|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
4-287 |
3.89e-162 |
|
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: 451.95 E-value: 3.89e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 4 FGTIATAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNN 83
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 84 THASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI* 163
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 164 DAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVTD 243
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
3HIJ_A 244 SLFMAPSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVM 287
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-290 |
7.04e-140 |
|
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: 395.68 E-value: 7.04e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 3 DFGTIATAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSN 82
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 83 NTHASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI 162
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 163 *DAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVT 242
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
3HIJ_A 243 DSLFMAPSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVMQSI 290
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
9-289 |
7.80e-132 |
|
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: 375.13 E-value: 7.80e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 9 TAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHASI 88
Cdd:TIGR00674 4 TALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATEEAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 89 DLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI*DAGGD 168
Cdd:TIGR00674 84 SLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEATGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 169 VLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVTDSLFMA 248
Cdd:TIGR00674 164 LERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKALFIE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
3HIJ_A 249 PSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVMQS 289
Cdd:TIGR00674 244 TNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKD 284
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-290 |
3.15e-124 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 356.29 E-value: 3.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 3 DFGTIATAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSN 82
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 83 NTHASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI 162
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 163 *DAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVT 242
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
3HIJ_A 243 DSLFMAPSPTPVKTALQMVGLDVGS-VRLPLLPLTEEERVTLQSVMQSI 290
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
9-292 |
7.12e-70 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 217.59 E-value: 7.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 9 TAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHASI 88
Cdd:PLN02417 7 TAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTREAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 89 DLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTplPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI*DAGGD 168
Cdd:PLN02417 87 HATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKECTGN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 169 vltmTEIIEKTADDFAVYSGDDGLTLPA-MAVGAKGIVSVASHVIGNEMQEMIAAfqagefKKAQKLHQLLVRVTDSLFM 247
Cdd:PLN02417 165 ----DRVKQYTEKGILLWSGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKLLPLMDWLFC 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3HIJ_A 248 APSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVMQSIPR 292
Cdd:PLN02417 235 EPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGR 279
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
4-287 |
3.89e-162 |
|
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: 451.95 E-value: 3.89e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 4 FGTIATAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNN 83
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 84 THASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI* 163
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 164 DAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVTD 243
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
3HIJ_A 244 SLFMAPSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVM 287
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-290 |
7.04e-140 |
|
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: 395.68 E-value: 7.04e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 3 DFGTIATAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSN 82
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 83 NTHASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI 162
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 163 *DAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVT 242
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
3HIJ_A 243 DSLFMAPSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVMQSI 290
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
9-289 |
7.80e-132 |
|
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: 375.13 E-value: 7.80e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 9 TAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHASI 88
Cdd:TIGR00674 4 TALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATEEAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 89 DLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI*DAGGD 168
Cdd:TIGR00674 84 SLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEATGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 169 VLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVTDSLFMA 248
Cdd:TIGR00674 164 LERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKALFIE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
3HIJ_A 249 PSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVMQS 289
Cdd:TIGR00674 244 TNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKD 284
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
9-287 |
8.13e-126 |
|
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: 359.94 E-value: 8.13e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 9 TAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHASI 88
Cdd:cd00408 3 PALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 89 DLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI*DAGGD 168
Cdd:cd00408 83 ELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 169 VLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVTDSLFMA 248
Cdd:cd00408 163 LDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKE 242
|
250 260 270
....*....|....*....|....*....|....*....
3HIJ_A 249 PSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVM 287
Cdd:cd00408 243 GNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-290 |
3.15e-124 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 356.29 E-value: 3.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 3 DFGTIATAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSN 82
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 83 NTHASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI 162
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 163 *DAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVT 242
