|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-296 |
4.10e-145 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 409.45 E-value: 4.10e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 3 KFSGIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSP 82
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 83 STDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLALqNENIVG 162
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 163 IKDTidsVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKL 242
Cdd:pfam00701 160 IKEA---SGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 90111725 243 LQLPAIYALEtPFVSLIKYSMQCVGLPVETYCLPPILEASEEAKDKVHVLLTAQ 296
Cdd:pfam00701 237 LPLIKILFAE-PNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-299 |
2.28e-107 |
|
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: 313.63 E-value: 2.28e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 3 KFSGIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSP 82
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 83 STDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVG 162
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 163 IKDTIDSVGHLRTMINTvksVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKL 242
Cdd:COG0329 160 IKEASGDLDRIAELIRA---TGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111725 243 LQLPAIYALEtPFVSLIKYSMQCVGLPVEtYCLPPILEASEEAKDKVHVLLTAQGIL 299
Cdd:COG0329 237 LPLIRALFAE-GNPAPVKAALALLGLPSG-PVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
7-293 |
5.02e-99 |
|
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: 292.14 E-value: 5.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 7 IIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPSTDE 86
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 87 AVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVGIKDT 166
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLA-EHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 167 IDSVGHLRTMINTvksVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKLLQLP 246
Cdd:cd00408 160 SGDLDRLTRLIAL---LGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 90111725 247 AIYALEtPFVSLIKYSMQCVGLPVeTYCLPPILEASEEAKDKVHVLL 293
Cdd:cd00408 237 EALFKE-GNPAPVKAALALLGLDA-GPVRLPLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
6-289 |
4.03e-60 |
|
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: 192.93 E-value: 4.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 6 GIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPSTD 85
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 86 EAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVGIKd 165
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLA-EEPNIVAIK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 166 tiDSVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKLLQL 245
Cdd:TIGR00674 159 --EATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 90111725 246 PAIYALET---PfvslIKYSMQCVGLPVETYCLpPILEASEEAKDKV 289
Cdd:TIGR00674 237 HKALFIETnpiP----VKTALALLGLIEGELRL-PLTELSEEHRNKL 278
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-235 |
5.59e-48 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 162.09 E-value: 5.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 1 MKKFSGIIPPVSSTFHRDGTLDKKAMREVADFLINK-GVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGV 79
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 80 GSPSTDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLaLQNEN 159
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNEL-FTLPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111725 160 IVGIKDTidsVGHLRTMiNTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATA 235
Cdd:PRK04147 160 VIGVKQT---AGDLYQL-ERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEA 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-296 |
4.10e-145 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 409.45 E-value: 4.10e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 3 KFSGIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSP 82
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 83 STDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLALqNENIVG 162
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 163 IKDTidsVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKL 242
Cdd:pfam00701 160 IKEA---SGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 90111725 243 LQLPAIYALEtPFVSLIKYSMQCVGLPVETYCLPPILEASEEAKDKVHVLLTAQ 296
Cdd:pfam00701 237 LPLIKILFAE-PNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-299 |
2.28e-107 |
|
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: 313.63 E-value: 2.28e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 3 KFSGIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSP 82
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 83 STDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVG 162
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 163 IKDTIDSVGHLRTMINTvksVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKL 242
Cdd:COG0329 160 IKEASGDLDRIAELIRA---TGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111725 243 LQLPAIYALEtPFVSLIKYSMQCVGLPVEtYCLPPILEASEEAKDKVHVLLTAQGIL 299
Cdd:COG0329 237 LPLIRALFAE-GNPAPVKAALALLGLPSG-PVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
7-293 |
5.02e-99 |
|
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: 292.14 E-value: 5.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 7 IIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPSTDE 86
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 87 AVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVGIKDT 166
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLA-EHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 167 IDSVGHLRTMINTvksVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKLLQLP 246
Cdd:cd00408 160 SGDLDRLTRLIAL---LGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 90111725 247 AIYALEtPFVSLIKYSMQCVGLPVeTYCLPPILEASEEAKDKVHVLL 293
Cdd:cd00408 237 EALFKE-GNPAPVKAALALLGLDA-GPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
4-289 |
5.91e-78 |
|
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: 238.55 E-value: 5.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 4 FSGIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPS 83
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 84 TDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVGI 163
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLA-EHPNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 164 KdtiDSVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKLl 243
Cdd:cd00950 160 K---EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKL- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 90111725 244 qLPAIYAL-ETPFVSLIKYSMQCVGLPVETYCLpPILEASEEAKDKV 289
Cdd:cd00950 236 -LPLIKALfAEPNPIPVKAALALLGLISGELRL-PLVPLSEELRAKL 280
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
6-289 |
4.03e-60 |
|
