|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-286 |
1.61e-150 |
|
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: 422.67 E-value: 1.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 2 LRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSNN 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 82 TAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGLK 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 162 EATGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLHQ 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 757641650 242 TLFCEPSPIPVKWACARLGlMATATLRLPLTDLTPEGEAAMTRAL 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLG-LISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-291 |
2.57e-136 |
|
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: 386.82 E-value: 2.57e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 1 MLRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGL 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 161 KEATGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 757641650 241 QTLFCEPSPIPVKWACARLGLmATATLRLPLTDLTPEGEAAMTRALTTAEL 291
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGL-PSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-279 |
6.47e-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: 373.20 E-value: 6.47e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 4 GSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSNNTA 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 84 HAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGLKEA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 164 TGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLHQTL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 757641650 244 FCEPSPIPVKWACARLGLMATAtLRLPLTDLTPEGE 279
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGE-LRLPLTELSEEHR 275
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-289 |
4.64e-124 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 355.91 E-value: 4.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 1 MLRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGL 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 161 KEATGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 757641650 241 QTLFCEPSPIPVKWACARLGLMATATLRLPLTDLTPEGEAAMTRALTTA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
1-282 |
1.23e-86 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 260.34 E-value: 1.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 1 MLRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASglPQILYNVPGRTCCDLKPETVARLAKVPGIIGL 160
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 161 KEATGDlGRtplLRELCGPDFALYSGDDASGCDFMLQ-GGDGVISVTTNIAAPQMADMCRaalagdAGQAHDINNRLMPL 239
Cdd:PLN02417 159 KECTGN-DR---VKQYTEKGILLWSGNDDECHDARWDyGADGVISVTSNLVPGLMHKLMF------AGKNKELNDKLLPL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 757641650 240 HQTLFCEPSPIPVKWACARLGLMATAtLRLPLTDLTP----EGEAAM 282
Cdd:PLN02417 229 MDWLFCEPNPIGLNTALAQLGLIRPV-FRLPYVPLDLakraEFVALV 274
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-286 |
1.61e-150 |
|
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: 422.67 E-value: 1.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 2 LRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSNN 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 82 TAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGLK 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 162 EATGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLHQ 241
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 757641650 242 TLFCEPSPIPVKWACARLGlMATATLRLPLTDLTPEGEAAMTRAL 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLG-LISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-291 |
2.57e-136 |
|
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: 386.82 E-value: 2.57e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 1 MLRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGL 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 161 KEATGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLH 240
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 757641650 241 QTLFCEPSPIPVKWACARLGLmATATLRLPLTDLTPEGEAAMTRALTTAEL 291
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGL-PSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-279 |
6.47e-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: 373.20 E-value: 6.47e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 4 GSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSNNTA 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 84 HAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGLKEA 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 164 TGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLHQTL 243
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 757641650 244 FCEPSPIPVKWACARLGLMATAtLRLPLTDLTPEGE 279
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGE-LRLPLTELSEEHR 275
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-289 |
4.64e-124 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 355.91 E-value: 4.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 1 MLRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGL 160
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 161 KEATGDLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLH 240
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 757641650 241 QTLFCEPSPIPVKWACARLGLMATATLRLPLTDLTPEGEAAMTRALTTA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-286 |
2.11e-111 |
|
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: 323.35 E-value: 2.11e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 6 IVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSNNTAHA 85