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
3HIJ_A 243 DSLFMAPSPTPVKTALQMVGLDVGS-VRLPLLPLTEEERVTLQSVMQSI 290
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
9-292 |
7.12e-70 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 217.59 E-value: 7.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 9 TAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHASI 88
Cdd:PLN02417 7 TAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTREAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 89 DLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTplPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI*DAGGD 168
Cdd:PLN02417 87 HATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKECTGN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 169 vltmTEIIEKTADDFAVYSGDDGLTLPA-MAVGAKGIVSVASHVIGNEMQEMIAAfqagefKKAQKLHQLLVRVTDSLFM 247
Cdd:PLN02417 165 ----DRVKQYTEKGILLWSGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKLLPLMDWLFC 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3HIJ_A 248 APSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVMQSIPR 292
Cdd:PLN02417 235 EPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGR 279
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-285 |
1.84e-63 |
|
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: 201.38 E-value: 1.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 5 GTIAtAMVTPFDINGNIDFAKTTKLVNYLID-NGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNN 83
Cdd:cd00954 3 GLIA-ALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 84 THASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTP-LPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI 162
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAAsLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 163 *DAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVT 242
Cdd:cd00954 162 KFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
3HIJ_A 243 DSLFMAPSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQS 285
Cdd:cd00954 242 TVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAKE 284
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-284 |
7.89e-50 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 166.32 E-value: 7.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 1 MIDFGTIATAMVTPFDINGNIDFAKTTKLVNYLID-NGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGT 79
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 80 GSNNTHASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENI 159
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 160 VAI*DAGGDVLTMtEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLV 239
Cdd:PRK04147 161 IGVKQTAGDLYQL-ERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECN 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
3HIJ_A 240 RVTDSLF-MAPSPTpVKTALQMVGLDVGSVRLPLLPLTEEERVTLQ 284
Cdd:PRK04147 240 DVIDLLIkNGVYPG-LKEILHYMGVDAGLCRKPFKPVDEKYLPALK 284
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
12-287 |
9.47e-39 |
|
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: 137.45 E-value: 9.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 12 VTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNnTHASIDLT 91
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 92 KKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNvpgRSIVQISVDTVVRLSE-IENIVAI*DAGGDVL 170
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAErCPNLVGFKDGVGDIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 171 TMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHV---IGNEMQEMIAAFQAGEFKKAqklHQLLVRVTDSLFM 247
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSAVfnfVPEIALAFYAAVRAGDHATV---KRLLRDFFLPYVD 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
3HIJ_A 248 APSPTP------VKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVM 287
Cdd:cd00951 242 IRNRRKgyavsiVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALI 287
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
12-287 |
4.52e-37 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 133.40 E-value: 4.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 12 VTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHAsIDLT 91
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGGTAQA-IEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 92 KKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNvpgRSIVQISVDTVVRLSE-IENIVAI*DAGGDVL 170
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAErCPNLVGFKDGVGDIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 171 TMTEIIEKTADDFAVYSGddgltLP-----AMAVGAKGiVSVASHVIGNEMQEMIAAF----QAGEFKKAQKLHQ----L 237
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGG-----LPtaevfAAAYLALG-VPTYSSAVFNFVPEIALAFyralRAGDHATVDRLLDdfflP 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
3HIJ_A 238 LVRVTD-------SLfmapsptpVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVM 287
Cdd:PRK03620 246 YVALRNrkkgyavSI--------VKAGARLVGLDAGPVRAPLTDLTPEELAELAALI 294
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
7-289 |
2.86e-30 |
|
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: 115.17 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 7 IATAMVTPFDiNGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKrvpVIAGTGSNNTHA 86
Cdd:cd00953 4 KITPVITPFT-GNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITDK---VIFQVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 87 SIDLTKKATEVGVDAVMLVAPYY-NKPSQEGMYQHFKAIAEstPLPVMLYNVPGRSIVQISVDTVVRlseienivaI*DA 165
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISS--PYPTFIYNYPKATGYDINARMAKE---------IKKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 166 GGDVLTMTEIIEKTA---------DDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHq 236
Cdd:cd00953 149 GGDIIGVKDTNEDIShmleykrlvPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIEDAFKLQFLI- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
3HIJ_A 237 llvrvtDSLFMAPSPTPVKTAL-----QMVGLDVGSVRLPLLPLTEEERVTLQSVMQS 289
Cdd:cd00953 228 ------NEVLDASRKYGSWSANyslvkIFQGYDAGEPRPPFYPLDEEEEEKLRKEVNE 279
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
21-246 |
1.51e-25 |
|
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: 102.91 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 21 IDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHASIDLTKKATEVGVD 100
Cdd:cd00952 26 VDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 101 AVMLVAPYYNKPSQEGMYQHFKAIAESTP-LPVMLYNVPGRSIVQISVDTVVRLSEIENIVAI*DAGGdvltmteiIEKT 179
Cdd:cd00952 106 GTMLGRPMWLPLDVDTAVQFYRDVAEAVPeMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKYLGD--------IGAL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3HIJ_A 180 ADDFAVYSGD------DGLTLPAMAVGAKGIVSVASH--VIGNEMQEMIA-AFQAGEFKKAQKLHQLLVRVTDSLF 246
Cdd:cd00952 178 LSDLAAVKGRmrllplEDDYYAAARLFPEEVTAFWSSgaACGPAPVTALRdAVATGDWTDARALTDRMRWAAEPLF 253
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
10-170 |
1.17e-04 |
|
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: 42.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 10 AMVTPFDINGNIDfakttKLVNYLIDNGTTAIVVGGTTgesptltseekVALYRHVVSvvDKRVPVIAGTGSNNTHASID 89
Cdd:cd00945 4 TLLHPDATLEDIA-----KLCDEAIEYGFAAVCVNPGY-----------VRLAADALA--GSDVPVIVVVGFPTGLTTTE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HIJ_A 90 ----LTKKATEVGVDAVMLVAPYYNKPS--QEGMYQHFKAIAE--STPLPVMLYNVPGRsivQISVDTVVRLSEIeniva 161
Cdd:cd00945 66 vkvaEVEEAIDLGADEIDVVINIGSLKEgdWEEVLEEIAAVVEaaDGGLPLKVILETRG---LKTADEIAKAARI----- 137
|
....*....
3HIJ_A 162 I*DAGGDVL 170
Cdd:cd00945 138 AAEAGADFI 146
|
|
| |
