|
Name |
Accession |
Description |
Interval |
E-value |
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-289 |
2.35e-167 |
|
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: 465.26 E-value: 2.35e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 4 GSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATA 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 84 EAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIREA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 164 TGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
3I7R_B 244 FVEPNPIPVKWACKELGLVATdTLRLPMTPITDSGRETVRAALKHA 289
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEG-ELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-289 |
4.60e-164 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 457.21 E-value: 4.60e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 1 MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 81 ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 161 REATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
3I7R_B 241 NKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-286 |
1.25e-159 |
|
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: 445.40 E-value: 1.25e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 2 FTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANA 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 82 TAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIR 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 162 EATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHN 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3I7R_B 242 KLFVEPNPIPVKWACKELGLvATDTLRLPMTPITDSGRETVRAAL 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGL-ISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-292 |
8.93e-142 |
|
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: 400.68 E-value: 8.93e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 1 MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 81 ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 161 REATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
3I7R_B 241 NKLFVEPNPIPVKWACKELGLvATDTLRLPMTPITDSGRETVRAALKHAGLL 292
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGL-PSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
1-292 |
2.03e-90 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 269.97 E-value: 2.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 1 MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN 80
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 81 ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAehtDL-PQILYNVPSRTGCDLLPETVGRLAKVKNIIG 159
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVL---DMgPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 160 IREATGNltrvNQIKELVSDDFVLLSGDDASALDF-MQLGGHGVISVTANVAARdmaQMCKLAAEGhfaEARVINQRLMP 238
Cdd:PLN02417 158 VKECTGN----DRVKQYTEKGILLWSGNDDECHDArWDYGADGVISVTSNLVPG---LMHKLMFAG---KNKELNDKLLP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
3I7R_B 239 LHNKLFVEPNPIPVKWACKELGLVATdTLRLPMTPITDSGRETVRAALKHAGLL 292
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRP-VFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-289 |
2.35e-167 |
|
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: 465.26 E-value: 2.35e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 4 GSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATA 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 84 EAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIREA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 164 TGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
3I7R_B 244 FVEPNPIPVKWACKELGLVATdTLRLPMTPITDSGRETVRAALKHA 289
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEG-ELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-289 |
4.60e-164 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 457.21 E-value: 4.60e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 1 MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 81 ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 161 REATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
3I7R_B 241 NKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-286 |
1.25e-159 |
|
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: 445.40 E-value: 1.25e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 2 FTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANA 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 82 TAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIR 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 162 EATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHN 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3I7R_B 242 KLFVEPNPIPVKWACKELGLvATDTLRLPMTPITDSGRETVRAAL 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGL-ISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-292 |
8.93e-142 |
|
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: 400.68 E-value: 8.93e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 1 MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 81 ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 161 REATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
3I7R_B 241 NKLFVEPNPIPVKWACKELGLvATDTLRLPMTPITDSGRETVRAALKHAGLL 292
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGL-PSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-286 |
7.68e-116 |
|
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: 334.52 E-value: 7.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 6 IVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEA 85
Cdd:cd00408 2 IPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 86 ISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIREATG 165
Cdd:cd00408 82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 166 NLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFV 245
Cdd:cd00408 162 DLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
3I7R_B 246 EPNPIPVKWACKELGLvATDTLRLPMTPITDSGRETVRAAL 286
Cdd:cd00408 242 EGNPAPVKAALALLGL-DAGPVRLPLVPLSEEERAKLEALL 281
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
1-292 |
2.03e-90 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 269.97 E-value: 2.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 1 MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN 80
