|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
64-343 |
0e+00 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 598.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 64 KALRVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSN 143
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 144 STREAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMGPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKE 223
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 224 CVGNKRVEEYTENGVVVWSGNDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNSSLNSKLLPLMAWLFHEPNPIG 303
Cdd:PLN02417 161 CTGNDRVKQYTEKGILLWSGNDDECHDARWDYGADGVISVTSNLVPGLMHKLMFAGKNKELNDKLLPLMDWLFCEPNPIG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15225477 304 INTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKEIGRE 343
Cdd:PLN02417 241 LNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
64-340 |
4.04e-123 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 356.29 E-value: 4.04e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 64 KALRVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSN 143
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 144 STREAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMG--PTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGV 221
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATdlPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 222 KECVGN----KRVEEYTENGVVVWSGnDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNS------SLNSKLLPL 291
Cdd:pfam00701 161 KEASGDldrmINIKKEAGPDFVILSG-DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGdlataaLINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15225477 292 MAWLFHEPNPIGINTALAQLGV-SRPVFRLPYVPLPLSKRLEFVKLVKEI 340
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLvVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
67-337 |
1.47e-119 |
|
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.
Pssm-ID: 188637 [Multi-domain] Cd Length: 284 Bit Score: 347.17 E-value: 1.47e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 67 RVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTR 146
Cdd:cd00950 3 GSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 147 EAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLH--MGPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKEC 224
Cdd:cd00950 83 EAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEatDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIKEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 225 VGN----KRVEEYTENGVVVWSGnDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNS------SLNSKLLPLMAW 294
Cdd:cd00950 163 TGDldrvSELIALCPDDFAVLSG-DDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGdlekarELHRKLLPLIKA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15225477 295 LFHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLV 337
Cdd:cd00950 242 LFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
67-341 |
5.45e-82 |
|
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440098 [Multi-domain] Cd Length: 291 Bit Score: 251.61 E-value: 5.45e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 67 RVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTR 146
Cdd:COG0329 4 GVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 147 EAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSV-----LhmgPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGV 221
Cdd:COG0329 84 EAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIaeavdL---PIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 222 KECVGN----KRVEEYTENGVVVWSGNDDECHDSRwDYGATGVISVTSNLVPGLMRKL---MFEGRNS---SLNSKLLPL 291
Cdd:COG0329 161 KEASGDldriAELIRATGDDFAVLSGDDALALPAL-ALGADGVISVTANVAPELMVALyeaALAGDLAearALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15225477 292 MAWLFHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKEIG 341
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
68-339 |
1.48e-73 |
|
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129757 [Multi-domain] Cd Length: 285 Bit Score: 229.91 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 68 VITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTRE 147
Cdd:TIGR00674 2 VITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 148 AIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMG--PTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKECV 225
Cdd:TIGR00674 82 AISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVdlPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 226 GN-KRVEEY---TENGVVVWSGNDDECHDSRwDYGATGVISVTSNLVPGLMRKLM---FEGRNSSL---NSKLLPLMAWL 295
Cdd:TIGR00674 162 GNlERISEIkaiAPDDFVVLSGDDALTLPMM-ALGGKGVISVTANVAPKLMKEMVnnaLEGDFAEAreiHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15225477 296 FHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKE 339
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKD 284
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
64-343 |
0e+00 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 598.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 64 KALRVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSN 143
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 144 STREAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMGPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKE 223
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 224 CVGNKRVEEYTENGVVVWSGNDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNSSLNSKLLPLMAWLFHEPNPIG 303
Cdd:PLN02417 161 CTGNDRVKQYTEKGILLWSGNDDECHDARWDYGADGVISVTSNLVPGLMHKLMFAGKNKELNDKLLPLMDWLFCEPNPIG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15225477 304 INTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKEIGRE 343
Cdd:PLN02417 241 LNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
64-340 |
4.04e-123 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 356.29 E-value: 4.04e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 64 KALRVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSN 143
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 144 STREAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMG--PTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGV 221
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATdlPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 222 KECVGN----KRVEEYTENGVVVWSGnDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNS------SLNSKLLPL 291
Cdd:pfam00701 161 KEASGDldrmINIKKEAGPDFVILSG-DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGdlataaLINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15225477 292 MAWLFHEPNPIGINTALAQLGV-SRPVFRLPYVPLPLSKRLEFVKLVKEI 340
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLvVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
67-337 |
1.47e-119 |
|
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.
