|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-285 |
1.98e-154 |
|
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: 432.30 E-value: 1.98e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 2 IKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNS 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 82 TAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGIK 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 162 DATGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLHG 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 425721716 242 KLFVEPNPVPVKWALADMGKMPAGLRLPLAPLSAQYHETVRAAL 285
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-291 |
1.61e-143 |
|
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: 404.92 E-value: 1.61e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 1 MIKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 81 STAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGI 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 161 KDATGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 425721716 241 GKLFVEPNPVPVKWALADMGKMPAGLRLPLAPLSAQYHETVRAALVEAGVH 291
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-285 |
3.65e-131 |
|
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: 373.59 E-value: 3.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 4 GSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNSTA 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 84 EAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGIKDA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 164 TGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLHGKL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 425721716 244 FVEPNPVPVKWALADMGkMPAG-LRLPLAPLSAQYHETVRAAL 285
Cdd:TIGR00674 241 FIETNPIPVKTALALLG-LIEGeLRLPLTELSEEHRNKLRDVL 282
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-288 |
3.86e-120 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 345.89 E-value: 3.86e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 1 MIKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 81 STAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGI 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 161 KDATGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 425721716 241 GKLFVEPNPVPVKWALADMG-KMPAGLRLPLAPLSAQYHETVRAALVEA 288
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGlVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
1-289 |
6.06e-91 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 271.52 E-value: 6.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 1 MIKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGN 80
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 81 STAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAesvDL-PIILYNVPGRTVADMANETVARLAPIENIVG 159
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVL---DMgPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 160 IKDATGN--IGrgiellKMVDKSFAVYSG-DDPSAMTLMFCGGAGNISVTANVAPRAMHELcvaAMAGdvaRAVEINNRV 236
Cdd:PLN02417 158 VKECTGNdrVK------QYTEKGILLWSGnDDECHDARWDYGADGVISVTSNLVPGLMHKL---MFAG---KNKELNDKL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 425721716 237 LGLHGKLFVEPNPVPVKWALADMGKMPAGLRLPLAPLSAQYHETVRAALVEAG 289
Cdd:PLN02417 226 LPLMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIG 278
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-285 |
1.98e-154 |
|
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: 432.30 E-value: 1.98e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 2 IKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNS 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 82 TAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGIK 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 162 DATGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLHG 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 425721716 242 KLFVEPNPVPVKWALADMGKMPAGLRLPLAPLSAQYHETVRAAL 285
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-291 |
1.61e-143 |
|
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: 404.92 E-value: 1.61e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 1 MIKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 81 STAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGI 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 161 KDATGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 425721716 241 GKLFVEPNPVPVKWALADMGKMPAGLRLPLAPLSAQYHETVRAALVEAGVH 291
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-285 |
3.65e-131 |
|
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: 373.59 E-value: 3.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 4 GSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNSTA 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 84 EAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGIKDA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 164 TGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLHGKL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 425721716 244 FVEPNPVPVKWALADMGkMPAG-LRLPLAPLSAQYHETVRAAL 285
Cdd:TIGR00674 241 FIETNPIPVKTALALLG-LIEGeLRLPLTELSEEHRNKLRDVL 282
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-288 |
3.86e-120 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 345.89 E-value: 3.86e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 1 MIKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 81 STAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGI 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 161 KDATGNIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 425721716 241 GKLFVEPNPVPVKWALADMG-KMPAGLRLPLAPLSAQYHETVRAALVEA 288
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGlVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-285 |
1.02e-117 |
|
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: 339.14 E-value: 1.02e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 6 IVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNSTAEA 85
Cdd:cd00408 2 IPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 86 IALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGIKDATG 165
Cdd:cd00408 82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 166 NIGRGIELLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEINNRVLGLHGKLFV 245
Cdd:cd00408 162 DLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 425721716 246 EPNPVPVKWALADMGKMPAGLRLPLAPLSAQYHETVRAAL 285
Cdd:cd00408 242 EGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
1-289 |
