|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-293 |
0e+00 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 511.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 2 NKDLKGLYAALLVPFDENGQVNEQGLKQIAQNAIETEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQV 81
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 82 GSLDLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKI 161
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 162 VGVKYTAPNFFLLERIRKAFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSND 241
Cdd:PRK04147 161 IGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECND 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 579537811 242 IIETVLSMGIYPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAKYDL 293
Cdd:PRK04147 241 VIDLLIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYLPALKALAAKYLK 292
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-290 |
4.15e-157 |
|
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: 439.44 E-value: 4.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 5 LKGLYAALLVPFDENGQVNEQGLKQIAQNAIETEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSL 84
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 85 DLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEAT-QNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRKAFP-DKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDI 242
Cdd:cd00954 161 VKFTATDLYDLERIRAASPeDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 579537811 243 IETVLSMGIYPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAK 290
Cdd:cd00954 241 ITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAKELAAK 288
|
|
| nanA |
TIGR00683 |
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid ... |
5-290 |
1.35e-113 |
|
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid aldolase, sialic acid aldolase, or sialate lyase. It is an intracellular enzyme. The structure of this homotetrameric enzyme related to dihydrodipicolinate synthase is known. In Clostridium tertium, the enzyme appears to be in an operon with a secreted sialidase that releases sialic acid from host sialoglycoconjugates. In several E. coli strains, however, this enzyme is responsible for N-acetyl-D-neuraminic acid synthesis for capsule production by condensing N-acetyl-D-mannosamine and pyruvate. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273217 Cd Length: 293 Bit Score: 329.60 E-value: 1.35e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 5 LKGLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSL 84
Cdd:TIGR00683 1 LRGVMAALLTPFDQQQALDKASLRRLVQFNIQ-QGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 85 DLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDII-EATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:TIGR00683 80 NTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIdSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRKAFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDII 243
Cdd:TIGR00683 160 LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 579537811 244 ETVLSMGIYPTLKEILRHRD-IDAGLPKRPFKPFNEahrQTLDQLIAK 290
Cdd:TIGR00683 240 DLLIKTGVFRGLKTVLHYMDvVSVPLCRKPFGPVDE---KYLPELKAL 284
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
4-288 |
1.19e-95 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 283.49 E-value: 1.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 4 DLKGLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGS 83
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLIN-KGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 84 LDLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:pfam00701 80 NSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRK-AFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDI 242
Cdd:pfam00701 160 IKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 579537811 243 IETVLSMGIYPTLKEILRHRDIDAG-LPKRPFKPFNEAHRQTLDQLI 288
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGpTCRLPLTPLSEEERPELEAIL 286
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
4-293 |
4.73e-90 |
|
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: 269.33 E-value: 4.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 4 DLKGLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGS 83
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLID-AGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 84 LDLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:COG0329 80 NSTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRKAFPDKL-ILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDI 242
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFaVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 579537811 243 IETVLSMGIYPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAKYDL 293
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-293 |
0e+00 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 511.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 2 NKDLKGLYAALLVPFDENGQVNEQGLKQIAQNAIETEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQV 81
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 82 GSLDLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKI 161
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 162 VGVKYTAPNFFLLERIRKAFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSND 241
Cdd:PRK04147 161 IGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECND 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 579537811 242 IIETVLSMGIYPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAKYDL 293
Cdd:PRK04147 241 VIDLLIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYLPALKALAAKYLK 292
