103
Cdd:pfam12697 2 VLVHGAGL---SAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLA---DLADLAALLDELGAARpVVLVGHSLGGAVALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 104 FAIAYPRRTrslVIIDGVSELDPVLTAAVESWKSAALSDPRVFYRSLIPwnYSAGYLETHLAQLREREELVAGLPQEYFQ 183
Cdd:pfam12697 76 AAAAALVVG---VLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAES--LARGFLDDLPADAEWAAALARLAALLAAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 609242772 184 AFASLcdafaeidltPRLEMIQCPSLVMVGENDILKHrgFARIIADNIAGSRLEIIPSAGHAvVIEQPGEVARR 257
Cdd:pfam12697 151 ALLPL----------AAWRDLPVPVLVLAEEDRLVPE--LAQRLLAALAGARLVVLPGAGHL-PLDDPEEVAEA 211
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
25-264 |
4.67e-10 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 58.09 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMSMNHWMPFVDAYSQH-APFLLHDFRGQLFSEKPRGGY-SLQNHADDTVQLMDHLGIETAD---IIGTSYGSE 99
Cdd:COG2267 32 VLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAALDALRARPGLpvvLLGHSMGGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 100 VAMEFAIAYPRRTRSLVIIDGVSELDPVLTAAVeswksaalsdprvfyrslipwnysagylethlaqlrereelvaglpq 179
Cdd:COG2267 112 IALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------------------------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 180 eyfqafaslcDAFAEIDLTPRLEMIQCPSLVMVGEND-ILKHRGFARIIADNIAGSRLEIIPSAGHAVVIEQPGE-VARR 257
Cdd:COG2267 145 ----------RWLRALRLAEALARIDVPVLVLHGGADrVVPPEAARRLAARLSPDVELVLLPGARHELLNEPAREeVLAA 214
|
....*..
gi 609242772 258 THDFLKQ 264
Cdd:COG2267 215 ILAWLER 221
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
53-249 |
5.44e-08 |
|
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
Pssm-ID: 463473 [Multi-domain] Cd Length: 238 Bit Score: 52.22 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 53 HDFRGQLFSEKPRGGY-SLQNHADDTVQLMDHLGIETAD----IIGTSYGSEVAMEFAIAYPRRTRSLVIID---GVSEL 124
Cdd:pfam12146 37 YDHRGHGRSDGKRGHVpSFDDYVDDLDTFVDKIREEHPGlplfLLGHSMGGLIAALYALRYPDKVDGLILSApalKIKPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 125 DPVLTAAVESWKSAalsdpRVFYRSLIPWNYSAGYLETHLAQLR--EREELVAGLPQeyFQAFASLCDAFAeiDLTPRLE 202
Cdd:pfam12146 117 LAPPILKLLAKLLG-----KLFPRLRVPNNLLPDSLSRDPEVVAayAADPLVHGGIS--ARTLYELLDAGE--RLLRRAA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 609242772 203 MIQCPSLVMVGENDILKHRGFARIIADNIAGS--RLEIIPSAGHAVVIE 249
Cdd:pfam12146 188 AITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPGLYHELLNE 236
|
|
| MET2 |
COG2021 |
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ... |
78-144 |
7.35e-08 |
|
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441624 [Multi-domain] Cd Length: 355 Bit Score: 52.40 E-value: 7.35e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 609242772 78 VQLMDHLGIET-ADIIGTSYGSEVAMEFAIAYPRRTRSLVIIDGVSELDPVLTAAVESWKSAALSDPR 144
Cdd:COG2021 118 KRLLDHLGIERlAAVIGGSMGGMQALEWAVSYPDRVRRAIVIATAARLSAQNIAFNEVQRQAIRADPN 185
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
25-264 |
4.44e-07 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 49.53 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 25 LLLNGIGMSMNHWMPFVDAYSQHA-PFLLHDFRGQLFSE-KPRG-GYSLQNHADDTVQ-LMDHLGIETADI--IGTSYGS 98
Cdd:COG1073 41 VVAHGNGGVKEQRALYAQRLAELGfNVLAFDYRGYGESEgEPREeGSPERRDARAAVDyLRTLPGVDPERIglLGISLGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 99 EVAMEfaiayprrtrslviidgvseldpvltaaveswksAALSDPRVfyRSLIPWnysAGYLET-HLAQLREREELVAGL 177
Cdd:COG1073 121 GYALN----------------------------------AAATDPRV--KAVILD---SPFTSLeDLAAQRAKEARGAYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 178 PQEYFQAFASLCDAFA-EIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGS-RLEIIPSAGHAVVIEQPGEVA 255
Cdd:COG1073 162 PGVPYLPNVRLASLLNdEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPkELLIVPGAGHVDLYDRPEEEY 241
|
250
....*....|
gi 609242772 256 RRT-HDFLKQ 264
Cdd:COG1073 242 FDKlAEFFKK 251
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
29-264 |
1.53e-06 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 48.09 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 29 GIGMSMNHWMPFVDAYSQH--ApFLLHDFRGQLFSEKPRGGYSLqnhaDDTVQLMDHLgIETAD-------IIGTSYGSE 99
Cdd:COG1506 32 GPGSRDDSFLPLAQALASRgyA-VLAPDYRGYGESAGDWGGDEV----DDVLAAIDYL-AARPYvdpdrigIYGHSYGGY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 100 VAMEFAIAYPRRTRSLVIIDGVSeldpvltaaveswksaalsDPRVFYRSLIPWNysagylethlaqlrereELVAGLPQ 179
Cdd:COG1506 106 MALLAAARHPDRFKAAVALAGVS-------------------DLRSYYGTTREYT-----------------ERLMGGPW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 180 EYFqafaslcDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAG----SRLEIIPSAGHAVVIEQPGEVA 255
Cdd:COG1506 150 EDP-------EAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKagkpVELLVYPGEGHGFSGAGAPDYL 222
|
....*....