6.06e-91 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 271.52 E-value: 6.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 1 MIKGSIVALVTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGN 80
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 81 STAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAesvDL-PIILYNVPGRTVADMANETVARLAPIENIVG 159
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVL---DMgPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 160 IKDATGN--IGrgiellKMVDKSFAVYSG-DDPSAMTLMFCGGAGNISVTANVAPRAMHELcvaAMAGdvaRAVEINNRV 236
Cdd:PLN02417 158 VKECTGNdrVK------QYTEKGILLWSGnDDECHDARWDYGADGVISVTSNLVPGLMHKL---MFAG---KNKELNDKL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 425721716 237 LGLHGKLFVEPNPVPVKWALADMGKMPAGLRLPLAPLSAQYHETVRAALVEAG 289
Cdd:PLN02417 226 LPLMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIG 278
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
3-284 |
6.49e-43 |
|
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: 148.61 E-value: 6.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 3 KGSIVALVTPMFEDGSLDRDSLRKLIDWHV-AEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNS 81
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIeKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 82 TAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESV-DLPIILYNVPGRTVADMANETVARLAPIENIVGI 160
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 161 KDATGN---IGRgieLLKMVDKSFAVYSGDD---PSAMTLmfcGGAGNISVTANVAPRAMHELCVAAMAGDVARAVEIN- 233
Cdd:cd00954 162 KFTATDlydLER---IRAASPEDKLVLNGFDemlLSALAL---GADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQh 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 425721716 234 --NRVLGLHGKLFVEPNpvpVKWALADMGkMPAGL-RLPLAPLSAQYHETVRAA 284
Cdd:cd00954 236 viNDVITVLIKNGLYPT---LKAILRLMG-LDAGPcRLPLRKVTEKALAKAKEL 285
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
10-285 |
3.04e-41 |
|
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: 144.00 E-value: 3.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 10 VTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNsTAEAIALT 89
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 90 RHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNvpgRTVADMANETVARLA-PIENIVGIKDATGNIG 168
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAeRCPNLVGFKDGVGDIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 169 RGIEL-LKMVDKSFavYSGDDPSAMTlmFCGGAGNISVTA------NVAPRAMHELCVAAMAGDVARA-----------V 230
Cdd:cd00951 165 LMRRIvAKLGDRLL--YLGGLPTAEV--FALAYLAMGVPTyssavfNFVPEIALAFYAAVRAGDHATVkrllrdfflpyV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 425721716 231 EINNRVLGLHGKLfvepnpvpVKWALADMGKMPAGLRLPLAPLSAQYHETVRAAL 285
Cdd:cd00951 241 DIRNRRKGYAVSI--------VKAGARLVGRDAGPVRPPLTDLTEEELAQLTALI 287
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-284 |
8.95e-41 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 142.83 E-value: 8.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 2 IKGSIVALVTPMFEDGSLDRDSLRKLIDWHVA-EGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGN 80
Cdd:PRK04147 4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 81 STAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNVPGRTVADMANETVARLAPIENIVGI 160
Cdd:PRK04147 84 NTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 161 KDATGNigrgIELLKMVDKSFA---VYSGDDPSAMTLMFCGGAGNISVTANV-APRAMhELCVAAMAGDVARAVEIN--- 233
Cdd:PRK04147 164 KQTAGD----LYQLERIRKAFPdklIYNGFDEMFASGLLAGADGAIGSTYNVnGWRAR-QIFEAAKAGDIQEAQELQhec 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 425721716 234 NRVLGLHGKLFVEPNpvpVKWALADMGkMPAGL-RLPLAPLSAQYHETVRAA 284
Cdd:PRK04147 239 NDVIDLLIKNGVYPG---LKEILHYMG-VDAGLcRKPFKPVDEKYLPALKAL 286
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
10-182 |
5.41e-39 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 138.41 E-value: 5.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 10 VTPMFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVIAGTGGNsTAEAIALT 89
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG-TAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 90 RHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESVDLPIILYNvpgRTVADMANETVARLAP-IENIVGIKDATGNIG 168
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAErCPNLVGFKDGVGDIE 171
|
170
....*....|....
gi 425721716 169 RGIELLKMVDKSFA 182
Cdd:PRK03620 172 LMQRIVRALGDRLL 185
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
2-192 |
5.77e-23 |
|
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: 95.98 E-value: 5.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 2 IKGSIVALVTPMFEDGS-------LDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKLAVDHVAGRIPVI 74
Cdd:cd00952 2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 75 AGTGGNSTAEAIALTRHAKECGADASLQVVPYYNRPTQEGMYRHFRAIAESV-DLPIILYNVPGRTVADMANETVARLAP 153
Cdd:cd00952 82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELAQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 425721716 154 IENIVGIKdATGNIGRGIELLKMVDKSFAVYSGDD---PSAM 192
Cdd:cd00952 162 IPQVVAAK-YLGDIGALLSDLAAVKGRMRLLPLEDdyyAAAR 202
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
5-217 |
1.51e-22 |
|
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: 94.37 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 5 SIVALVTPmFEDGSLDRDSLRKLIDWHVAEGTDAIVIVGTTGESATVSPEEHCELVKlAVDHVAGRipVIAGTGGNSTAE 84
Cdd:cd00953 4 KITPVITP-FTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLK-AYSDITDK--VIFQVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 85 AIALTRHAKECGADASLQVVPYY-NRPTQEGMYRHFRAIAESVdlPIILYNVP---GRTV-ADMANETVARLApieNIVG 159
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISSPY--PTFIYNYPkatGYDInARMAKEIKKAGG---DIIG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 425721716 160 IKDATGNIGRGIElLKMVDKSFAVYSGDDPSAMTLMFCGGAGNISVTANVAPRAMHEL 217
Cdd:cd00953 155 VKDTNEDISHMLE-YKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKI 211
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
16-170 |
1.32e-09 |
|
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: 56.57 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 16 DGSLDRDSLRKLIDWHVAEGTDAIVIVGTTgesatvspeehcelVKLAVDHVAG-RIPVIA----GTGGNSTAEAIALTR 90
Cdd:cd00945 7 HPDATLEDIAKLCDEAIEYGFAAVCVNPGY--------------VRLAADALAGsDVPVIVvvgfPTGLTTTEVKVAEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721716 91 HAKECGADASLQVVPYYNRPT--QEGMYRHFRAIAESVD--LPIILYNVPGRTVADMANETVARLAPIENIVGIKDATGN 166
Cdd:cd00945 73 EAIDLGADEIDVVINIGSLKEgdWEEVLEEIAAVVEAADggLPLKVILETRGLKTADEIAKAARIAAEAGADFIKTSTGF 152
|
....
gi 425721716 167 IGRG 170
Cdd:cd00945 153 GGGG 156
|
|
| |