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-290 |
4.15e-157 |
|
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: 439.44 E-value: 4.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 5 LKGLYAALLVPFDENGQVNEQGLKQIAQNAIETEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSL 84
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 85 DLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEAT-QNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRKAFP-DKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDI 242
Cdd:cd00954 161 VKFTATDLYDLERIRAASPeDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 579537811 243 IETVLSMGIYPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAK 290
Cdd:cd00954 241 ITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAKELAAK 288
|
|
| nanA |
TIGR00683 |
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid ... |
5-290 |
1.35e-113 |
|
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid aldolase, sialic acid aldolase, or sialate lyase. It is an intracellular enzyme. The structure of this homotetrameric enzyme related to dihydrodipicolinate synthase is known. In Clostridium tertium, the enzyme appears to be in an operon with a secreted sialidase that releases sialic acid from host sialoglycoconjugates. In several E. coli strains, however, this enzyme is responsible for N-acetyl-D-neuraminic acid synthesis for capsule production by condensing N-acetyl-D-mannosamine and pyruvate. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273217 Cd Length: 293 Bit Score: 329.60 E-value: 1.35e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 5 LKGLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSL 84
Cdd:TIGR00683 1 LRGVMAALLTPFDQQQALDKASLRRLVQFNIQ-QGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 85 DLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDII-EATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:TIGR00683 80 NTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIdSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRKAFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDII 243
Cdd:TIGR00683 160 LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 579537811 244 ETVLSMGIYPTLKEILRHRD-IDAGLPKRPFKPFNEahrQTLDQLIAK 290
Cdd:TIGR00683 240 DLLIKTGVFRGLKTVLHYMDvVSVPLCRKPFGPVDE---KYLPELKAL 284
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
4-288 |
1.19e-95 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 283.49 E-value: 1.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 4 DLKGLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGS 83
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLIN-KGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 84 LDLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:pfam00701 80 NSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRK-AFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDI 242
Cdd:pfam00701 160 IKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 579537811 243 IETVLSMGIYPTLKEILRHRDIDAG-LPKRPFKPFNEAHRQTLDQLI 288
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGpTCRLPLTPLSEEERPELEAIL 286
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
4-293 |
4.73e-90 |
|
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: 269.33 E-value: 4.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 4 DLKGLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGS 83
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLID-AGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 84 LDLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVG 163
Cdd:COG0329 80 NSTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 164 VKYTAPNFFLLERIRKAFPDKL-ILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDI 242
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFaVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 579537811 243 IETVLSMGIYPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAKYDL 293
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-288 |
5.49e-90 |
|
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: 269.03 E-value: 5.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 8 LYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSLDLN 87
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIE-AGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 88 EAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVGVKYT 167
Cdd:cd00408 80 EAIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 168 APNFFLLERIRKAFPDKL-ILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDIIETV 246
Cdd:cd00408 160 SGDLDRLTRLIALLGPDFaVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 579537811 247 LSMGIYPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLI 288
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
5-288 |
1.38e-50 |
|
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: 168.06 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 5 LKGLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSL 84
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIE-NGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 85 DLNEAIELGKYATELGYDALSAVTPfYY--PfTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIV 162
Cdd:cd00950 80 NTAEAIELTKRAEKAGADAALVVTP-YYnkP-SQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 163 GVKYTAPNFFLLERIRKAFPDKL-ILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSND 241
Cdd:cd00950 158 GIKEATGDLDRVSELIALCPDDFaVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLP 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 579537811 242 IIEtVLSMGIYPT-LKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLI 288