Pssm-ID: 188637 [Multi-domain] Cd Length: 284 Bit Score: 347.17 E-value: 1.47e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 67 RVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTR 146
Cdd:cd00950 3 GSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 147 EAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLH--MGPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKEC 224
Cdd:cd00950 83 EAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEatDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIKEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 225 VGN----KRVEEYTENGVVVWSGnDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNS------SLNSKLLPLMAW 294
Cdd:cd00950 163 TGDldrvSELIALCPDDFAVLSG-DDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGdlekarELHRKLLPLIKA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15225477 295 LFHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLV 337
Cdd:cd00950 242 LFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
68-337 |
6.50e-86 |
|
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.
Pssm-ID: 188630 [Multi-domain] Cd Length: 281 Bit Score: 261.33 E-value: 6.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 68 VITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTRE 147
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 148 AIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLH--MGPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKECV 225
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADasDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 226 GN----KRVEEYTENGVVVWSGnDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNS------SLNSKLLPLMAWL 295
Cdd:cd00408 161 GDldrlTRLIALLGPDFAVLSG-DDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGdleearALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15225477 296 FHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLV 337
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
67-341 |
5.45e-82 |
|
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440098 [Multi-domain] Cd Length: 291 Bit Score: 251.61 E-value: 5.45e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 67 RVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTR 146
Cdd:COG0329 4 GVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 147 EAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSV-----LhmgPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGV 221
Cdd:COG0329 84 EAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIaeavdL---PIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 222 KECVGN----KRVEEYTENGVVVWSGNDDECHDSRwDYGATGVISVTSNLVPGLMRKL---MFEGRNS---SLNSKLLPL 291
Cdd:COG0329 161 KEASGDldriAELIRATGDDFAVLSGDDALALPAL-ALGADGVISVTANVAPELMVALyeaALAGDLAearALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15225477 292 MAWLFHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKEIG 341
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
68-339 |
1.48e-73 |
|
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129757 [Multi-domain] Cd Length: 285 Bit Score: 229.91 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 68 VITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTRE 147
Cdd:TIGR00674 2 VITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 148 AIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMG--PTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKECV 225
Cdd:TIGR00674 82 AISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVdlPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 226 GN-KRVEEY---TENGVVVWSGNDDECHDSRwDYGATGVISVTSNLVPGLMRKLM---FEGRNSSL---NSKLLPLMAWL 295
Cdd:TIGR00674 162 GNlERISEIkaiAPDDFVVLSGDDALTLPMM-ALGGKGVISVTANVAPKLMKEMVnnaLEGDFAEAreiHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15225477 296 FHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKE 339
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKD 284
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
68-330 |
6.04e-26 |
|
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.
