|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-286 |
5.24e-153 |
|
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: 428.84 E-value: 5.24e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 2 FSGSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANA 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 82 THESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVALK 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 162 DATGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLHK 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490872271 242 NLFVESNPIPVKWAVHKMGLIaEGGLRLPLTELSKPAQPVVAQAM 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLI-SGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-289 |
6.47e-142 |
|
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: 400.94 E-value: 6.47e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 4 GSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANATH 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 84 ESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVALKDA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 164 TGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLHKNL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490872271 244 FVESNPIPVKWAVHKMGLIaEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLI-EGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-289 |
2.44e-141 |
|
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: 399.53 E-value: 2.44e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 1 MFSGSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGAN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 81 ATHESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVAL 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 161 KDATGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490872271 241 KNLFVESNPIPVKWAVHKMGlIAEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:COG0329 241 RALFAEGNPAPVKAALALLG-LPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-289 |
9.02e-139 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 392.89 E-value: 9.02e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 1 MFSGSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGAN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 81 ATHESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVAL 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 161 KDATGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490872271 241 KNLFVESNPIPVKWAVHKMGLIAEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
4-289 |
1.20e-87 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 263.04 E-value: 1.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 4 GSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANATH 83
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 84 ESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSdvPQILYNVPGRTAVDLLPETVARLAEIENIVALKDA 163
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 164 TGDlDRIaihRELCGEDFILLSGDDLTGLEFV-KRGGDGVISVTNNVAAadmATMFKLAKEGKfeeAEAINERLMPLHKN 242
Cdd:PLN02417 162 TGN-DRV---KQYTEKGILLWSGNDDECHDARwDYGADGVISVTSNLVP---GLMHKLMFAGK---NKELNDKLLPLMDW 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490872271 243 LFVESNPIPVKWAVHKMGLIaEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:PLN02417 232 LFCEPNPIGLNTALAQLGLI-RPVFRLPYVPLDLAKRAEFVALVKAI 277
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-286 |
5.24e-153 |
|
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: 428.84 E-value: 5.24e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 2 FSGSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANA 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 82 THESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVALK 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 162 DATGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLHK 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490872271 242 NLFVESNPIPVKWAVHKMGLIaEGGLRLPLTELSKPAQPVVAQAM 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLI-SGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-289 |
6.47e-142 |
|
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: 400.94 E-value: 6.47e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 4 GSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANATH 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 84 ESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVALKDA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 164 TGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLHKNL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490872271 244 FVESNPIPVKWAVHKMGLIaEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLI-EGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-289 |
2.44e-141 |
|
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: 399.53 E-value: 2.44e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 1 MFSGSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGAN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 81 ATHESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVAL 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 161 KDATGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490872271 241 KNLFVESNPIPVKWAVHKMGlIAEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:COG0329 241 RALFAEGNPAPVKAALALLG-LPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-289 |
9.02e-139 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 392.89 E-value: 9.02e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 1 MFSGSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGAN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 81 ATHESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVAL 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 161 KDATGDLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490872271 241 KNLFVESNPIPVKWAVHKMGLIAEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-286 |
5.70e-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: 337.60 E-value: 5.70e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 6 IVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANATHES 85