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: 192.93 E-value: 4.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 6 GIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPSTD 85
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 86 EAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVGIKd 165
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLA-EEPNIVAIK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 166 tiDSVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKLLQL 245
Cdd:TIGR00674 159 --EATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 90111725 246 PAIYALET---PfvslIKYSMQCVGLPVETYCLpPILEASEEAKDKV 289
Cdd:TIGR00674 237 HKALFIETnpiP----VKTALALLGLIEGELRL-PLTELSEEHRNKL 278
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-285 |
1.09e-54 |
|
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: 179.04 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 5 SGIIPPVSSTFHRDGTLDKKAMREVADFLINK-GVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPS 83
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 84 TDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVT-LPVILYNFPDLTGQDLTPETVTRLaLQNENIVG 162
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAAsLPMIIYHIPALTGVNLTLEQFLEL-FEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 163 IKDTidsVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKL 242
Cdd:cd00954 161 VKFT---ATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 90111725 243 LQLpaIYAL-ETPFVSLIKYSMQCVGLPVeTYCLPPILEASEEA 285
Cdd:cd00954 238 NDV--ITVLiKNGLYPTLKAILRLMGLDA-GPCRLPLRKVTEKA 278
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-235 |
5.59e-48 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 162.09 E-value: 5.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 1 MKKFSGIIPPVSSTFHRDGTLDKKAMREVADFLINK-GVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGV 79
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 80 GSPSTDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLaLQNEN 159
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNEL-FTLPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111725 160 IVGIKDTidsVGHLRTMiNTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATA 235
Cdd:PRK04147 160 VIGVKQT---AGDLYQL-ERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEA 231
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
7-223 |
1.32e-39 |
|
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: 139.82 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 7 IIPPVSSTFhRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDgrvPVLIGVGSPSTDE 86
Cdd:cd00953 4 KITPVITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 87 AVKLAQHAQAYGADGIVAINPYYWKVAPRN-LDDYYQQIARSVtlPVILYNFPDLTGQDLTPETVTRLALQNENIVGIKD 165
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYFPGIPEEwLIKYFTDISSPY--PTFIYNYPKATGYDINARMAKEIKKAGGDIIGVKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111725 166 TIDSVGHlrtMINTvKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGI 223
Cdd:cd00953 158 TNEDISH---MLEY-KRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKI 211
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
18-245 |
4.86e-36 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 130.53 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 18 DGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPSTDEAVKLAQHAQAY 97
Cdd:PLN02417 16 DGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTREAIHATEQGFAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 98 GADGIVAINPYYWKVAPRNLDDYYQQIARsvTLPVILYNFPDLTGQDLTPETVTRLAlQNENIVGIKdtiDSVGHLRtmi 177
Cdd:PLN02417 96 GMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIA-QHPNFAGVK---ECTGNDR--- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111725 178 ntVKS-VRPSFSVFCGYDDHLLNTML-LGGDGAITASANFAPELSvgiyrawreGDLATAA---TLNKKLLQL 245
Cdd:PLN02417 167 --VKQyTEKGILLWSGNDDECHDARWdYGADGVISVTSNLVPGLM---------HKLMFAGknkELNDKLLPL 228
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
4-284 |
5.44e-36 |
|
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: 130.52 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 4 FSGIIP-PVSStFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSP 82
Cdd:cd00951 1 GSGLLSfPVTH-FDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 83 sTDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDltgQDLTPETVTRLALQNENIVG 162
Cdd:cd00951 80 -TATAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRAN---AVLTADSLARLAERCPNLVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 163 IKdtiDSVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASA---NFAPELSVGIYRAWREGDLATAatln 239
Cdd:cd00951 156 FK---DGVGDIELMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSavfNFVPEIALAFYAAVRAGDHATV---- 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111725 240 KKLLQ---LPAI--------YAletpfVSLIKYSMQCVGLPVETyCLPPILEASEE 284
Cdd:cd00951 229 KRLLRdffLPYVdirnrrkgYA-----VSIVKAGARLVGRDAGP-VRPPLTDLTEE 278
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
10-299 |
1.35e-35 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 129.94 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 10 PVSStFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPsTDEAVK 89
Cdd:PRK03620 15 PVTP-FDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG-TAQAIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 90 LAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNfpdltgQD---LTPETVTRLALQNENIVGIKdt 166
Cdd:PRK03620 93 YAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN------RDnavLTADTLARLAERCPNLVGFK-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 167 iDSVGHLRTMINTVKSVRPSFSVFCGYDDHLLnTML----LGGDGAITASANFAPELSVGIYRAWREGDLATAatlnKKL 242
Cdd:PRK03620 165 -DGVGDIELMQRIVRALGDRLLYLGGLPTAEV-FAAaylaLGVPTYSSAVFNFVPEIALAFYRALRAGDHATV----DRL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111725 243 LQ---LPAI--------YAletpfVSLIKYSMQCVGLPVETyCLPPILEASEEAKDKVHVLLTAQGIL 299
Cdd:PRK03620 239 LDdffLPYValrnrkkgYA-----VSIVKAGARLVGLDAGP-VRAPLTDLTPEELAELAALIAKGGAQ 300
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
6-284 |
4.82e-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: 74.02 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 6 GIIP----PVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGS 81
Cdd:cd00952 7 AIVPtpskPDASDWRATDTVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 82 PSTDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSV-TLPVILYNFPDLTGQDLTPETVTRLAlQNENI 160
Cdd:cd00952 87 LNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELA-QIPQV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111725 161 VGIKdTIDSVGHLrtmINTVKSVRPSFSVFCGYDDHLLNTMLLGG--DGAITASANFAPELSVGIYRAWREGDLATAATL 238
Cdd:cd00952 166 VAAK-YLGDIGAL---LSDLAAVKGRMRLLPLEDDYYAAARLFPEevTAFWSSGAACGPAPVTALRDAVATGDWTDARAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 90111725 239 NKKLLQLPAIYALETPFVSLIKYS-------MQCVGLPVETYCLPPILEASEE 284
Cdd:cd00952 242 TDRMRWAAEPLFPRGDFSEFSKYNialekarFDAAGYMRAGPARPPYNTAPEA 294
|
|
| |
