|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
2-290 |
1.62e-101 |
|
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: 298.99 E-value: 1.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 2 KFEGIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAI 81
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 82 RTEDSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAI 161
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 162 KESSGSTAQLHRLACRHP-RIALSCGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQACvVENDFAKGRRIMAAMMPL 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGdDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAA-LAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15599383 241 MDFLESGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVARLK 290
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-286 |
6.13e-97 |
|
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: 287.14 E-value: 6.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 6 IYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIRTED 85
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 86 SLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIKESS 165
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 166 GSTAQLHRLACR-HPRIALSCGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQACvVENDFAKGRRIMAAMMPLMDFL 244
Cdd:cd00408 161 GDLDRLTRLIALlGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAA-RAGDLEEARALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15599383 245 ESGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIV 286
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
2-286 |
9.23e-57 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 184.49 E-value: 9.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 2 KFEGIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAI 81
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 82 RTEDSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAI 161
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 162 KESSGSTAQLHRLACR-HPRIALSCGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQAcVVENDFAKGRRIMAAMMPL 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEaGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKA-LKNGDLATAALINHKLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15599383 241 MDFLESGHFVQSIKHGCELAGLRAG-GVRAPLKALDEAGKAALAEIV 286
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGpTCRLPLTPLSEEERPELEAIL 286
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-289 |
3.86e-55 |
|
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: 180.22 E-value: 3.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 5 GIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIRTE 84
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 85 DSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIKES 164
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 165 SGSTAQLHRLACRHPR-IALSCGWDDQALEFFAWGARSWVCAGSNFIPgEHLALYQACVVENDFAKGRRIMAAMMPLMDF 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDdFVVLSGDDALTLPMMALGGKGVISVTANVAP-KLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15599383 244 LesghFVQS----IKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVARL 289
Cdd:TIGR00674 240 L----FIETnpipVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
5-302 |
3.20e-35 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 128.61 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 5 GIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIRTE 84
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 85 DSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVdrAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIKES 164
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETV--LDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 165 SGSTaqlhRLACRHPR-IALSCGWDDQALEF-FAWGARSWVCAGSNFIPGEHLALYQAcvvendfAKGRRIMAAMMPLMD 242
Cdd:PLN02417 162 TGND----RVKQYTEKgILLWSGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFA-------GKNKELNDKLLPLMD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599383 243 FLesghFVQS----IKHGCELAGLRAGGVRAPLKALDEAgkaalaeivarLKGEVARIVEG-GRH 302
Cdd:PLN02417 231 WL----FCEPnpigLNTALAQLGLIRPVFRLPYVPLDLA-----------KRAEFVALVKAiGRE 280
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
2-290 |
1.62e-101 |
|
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: 298.99 E-value: 1.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 2 KFEGIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAI 81
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 82 RTEDSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAI 161
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 162 KESSGSTAQLHRLACRHP-RIALSCGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQACvVENDFAKGRRIMAAMMPL 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGdDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAA-LAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15599383 241 MDFLESGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVARLK 290
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-286 |
6.13e-97 |
|
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: 287.14 E-value: 6.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 6 IYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIRTED 85