gi 609242772 256 RRTHDFLKQ 264
Cdd:COG1506 223 ERILDFLDR 231
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
91-265 |
3.10e-06 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 47.24 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 91 IIGTSYGSEVAMEFAIAYPRrtrslviIDGVseldpVLTAAveswkSAALSDPRVFyrsLIPW-NYSAGYLETHLAQLRE 169
Cdd:COG1647 88 VIGLSMGGLLALLLAARYPD-------VAGL-----VLLSP-----ALKIDDPSAP---LLPLlKYLARSLRGIGSDIED 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 170 REELVAGLPQEYFQAFASLCDAFAEIDltPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEII--PSAGHAVV 247
Cdd:COG1647 148 PEVAEYAYDRTPLRALAELQRLIREVR--RDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVwlEDSGHVIT 225
|
170
....*....|....*....
gi 609242772 248 I-EQPGEVARRTHDFLKQL 265
Cdd:COG1647 226 LdKDREEVAEEILDFLERL 244
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
91-251 |
6.39e-06 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 46.83 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 91 IIGTSYGSEVAMEFAIAYPRRTRSLVIID--GVS----ELDPVLTAAVESWKSAALS-------DPRVFYRSLIPW---- 153
Cdd:PLN02894 180 LLGHSFGGYVAAKYALKHPEHVQHLILVGpaGFSsesdDKSEWLTKFRATWKGAVLNhlwesnfTPQKIIRGLGPWgpnl 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 154 --NYSAGYLETHLA--QLREREelvAGLPQEYF------QAFASLC-------DAFAEIDLTPRLEMIQCPSLVMVGEND 216
Cdd:PLN02894 260 vrRYTTARFGAHSTgdILSEEE---SKLLTDYVyhtlaaKASGELClkyifsfGAFARKPLLESASEWKVPTTFIYGRHD 336
|
170 180 190
....*....|....*....|....*....|....*
gi 609242772 217 ILKHRGFARIIADNIAGSRLEIIPSAGHAVVIEQP 251
Cdd:PLN02894 337 WMNYEGAVEARKRMKVPCEIIRVPQGGHFVFLDNP 371
|
|
| PRK10673 |
PRK10673 |
esterase; |
74-119 |
1.06e-05 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 45.49 E-value: 1.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 609242772 74 ADDTVQLMDHLGIETADIIGTSYGSEVAMEFAIAYPRRTRSLVIID 119
Cdd:PRK10673 68 AQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
|
|
| PRK08775 |
PRK08775 |
homoserine O-succinyltransferase; |
69-130 |
1.94e-05 |
|
homoserine O-succinyltransferase;
Pssm-ID: 181553 [Multi-domain] Cd Length: 343 Bit Score: 45.17 E-value: 1.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 609242772 69 SLQNHADDTVQLMDHLGIETAD-IIGTSYGSEVAMEFAIAYPRRTRSLVIIDGVSELDPVLTA 130
Cdd:PRK08775 119 DTADQADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPARVRTLVVVSGAHRAHPYAAA 181
|
|
| metX |
PRK00175 |
homoserine O-acetyltransferase; Provisional |
78-118 |
4.40e-05 |
|
homoserine O-acetyltransferase; Provisional
Pssm-ID: 234678 [Multi-domain] Cd Length: 379 Bit Score: 44.03 E-value: 4.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 609242772 78 VQLMDHLGIET-ADIIGTSYGSEVAMEFAIAYPRRTRSLVII 118
Cdd:PRK00175 137 ARLLDALGITRlAAVVGGSMGGMQALEWAIDYPDRVRSALVI 178
|
|
| PRK03204 |
PRK03204 |
haloalkane dehalogenase; Provisional |
54-150 |
3.75e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179554 [Multi-domain] Cd Length: 286 Bit Score: 41.00 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 54 DFRGQLFSEKPRG-GYSLQNHADDTVQLMDHLGIETADIIGTSYGSEVAMEFAIAYPRRTRSLVIidGVSELDPVLTAAV 132
Cdd:PRK03204 67 DYLGFGLSERPSGfGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVL--GNTWFWPADTLAM 144
|
90
....*....|....*...
gi 609242772 133 ESWkSAALSDPRVFYRSL 150
Cdd:PRK03204 145 KAF-SRVMSSPPVQYAIL 161
|
|
| Ndr |
pfam03096 |
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ... |
69-263 |
3.80e-04 |
|
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).