Pssm-ID: 188641 [Multi-domain] Cd Length: 288 Bit Score: 105.08 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 68 VITAIKTPYLPDGRFDLEAYDDLVNIQI-QNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTR 146
Cdd:cd00954 4 LIAALLTPFDENGEINEDVLRAIVDYLIeKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLNLK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 147 EAI----HATEQGFavgmHAALHINPYYGKTSIEGLIAHFQSVLHMG---PTIIYNVPGRTGQDIPPRAIFKLSQNPNLA 219
Cdd:cd00954 84 ESQelakHAEELGY----DAISAITPFYYKFSFEEIKDYYREIIAAAaslPMIIYHIPALTGVNLTLEQFLELFEIPNVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 220 GVKECVGN----KRVEEYTENGVVVWSGNDDECHDSRWdYGATGVISVTSNLVPGLMRKlMFEGRNSSLNSKLLPLMawl 295
Cdd:cd00954 160 GVKFTATDlydlERIRAASPEDKLVLNGFDEMLLSALA-LGADGAIGSTYNVNGKRYRK-IFEAFNAGDIDTARELQ--- 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 15225477 296 fHEPNPIgINTALAQLGVS--RPVFRLPYVPLPLSKR 330
Cdd:cd00954 235 -HVINDV-ITVLIKNGLYPtlKAILRLMGLDAGPCRL 269
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
64-324 |
1.40e-21 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 93.13 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 64 KALR-VITAIKTPYLPDGRFDLEAYDDLVNIQIQ-NGAEGVIVGGTTGEGQLMSWDE--HIMLIGHTVNcfGGSIKVIGN 139
Cdd:PRK04147 2 KNLKgVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEkkQVLEIVAEEA--KGKVKLIAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 140 TGSNSTREAI----HATEQGFavgmHAALHINPYYGKTSIEGLIAHFQSVLHM--GPTIIYNVPGRTGQDIPPRAIFKLS 213
Cdd:PRK04147 80 VGSVNTAEAQelakYATELGY----DAISAVTPFYYPFSFEEICDYYREIIDSadNPMIVYNIPALTGVNLSLDQFNELF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 214 QNPNLAGVKECVGNKRVEEYTENGV---VVWSGNDDECHdSRWDYGATGVISVTSNlVPGLMRKLMFEGRNSSLNSKLLP 290
Cdd:PRK04147 156 TLPKVIGVKQTAGDLYQLERIRKAFpdkLIYNGFDEMFA-SGLLAGADGAIGSTYN-VNGWRARQIFEAAKAGDIQEAQE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15225477 291 LMawlfHEPNPI-----------GINTALAQLGVSRPVFRLPYVP 324
Cdd:PRK04147 234 LQ----HECNDVidllikngvypGLKEILHYMGVDAGLCRKPFKP 274
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
69-275 |
5.99e-14 |
|
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188640 Cd Length: 279 Bit Score: 71.26 E-value: 5.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 69 ITAIKTPYlPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHtvnCFGGSIKVIGNTGSNSTREA 148
Cdd:cd00953 5 ITPVITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKA---YSDITDKVIFQVGSLNLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 149 IHATEQGFAVGMHAALHINPYY-GKTSIEGLIAHFQSVLHMGPTIIYNVPGRTGQDIPPRAIFKLSQNP-NLAGVKECVG 226
Cdd:cd00953 81 IELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISSPYPTFIYNYPKATGYDINARMAKEIKKAGgDIIGVKDTNE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15225477 227 N-KRVEEYT--ENGVVVWSGNDDECHDSrWDYGATGVISVTSNLVPGLMRKL 275
Cdd:cd00953 161 DiSHMLEYKrlVPDFKVYSGPDSLIFSA-LRSGLDGSVAAASNYLPEVFVKI 211
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
74-227 |
4.75e-12 |
|
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH); 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate.
Pssm-ID: 188638 Cd Length: 289 Bit Score: 65.81 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 74 TPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNsTREAIHATE 153
Cdd:cd00951 10 THFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYAQ 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225477 154 QGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMG--PTIIYNvpgRTGQDIPPRAIFKLSQN-PNLAGVKECVGN 227
Cdd:cd00951 89 AAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTdlGVIVYN---RANAVLTADSLARLAERcPNLVGFKDGVGD 162
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
62-222 |
2.52e-10 |
|
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA); Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188639 Cd Length: 309 Bit Score: 60.92 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 62 DIKALRVItaIKTPYLPDGR-------FDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSI 134
Cdd:cd00952 1 DIKGVWAI--VPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 135 KV-IGNTGSNsTREAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMGP---TIIYNVPGRTGQDIPPRAIF 210
Cdd:cd00952 79 PVfVGATTLN-TRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVPemaIAIYANPEAFKFDFPRAAWA 157
|
170
....*....|..
gi 15225477 211 KLSQNPNLAGVK 222
Cdd:cd00952 158 ELAQIPQVVAAK 169
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
74-227 |
7.44e-10 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 59.44 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225477 74 TPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNsTREAIHATE 153
Cdd:PRK03620 17 TPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG-TAQAIEYAQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225477 154 QGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMG--PTIIYNvpgRTGQDIPPRAIFKLS-QNPNLAGVKECVGN 227
Cdd:PRK03620 96 AAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTdlGVIVYN---RDNAVLTADTLARLAeRCPNLVGFKDGVGD 169
|
|
| |