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 86 SLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIKESS 165
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 166 GSTAQLHRLACR-HPRIALSCGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQACvVENDFAKGRRIMAAMMPLMDFL 244
Cdd:cd00408 161 GDLDRLTRLIALlGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAA-RAGDLEEARALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15599383 245 ESGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIV 286
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
3-286 |
5.78e-72 |
|
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: 223.52 E-value: 5.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 3 FEGIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIR 82
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 83 TEDSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIK 162
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 163 ESSGSTAQLHRL-ACRHPRIALSCGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQACvVENDFAKGRRIMAAMMPLM 241
Cdd:cd00950 161 EATGDLDRVSELiALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAA-LAGDLEKARELHRKLLPLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15599383 242 DFLesghFVQS----IKHGCELAGLRAGGVRAPLKALDEAGKAALAEIV 286
Cdd:cd00950 240 KAL----FAEPnpipVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
2-286 |
9.23e-57 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 184.49 E-value: 9.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 2 KFEGIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAI 81
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 82 RTEDSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAI 161
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 162 KESSGSTAQLHRLACR-HPRIALSCGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQAcVVENDFAKGRRIMAAMMPL 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEaGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKA-LKNGDLATAALINHKLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15599383 241 MDFLESGHFVQSIKHGCELAGLRAG-GVRAPLKALDEAGKAALAEIV 286
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGpTCRLPLTPLSEEERPELEAIL 286
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-289 |
3.86e-55 |
|
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: 180.22 E-value: 3.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 5 GIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIRTE 84
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 85 DSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIKES 164
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 165 SGSTAQLHRLACRHPR-IALSCGWDDQALEFFAWGARSWVCAGSNFIPgEHLALYQACVVENDFAKGRRIMAAMMPLMDF 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDdFVVLSGDDALTLPMMALGGKGVISVTANVAP-KLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15599383 244 LesghFVQS----IKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVARL 289
Cdd:TIGR00674 240 L----FIETnpipVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
4-287 |
3.72e-40 |
|
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: 141.68 E-value: 3.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 4 EGIYTPAITPLSADGSIDTQAFAEVLEFLVE-SKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIR 82
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 83 TEDSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAV-DRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAI 161
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIiAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 162 KESSGSTAQLHRLACRHPR--IALScGWDDQALEFFAWGARSWVCAGSNFIPGEHLALYQAcVVENDFAKGRRIMAAMMP 239
Cdd:cd00954 162 KFTATDLYDLERIRAASPEdkLVLN-GFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEA-FNAGDIDTARELQHVIND 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15599383 240 LMDFLESGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVA 287
Cdd:cd00954 240 VITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAKELAA 287
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
5-302 |
3.20e-35 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 128.61 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 5 GIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIRTE 84
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 85 DSLAYAEAARAIGADAILVGSPPYALPTSREIAEHVLAVdrAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIKES 164
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETV--LDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 165 SGSTaqlhRLACRHPR-IALSCGWDDQALEF-FAWGARSWVCAGSNFIPGEHLALYQAcvvendfAKGRRIMAAMMPLMD 242
Cdd:PLN02417 162 TGND----RVKQYTEKgILLWSGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFA-------GKNKELNDKLLPLMD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599383 243 FLesghFVQS----IKHGCELAGLRAGGVRAPLKALDEAgkaalaeivarLKGEVARIVEG-GRH 302
Cdd:PLN02417 231 WL----FCEPnpigLNTALAQLGLIRPVFRLPYVPLDLA-----------KRAEFVALVKAiGRE 280
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-289 |
1.31e-34 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 127.03 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 1 MKFEGIYTPAITPLSADGSIDTQAFAEVLEFLVE-SKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTG 79