Cdd:cd00408 2 IPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 86 VLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVALKDATG 165
Cdd:cd00408 82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 166 DLDRIAIHRELCGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLHKNLFV 245
Cdd:cd00408 162 DLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490872271 246 ESNPIPVKWAVHKMGLIAeGGLRLPLTELSKPAQPVVAQAM 286
Cdd:cd00408 242 EGNPAPVKAALALLGLDA-GPVRLPLVPLSEEERAKLEALL 281
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
4-289 |
1.20e-87 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 263.04 E-value: 1.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 4 GSIVALVTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANATH 83
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 84 ESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSdvPQILYNVPGRTAVDLLPETVARLAEIENIVALKDA 163
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 164 TGDlDRIaihRELCGEDFILLSGDDLTGLEFV-KRGGDGVISVTNNVAAadmATMFKLAKEGKfeeAEAINERLMPLHKN 242
Cdd:PLN02417 162 TGN-DRV---KQYTEKGILLWSGNDDECHDARwDYGADGVISVTSNLVP---GLMHKLMFAGK---NKELNDKLLPLMDW 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490872271 243 LFVESNPIPVKWAVHKMGLIaEGGLRLPLTELSKPAQPVVAQAMTEA 289
Cdd:PLN02417 232 LFCEPNPIGLNTALAQLGLI-RPVFRLPYVPLDLAKRAEFVALVKAI 277
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
3-285 |
5.00e-46 |
|
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: 156.70 E-value: 5.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 3 SGSIVALVTPFNTDGEVDFDSLKKLVEHHV-AAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANA 81
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIeKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 82 THESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAI-AEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVAL 160
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIiAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 161 KDATGDLDRIAIHRELCGEDFILLSGDD---LTGLEFvkrGGDGVISVTNNVAAADMATMFKLAKEGKFEEAE----AIN 233
Cdd:cd00954 162 KFTATDLYDLERIRAASPEDKLVLNGFDemlLSALAL---GADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARelqhVIN 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490872271 234 ERLMPLHKNLFVESNpipvKWAVHKMGLIAeGGLRLPLTELSKPAQPVVAQA 285
Cdd:cd00954 239 DVITVLIKNGLYPTL----KAILRLMGLDA-GPCRLPLRKVTEKALAKAKEL 285
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
10-186 |
5.68e-37 |
|
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: 132.83 E-value: 5.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 10 VTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANaTHESVLFS 89
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 90 RLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNvpgRTAVDLLPETVARLAE-IENIVALKDATGDLD 168
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAErCPNLVGFKDGVGDIE 164
|
170
....*....|....*...
gi 490872271 169 RIAIHRELCGEDFILLSG 186
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGG 182
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
4-232 |
3.74e-35 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 128.19 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 4 GSIVALVTPFNTDGEVDFDSLKKLVEHHVAA-GSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANAT 82
Cdd:PRK04147 6 GVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSVNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 83 HESVLFSRLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNVPGRTAVDLLPETVARLAEIENIVALKD 162
Cdd:PRK04147 86 AEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGVKQ 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872271 163 ATGD---LDRI-AIHrelcgEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAI 232
Cdd:PRK04147 166 TAGDlyqLERIrKAF-----PDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQEL 234
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
10-186 |
2.10e-33 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 123.77 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 10 VTPFNTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANaTHESVLFS 89
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG-TAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 90 RLLNGSGIAGCLSVTPYYNKPTQEGLYQHYKAIAEVSDVPQILYNvpgRTAVDLLPETVARLAE-IENIVALKDATGDLD 168
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAErCPNLVGFKDGVGDIE 171
|
170
....*....|....*...
gi 490872271 169 RIAIHRELCGEDFILLSG 186
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGG 189
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
19-244 |
5.31e-26 |
|
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: 104.45 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 19 VDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANATHESVLFSRLLNGSGIA 98
Cdd:cd00952 26 VDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 99 GCLSVTPYYNKPTQEGLYQHYKAIAE-VSDVPQILYNVPGRTAVDLLPETVARLAEIENIVALKdATGDLDRIAIHRELC 177
Cdd:cd00952 106 GTMLGRPMWLPLDVDTAVQFYRDVAEaVPEMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAK-YLGDIGALLSDLAAV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872271 178 GEDFILLSGDD--LTGLEFVKRGGDGVISVTNNVAAADMATMFKLAKEGKFEEAEAINERLMPLHKNLF 244
Cdd:cd00952 185 KGRMRLLPLEDdyYAAARLFPEEVTAFWSSGAACGPAPVTALRDAVATGDWTDARALTDRMRWAAEPLF 253
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
5-217 |
1.51e-16 |
|
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: 77.81 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 5 SIVALVTPFnTDGEVDFDSLKKLVEHHVAAGSDGLVAVGTTGESSTLTIEEHVKVVNKIVEFADGRIPVIAGTGANathE 84
Cdd:cd00953 4 KITPVITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITDKVIFQVGSLNLE---E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872271 85 SVLFSRLLNGSGIAGCLSVTPYY-NKPTQEGLYQHYKAIAEVsdVPQILYNVPGRTAVDLLPETVARLAEI-ENIVALKD 162
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIKKAgGDIIGVKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490872271 163 ATGDLDRIAIHRELcGEDFILLSGDDLTGLEFVKRGGDGVISVTNNVAAADMATM 217
Cdd:cd00953 158 TNEDISHMLEYKRL-VPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKI 211
|
|
| |