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 81 ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAehtDL-PQILYNVPSRTGCDLLPETVGRLAKVKNIIG 159
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVL---DMgPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 160 IREATGNltrvNQIKELVSDDFVLLSGDDASALDF-MQLGGHGVISVTANVAARdmaQMCKLAAEGhfaEARVINQRLMP 238
Cdd:PLN02417 158 VKECTGN----DRVKQYTEKGILLWSGNDDECHDArWDYGADGVISVTSNLVPG---LMHKLMFAG---KNKELNDKLLP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
3I7R_B 239 LHNKLFVEPNPIPVKWACKELGLVATdTLRLPMTPITDSGRETVRAALKHAGLL 292
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRP-VFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
3-287 |
5.42e-44 |
|
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: 151.31 E-value: 5.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 3 TGSIVAIVTPMDEKGNVCRASLKKLIDYHV-ASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANA 81
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIeKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 82 TAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHT-DLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI 160
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 161 REATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARvinqRLMPLH 240
Cdd:cd00954 162 KFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTAR----ELQHVI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
3I7R_B 241 NKL--FVEPNPI-PV-KWACKELGLVATDTlRLPMTPITDSGRETVRAALK 287
Cdd:cd00954 238 NDVitVLIKNGLyPTlKAILRLMGLDAGPC-RLPLRKVTEKALAKAKELAA 287
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-287 |
2.23e-34 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 126.26 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 2 FTGSIVAIVTPMDEKGNVCRASLKKLIDYHVA-SGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN 80
Cdd:PRK04147 4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 81 ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI 160
Cdd:PRK04147 84 NTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 161 REATGNLTRVNQIKELVSDDfVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEAR---------- 230
Cdd:PRK04147 164 KQTAGDLYQLERIRKAFPDK-LIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQelqhecndvi 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
3I7R_B 231 --VINQRLMPLhnklfvepnpipVKWACKELGlVATDTLRLPMTPITDSGRETVRAALK 287
Cdd:PRK04147 243 dlLIKNGVYPG------------LKEILHYMG-VDAGLCRKPFKPVDEKYLPALKALAA 288
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
10-186 |
1.18e-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: 116.27 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 10 VTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANaTAEAISLT 89
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 90 QRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNvpsRTGCDLLPETVGRLA-KVKNIIGIREATGNLT 168
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAeRCPNLVGFKDGVGDIE 164
|
170
....*....|....*...
3I7R_B 169 RVNQIKELVSDDFVLLSG 186
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGG 182
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
10-186 |
5.77e-30 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 114.53 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 10 VTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANaTAEAISLT 89
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG-TAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 90 QRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNvpsRTGCDLLPETVGRLA-KVKNIIGIREATGNLT 168
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAeRCPNLVGFKDGVGDIE 171
|
170
....*....|....*...
3I7R_B 169 RVNQIKELVSDDFVLLSG 186
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGG 189
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
26-188 |
2.70e-15 |
|
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: 74.40 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 26 KLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTP 105
Cdd:cd00952 33 RLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 106 YYNRPSQEGLYQHFKAIAEHT-DLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIREaTGNLTRVNQIKELVSDDFVLL 184
Cdd:cd00952 113 MWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKY-LGDIGALLSDLAAVKGRMRLL 191
|
....
3I7R_B 185 SGDD 188
Cdd:cd00952 192 PLED 195
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
5-244 |
1.01e-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: 72.41 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 5 SIVAIVTPMdeKGNVC-----RASLKKLIDyhvaSGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGA 79
Cdd:cd00953 4 KITPVITPF--TGNKIdkekfKKHCENLIS----KGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITDKVIFQVGSLNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 80 NataEAISLTQRFNDSGIVGCLTVTPYY-NRPSQEGLYQHFKAIAEHtdLPQILYNVPSRTGCDLLPETVGRLAKVK-NI 157
Cdd:cd00953 78 E---ESIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIKKAGgDI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 158 IGIREATGNLTRVNQIKELVsDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMcklaAEGHFAEARVINQRlm 237
Cdd:cd00953 153 IGVKDTNEDISHMLEYKRLV-PDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKI----KDHVAIEDAFKLQF-- 225
|
....*..
3I7R_B 238 pLHNKLF 244
Cdd:cd00953 226 -LINEVL 231
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
9-204 |
3.18e-06 |
|
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: 46.94 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 9 IVTPMDeKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESAtlnHDEhadvvmmtldLADGRIPVIA----GTGANATAE 84
Cdd:cd00945 1 IDLTLL-HPDATLEDIAKLCDEAIEYGFAAVCVNPGYVRLA---ADA----------LAGSDVPVIVvvgfPTGLTTTEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I7R_B 85 AISLTQRFNDSGIVGCLTVTPYYNRPS--QEGLYQHFKAIAEH--TDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI 160
Cdd:cd00945 67 KVAEVEEAIDLGADEIDVVINIGSLKEgdWEEVLEEIAAVVEAadGGLPLKVILETRGLKTADEIAKAARIAAEAGADFI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
3I7R_B 161 REATG------NLTRVNQIKELVSDDF-VLLSGDD---ASALDFMQLGGHGVIS 204
Cdd:cd00945 147 KTSTGfggggaTVEDVKLMKEAVGGRVgVKAAGGIktlEDALAAIEAGADGIGT 200
|
|
| |