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 80 AIRTEDSLAYAEAARAIGADAIlVGSPPYALPTSR-EIAEHVLAVDRAAGLPIMLYNYPARMGVEMDEAFFAAVAGCRNI 158
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAI-SAVTPFYYPFSFeEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 159 VAIKESSGSTAQLHRLACRHPRIALSCGWDDQALEFFAWGARSwvCAGSNF-IPGEHLALYQACVVENDFAKGRRIMAAM 237
Cdd:PRK04147 161 IGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADG--AIGSTYnVNGWRARQIFEAAKAGDIQEAQELQHEC 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15599383 238 MPLMDFLESGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVARL 289
Cdd:PRK04147 239 NDVIDLLIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYLPALKALAAKY 290
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
1-295 |
2.33e-30 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 116.07 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 1 MKFEGIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGA 80
Cdd:PRK03620 6 ILGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 81 iRTEDSLAYAEAARAIGADAILVgSPPYALPTSRE-IAEHVLAVDRAAGLPIMLYNypaRMGVEMDEAFFAAVAG-CRNI 158
Cdd:PRK03620 86 -GTAQAIEYAQAAERAGADGILL-LPPYLTEAPQEgLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAErCPNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 159 VAIKESSGSTAQLHRlacrhprIALSCGwDD------------QALEFFAWGARSWVCAGSNFIPGEHLALYQAcVVEND 226
Cdd:PRK03620 161 VGFKDGVGDIELMQR-------IVRALG-DRllylgglptaevFAAAYLALGVPTYSSAVFNFVPEIALAFYRA-LRAGD 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599383 227 FAKGRRIMAA-MMPLMDF--LESGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVARLKGEVAR 295
Cdd:PRK03620 232 HATVDRLLDDfFLPYVALrnRKKGYAVSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGGAQLPE 303
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
3-288 |
2.57e-30 |
|
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: 115.50 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 3 FEGIYTPAITPLSADGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAiR 82
Cdd:cd00951 1 GSGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 83 TEDSLAYAEAARAIGADAILVgSPPYALPTSRE-IAEHVLAVDRAAGLPIMLYNypaRMGVEMDEAFFAAVA-GCRNIVA 160
Cdd:cd00951 80 TATAIAYAQAAEKAGADGILL-LPPYLTEAPQEgLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAeRCPNLVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 161 IKESSGSTAQLHRLACRHP-RIALSCGW---DDQALEFFAWGARSWVCAGSNFIPGEHLALYQACVVENDFAKGRRIMAA 236
Cdd:cd00951 156 FKDGVGDIELMRRIVAKLGdRLLYLGGLptaEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15599383 237 MMPLMDFLE--SGHFVQSIKHGCELAGLRAGGVRAPLKALDEAGKAALAEIVAR 288
Cdd:cd00951 236 FLPYVDIRNrrKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
8-277 |
1.88e-21 |
|
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: 92.12 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 8 TPAiTPLSAD----GSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALAAHASEVIAGRLPLVVGTGAIRT 83
Cdd:cd00952 11 TPS-KPDASDwratDTVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 84 EDSLAYAEAARAIGADAILVGSPPYALPTS-------REIAEhvlAVDRAAglpIMLYNYPARMGVEMDEAFFAAVAGCR 156
Cdd:cd00952 90 RDTIARTRALLDLGADGTMLGRPMWLPLDVdtavqfyRDVAE---AVPEMA---IAIYANPEAFKFDFPRAAWAELAQIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 157 NIVAIKESSGSTAQLHRLACRHPRIALSCGWDD--QALEFFA------WGarSWVCAGsnfiPGEHLALYQACvVENDFA 228
Cdd:cd00952 164 QVVAAKYLGDIGALLSDLAAVKGRMRLLPLEDDyyAAARLFPeevtafWS--SGAACG----PAPVTALRDAV-ATGDWT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599383 229 KGRRIMAAMMPLMD-FLESGHF-------VQSIKHGCELAG-LRAGGVRAPLKALDEA 277
Cdd:cd00952 237 DARALTDRMRWAAEpLFPRGDFsefskynIALEKARFDAAGyMRAGPARPPYNTAPEA 294
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
6-287 |
5.35e-11 |
|
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: 62.01 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 6 IYTPAITPLSaDGSIDTQAFAEVLEFLVESKVHGIVIGGSTGEYYAHTAEERLALaAHASEVIAGRLPLVVGTgaIRTED 85
Cdd:cd00953 4 KITPVITPFT-GNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLEL-LKAYSDITDKVIFQVGS--LNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 86 SLAYAEAARAIGADAIlVGSPPYALPTSREiaEHVLA--VDRAAGLPIMLYNYP--------ARMGVEMDEAffaavAGC 155
Cdd:cd00953 80 SIELARAAKSFGIYAI-ASLPPYYFPGIPE--EWLIKyfTDISSPYPTFIYNYPkatgydinARMAKEIKKA-----GGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 156 rnIVAIKESSGSTAqlHRLACRH--PRIALSCGWDDQALEFFAWGARSWVCAGSNFIPgeHLALYQACVVENDfaKGRRI 233
Cdd:cd00953 152 --IIGVKDTNEDIS--HMLEYKRlvPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLP--EVFVKIKDHVAIE--DAFKL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 234 MAAMMPLMDFleSGHFVQS------IKhgcELAGLRAGGVRAPLKALDEAGKAALAEIVA 287
Cdd:cd00953 224 QFLINEVLDA--SRKYGSWsanyslVK---IFQGYDAGEPRPPFYPLDEEEEEKLRKEVN 278
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
58-166 |
6.70e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 36.92 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599383 58 LALAAHASEVIAGRLPLVV-----GTGAIRTEDSLAYAEAARAIGADAILVGSPPYALPT--SREIAEHVLAVDRAA--G 128
Cdd:cd00945 34 PGYVRLAADALAGSDVPVIvvvgfPTGLTTTEVKVAEVEEAIDLGADEIDVVINIGSLKEgdWEEVLEEIAAVVEAAdgG 113
|
90 100 110
....*....|....*....|....*....|....*...
gi 15599383 129 LPIMLYNYPARMGVEMDEAFFAAVAGCRNIVAIKESSG 166
Cdd:cd00945 114 LPLKVILETRGLKTADEIAKAARIAAEAGADFIKTSTG 151
|
|
| |