Pssm-ID: 397285 [Multi-domain] Cd Length: 285 Bit Score: 41.18 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 69 SLQNHADDTVQLMDHLGIETADIIGTSYGSEVAMEFAIAYPRRTRSLVIIDGVSELDPVLTAAVESWKSAALSDPRV--F 146
Cdd:pfam03096 81 SMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLLYYYGMtdS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 147 YRSLIPWNY-SAGYLETHLAQLREREELVAGLP-----QEYFQAFASlcdafaEIDLTPRLEMI--QCPSLVMVGEN--- 215
Cdd:pfam03096 161 AKDYLLAHYfGKEELSNNSDIVQEYRKFLKERLnpknlQLYLEAYNS------RRDLTIERPGLetKCPVLLVVGDNsph 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 609242772 216 --DILK-HRgfariIADNIAGSRLEIIPSAGhAVVIEQPGEVARRTHDFLK 263
Cdd:pfam03096 235 vdAVVEcNT-----KLDPTKTTLLKVADCGG-LVQQEQPGKLTESFKLFLQ 279
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
5-265 |
9.41e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 39.98 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 5 VTIRDCSIGYElKNGEGVTKLLLNGIGMSMNHW---MPFVdaySQHAPFLLHDFRGQLFSEKPRGGYSLQNHADDTVQLM 81
Cdd:PRK03592 12 VEVLGSRMAYI-ETGEGDPIVFLHGNPTSSYLWrniIPHL---AGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 82 DHLGIETADIIGTSYGSEVAMEFAIAYPRRTRSLVIIDGVS------ELDPVLTAAVESWKSAALSDPRV-----FYRSL 150
Cdd:PRK03592 88 DALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVrpmtwdDFPPAVRELFQALRSPGEGEEMVleenvFIERV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 151 IPWNYSAGYLETHLAQLRE---------------REELVAGLPQEYFQAFASLCDAFAEIDLtprlemiqcPSLVMVGEN 215
Cdd:PRK03592 168 LPGSILRPLSDEEMAVYRRpfptpesrrptlswpRELPIDGEPADVVALVEEYAQWLATSDV---------PKLLINAEP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 609242772 216 DILKHRGFAR-IIADNIAGSRLEIIPSAGHAVVIEQPGEVARRTHDFLKQL 265
Cdd:PRK03592 239 GAILTTGAIRdWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRRL 289
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
19-253 |
1.12e-03 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 39.62 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 19 GEGVTKL-LLNGIGMSMNHWMPFVDAYSQHAPFLLHDFRGQLFSEkprgGYSLQNHADDTVQLMDHlGIETADIIGTSYG 97
Cdd:PRK10349 10 GQGNVHLvLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR----GFGALSLADMAEAVLQQ-APDKAIWLGWSLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 98 SEVAMEFAIAYPRRTRSLVII---------DGVSELDPVLTAAVESwksaALSD--PRVFYRSLIPWNYSAgylETHLAQ 166
Cdd:PRK10349 85 GLVASQIALTHPERVQALVTVasspcfsarDEWPGIKPDVLAGFQQ----QLSDdfQRTVERFLALQTMGT---ETARQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 167 LREREELVAGLPQEYFQAFASLCDAFAEIDLTPRLEMIQCPSLVMVGENDILKHRGFARIIADNIAGSRLEIIPSAGHAV 246
Cdd:PRK10349 158 ARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAP 237
|
....*..
gi 609242772 247 VIEQPGE 253
Cdd:PRK10349 238 FISHPAE 244
|
|
| PRK06765 |
PRK06765 |
homoserine O-acetyltransferase; Provisional |
80-143 |
6.18e-03 |
|
homoserine O-acetyltransferase; Provisional
Pssm-ID: 235859 [Multi-domain] Cd Length: 389 Bit Score: 37.37 E-value: 6.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 609242772 80 LMDHLGIETAD-IIGTSYGSEVAMEFAIAYPRRTRSLVIIDGVSELDPVL-TAAVESWKSAALSDP 143
Cdd:PRK06765 153 LIKSLGIARLHaVMGPSMGGMQAQEWAVHYPHMVERMIGVIGNPQNDAWTsVNVLQNWAEAIRLDP 218
|
|
| PLN02578 |
PLN02578 |
hydrolase |
6-119 |
6.85e-03 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 37.51 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609242772 6 TIRDCSIGYeLKNGEGVTKLLLNGIGMSMNHW---MPfvDAYSQHAPFLLhDFRGQLFSEKPRGGYSLQNHADDTVQLMD 82
Cdd:PLN02578 72 TWRGHKIHY-VVQGEGLPIVLIHGFGASAFHWrynIP--ELAKKYKVYAL-DLLGFGWSDKALIEYDAMVWRDQVADFVK 147
|
90 100 110
....*....|....*....|....*....|....*..
gi 609242772 83 HLGIETADIIGTSYGSEVAMEFAIAYPRRTRSLVIID 119
Cdd:PLN02578 148 EVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLN 184
|
|
| |