Cdd:cd00950 238 LIK-ALFAEPNPIpVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-291 |
3.61e-37 |
|
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: 133.22 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 7 GLYAALLVPFDENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSLDL 86
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIE-NGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 87 NEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVGVKY 166
Cdd:TIGR00674 80 EEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 167 TAPNFFLLERIRKAFPDKL-ILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQH-------- 237
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFvVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQklmplhka 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 579537811 238 ---DSNDIietvlsmgiypTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAKY 291
Cdd:TIGR00674 240 lfiETNPI-----------PVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
12-290 |
5.67e-27 |
|
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: 106.31 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 12 LLVPFdENGQVNEQGLKQIAQNAIEtEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEaVGDKVklIAQVGSLDLNEAIE 91
Cdd:cd00953 8 VITPF-TGNKIDKEKFKKHCENLIS-KGIDYVFVAGTTGLGPSLSFQEKLELLKAYSD-ITDKV--IFQVGSLNLEESIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 92 LGKYATELGYDALSAVTPFYYPFTFEE-IRDYYFDIIEATQnnMIIYAIPDLTGVNISIEQFSEL-FNHEKIVGVKYTAP 169
Cdd:cd00953 83 LARAAKSFGIYAIASLPPYYFPGIPEEwLIKYFTDISSPYP--TFIYNYPKATGYDINARMAKEIkKAGGDIIGVKDTNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 170 NFFLLERIRKAFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLArqgQIQEAYQLQHDSNDIIETVLSM 249
Cdd:cd00953 161 DISHMLEYKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV---AIEDAFKLQFLINEVLDASRKY 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 579537811 250 GIYPT---LKEILrhRDIDAGLPKRPFKPFNEAHRQTLDQLIAK 290
Cdd:cd00953 238 GSWSAnysLVKIF--QGYDAGEPRPPFYPLDEEEEEKLRKEVNE 279
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
7-212 |
3.73e-21 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 90.47 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 7 GLYAALLVPFDENGQVNEQGLKQIAQNAIETEeLDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSLDL 86
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENG-AEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 87 NEAIELGKYATELGYDALSAVTPfYYPFTFEEIRDYYFDIIeATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVGVKY 166
Cdd:PLN02417 83 REAIHATEQGFAVGMHAALHINP-YYGKTSQEGLIKHFETV-LDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 579537811 167 TAPNffllERIRKAFPDKLIL-SGFDEMLVQATIS-GVDGAIGSTYNV 212
Cdd:PLN02417 161 CTGN----DRVKQYTEKGILLwSGNDDECHDARWDyGADGVISVTSNL 204
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
4-285 |
5.49e-12 |
|
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: 65.16 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 4 DLKGLYAALLVP-FDENGQVNeqglkqiAQNAIETEEL------------DGLYVNGSSGENFLLNTEQKKQVFKVAKEA 70
Cdd:cd00952 1 DIKGVWAIVPTPsKPDASDWR-------ATDTVDLDETarlverliaagvDGILTMGTFGECATLTWEEKQAFVATVVET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 71 VGDKVKLIAQVGSLDLNEAIELGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQN-NMIIYAIPDLTGVNISI 149
Cdd:cd00952 74 VAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVPEmAIAIYANPEAFKFDFPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 150 EQFSELFNHEKIVGVKYTAPNFFLLERIRKAFPDKLILSGFDEMLVQATI--SGVDGAIGSTYNVNGRRARKIFDLARQG 227
Cdd:cd00952 154 AAWAELAQIPQVVAAKYLGDIGALLSDLAAVKGRMRLLPLEDDYYAAARLfpEEVTAFWSSGAACGPAPVTALRDAVATG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537811 228 QIQEAYQLQHDSNDIIETVLSMGIYPTLK----EILRHRDIDAGL----PKRPfkPFNEAHRQTLD 285
Cdd:cd00952 234 DWTDARALTDRMRWAAEPLFPRGDFSEFSkyniALEKARFDAAGYmragPARP--PYNTAPEAYLE 297
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
13-290 |
1.77e-08 |
|
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: 54.25 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 13 LVPFDENGQVNEQGLKQ-IAQNAieTEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSlDLNEAIE 91
Cdd:cd00951 9 VTHFDADGSFDEDAYRAhVEWLL--SYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTATAIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 92 LGKYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIY------AIPDltgvniSIEQFSELFnhEKIVGVK 165
Cdd:cd00951 86 YAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYnranavLTAD------SLARLAERC--PNLVGFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 166 YTAPNFFLLERIRKAFPDKLILSG-------FDEMLVQATISGVDGAIgstYNVNGRRARKIFDLARQGQIQEAYQLQHD 238
Cdd:cd00951 158 DGVGDIELMRRIVAKLGDRLLYLGglptaevFALAYLAMGVPTYSSAV---FNFVPEIALAFYAAVRAGDHATVKRLLRD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537811 239 ----SNDIIETVLSMGIyPTLKEILRHRDIDAGLPKRPFKPFNEAHRQTLDQLIAK 290
Cdd:cd00951 235 fflpYVDIRNRRKGYAV-SIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
15-185 |
1.56e-06 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 48.66 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 15 PFDENGQVNEQGLKQ-IAQNAieTEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSlDLNEAIELG 93
Cdd:PRK03620 18 PFDADGSFDEAAYREhLEWLA--PYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537811 94 KYATELGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIY----AIPDLTgvniSIEQFSElfNHEKIVGVKYTAP 169
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYnrdnAVLTAD----TLARLAE--RCPNLVGFKDGVG 168
|
170
....*....|....*.
gi 579537811 170 NFFLLERIRKAFPDKL 185
Cdd:PRK03620 169 DIELMQRIVRALGDRL 184
|
|
| |