Cdd:cd00408 2 IPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 86 IALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGLKEATG 165
Cdd:cd00408 82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 166 DLGRTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQAHDINNRLMPLHQTLFC 245
Cdd:cd00408 162 DLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 757641650 246 EPSPIPVKWACARLGLMAtATLRLPLTDLTPEGEAAMTRAL 286
Cdd:cd00408 242 EGNPAPVKAALALLGLDA-GPVRLPLVPLSEEERAKLEALL 281
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
1-282 |
1.23e-86 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 260.34 E-value: 1.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 1 MLRGSIVALVTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASglPQILYNVPGRTCCDLKPETVARLAKVPGIIGL 160
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 161 KEATGDlGRtplLRELCGPDFALYSGDDASGCDFMLQ-GGDGVISVTTNIAAPQMADMCRaalagdAGQAHDINNRLMPL 239
Cdd:PLN02417 159 KECTGN-DR---VKQYTEKGILLWSGNDDECHDARWDyGADGVISVTSNLVPGLMHKLMF------AGKNKELNDKLLPL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 757641650 240 HQTLFCEPSPIPVKWACARLGLMATAtLRLPLTDLTP----EGEAAM 282
Cdd:PLN02417 229 MDWLFCEPNPIGLNTALAQLGLIRPV-FRLPYVPLDLakraEFVALV 274
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
2-281 |
3.02e-41 |
|
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: 143.99 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 2 LRGSIVALVTPMLPSGDIDWVSLAALVEYHVD-AGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAI-AEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIG 159
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIiAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 160 LKEATGDLGRTPLLRELCGPDFALYsgddaSGCDFMLQGG-----DGVISVTTNIAAPQMADMCRAALAGDAGQAHDINN 234
Cdd:cd00954 161 VKFTATDLYDLERIRAASPEDKLVL-----NGFDEMLLSAlalgaDGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 757641650 235 RLMPLHQTLFcepspipvkwacaRLGLMATATL------------RLPLTDLTPEGEAA 281
Cdd:cd00954 236 VINDVITVLI-------------KNGLYPTLKAilrlmgldagpcRLPLRKVTEKALAK 281
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
10-288 |
3.82e-33 |
|
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: 122.82 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 10 VTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSnNTAHAIALS 89
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 90 RRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNvpgRTCCDLKPETVARLA-KVPGIIGLKEATGDLG 168
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAeRCPNLVGFKDGVGDIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 169 RTPLLRELCGPDFALYSGDDASGCDFMLQGGDGVISVTTNIA--APQMADMCRAAL-AGDAGQAH-----------DINN 234
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSAVFnfVPEIALAFYAAVrAGDHATVKrllrdfflpyvDIRN 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 757641650 235 RlmplhqtlfCEPSPIPVKWACARLGLMATATLRLPLTDLTPEGEAAMTRALTT 288
Cdd:cd00951 245 R---------RKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
10-186 |
8.68e-32 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 119.54 E-value: 8.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 10 VTPMLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSnNTAHAIALS 89
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 90 RRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNvpgRTCCDLKPETVARLA-KVPGIIGLKEATGDLG 168
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAeRCPNLVGFKDGVGDIE 171
|
170
....*....|....*...
gi 757641650 169 RTPLLRELCGPDFALYSG 186
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGG 189
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-234 |
5.35e-31 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 117.40 E-value: 5.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 2 LRGSIVALVTPMLPSGDIDWVSLAALVEYHVDA-GTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVIAGCGSN 80
Cdd:PRK04147 4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 81 NTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEASGLPQILYNVPGRTCCDLKPETVARLAKVPGIIGL 160
Cdd:PRK04147 84 NTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 161 KEATGDLGRTPLLRElCGPDFALYSGDD---ASGcdfMLQGGDGVISVTTNIAAPQMADMCRAALAGDAGQA----HDIN 233
Cdd:PRK04147 164 KQTAGDLYQLERIRK-AFPDKLIYNGFDemfASG---LLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAqelqHECN 239
|
.
gi 757641650 234 N 234
Cdd:PRK04147 240 D 240
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
2-161 |
2.43e-17 |
|
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: 80.57 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 2 LRGSIVALVTPMLPSGD-------IDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVEKTVEYAAGRIPVI 74
Cdd:cd00952 2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 75 AGCGSNNTAHAIALSRRFATMGVVAGLSVTPYYNKPTQEGLYRHYCAIAEAsgLPQ---ILYNVPGRTCCDLKPETVARL 151
Cdd:cd00952 82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEA--VPEmaiAIYANPEAFKFDFPRAAWAEL 159
|
170
....*....|
gi 757641650 152 AKVPGIIGLK 161
Cdd:cd00952 160 AQIPQVVAAK 169
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
5-208 |
1.96e-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: 71.64 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 5 SIVALVTPmLPSGDIDWVSLAALVEYHVDAGTSAIVAVGTTGESVTLSEQEHIAVVeKTVEYAAGRipVIAGCGSNNTAH 84
Cdd:cd00953 4 KITPVITP-FTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELL-KAYSDITDK--VIFQVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757641650 85 AIALSRRFATMGVVAGLSVTPYY-NKPTQEGLYRHYCAIAEAsgLPQILYNVPGRTCCDLKPETVARLAKVPG-IIGLKE 162
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIKKAGGdIIGVKD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 757641650 163 ATGDLGRTPLLRELcGPDFALYSGDDASGCDFMLQGGDGVISVTTN 208
Cdd:cd00953 158 TNEDISHMLEYKRL-VPDFKVYSGPDSLIFSALRSGLDGSVAAASN 202
|
|
| |
