|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
1-300 |
1.20e-148 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 418.84 E-value: 1.20e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 1 MLDGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGGA 80
Cdd:PRK03620 7 LGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 81 LPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYHRANGQFTEQSALAVA-RLPKVVGFKDG 159
Cdd:PRK03620 87 TAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNRDNAVLTADTLARLAeRCPNLVGFKDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 160 VGDLDLTSRIVRTLRDslgdkEFQFFNGLPTAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNRE 239
Cdd:PRK03620 167 VGDIELMQRIVRALGD-----RLLYLGGLPTAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLDD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 669178896 240 FFHPLVRLRDTTPGYAVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVAAGRKVLA 300
Cdd:PRK03620 242 FFLPYVALRNRKKGYAVSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGGAQLP 302
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
3-294 |
1.30e-117 |
|
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: 339.68 E-value: 1.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 3 DGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGGALP 82
Cdd:cd00951 2 SGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 83 VAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYHRANGQFTEQSALAVA-RLPKVVGFKDGVG 161
Cdd:cd00951 82 TAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRANAVLTADSLARLAeRCPNLVGFKDGVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 162 DLDLTSRIVRTLRDSLGdkefqFFNGLPTAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNREFF 241
Cdd:cd00951 162 DIELMRRIVAKLGDRLL-----YLGGLPTAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 669178896 242 HPLVRLRDTTPGYAVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVAA 294
Cdd:cd00951 237 LPYVDIRNRRKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| KdgD |
TIGR03249 |
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only ... |
4-292 |
8.14e-99 |
|
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only catalyzes the dehydration of the substrate (diol to ketone + water), but causes the decarboxylation of the intermediate product to yield 2-oxoglutarate semialdehyde (2,5-dioxopentanoate). The gene for the enzyme is usually observed in the vicinity of transporters and dehydratases handling D-galactarate and D-gluconate as well as aldehyde dehydrogenases which convert the product to alpha-ketoglutarate.
Pssm-ID: 132293 Cd Length: 296 Bit Score: 292.38 E-value: 8.14e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 4 GVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGGALPV 83
Cdd:TIGR03249 8 GLLSFPVTPFDADGSFDEAAYRENIEWLLGYGLEALFAAGGTGEFFSLTPAEYEQVVEIAVSTAKGKVPVYTGVGGNTSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 84 AKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYHRANGQFT-EQSALAVARLPKVVGFKDGVGD 162
Cdd:TIGR03249 88 AIEIARLAEKAGADGYLLLPPYLINGEQEGLYAHVEAVCESTDLGVIVYQRDNAVLNaDTLERLADRCPNLVGFKDGIGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 163 LDLTSRIVRTLRDSLGdkefqFFNGLPTAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNREFFH 242
Cdd:TIGR03249 168 MEQMIEITQRLGDRLG-----YLGGMPTAEVTAPAYLPLGVTSYSSAIFNFIPHIARAFYEALRRGDHATVGEIYKEFIL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 669178896 243 PLVRLRDTTPGYAVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIV 292
Cdd:TIGR03249 243 PINEIRNRKKGYAVSIIKAGMEIVGLPAGPVRPPLTDLTKEEYAQLEVIL 292
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-294 |
5.35e-56 |
|
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: 182.66 E-value: 5.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 1 MLDGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG- 79
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 80 ALPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYH---RANGQFTEQSALAVARLPKVVGF 156
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNipgRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 157 KDGVGDLDLTSRIVRTLRDslgdkEFQFFNG-----LPTaevsqqayRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTE 231
Cdd:COG0329 161 KEASGDLDRIAELIRATGD-----DFAVLSGddalaLPA--------LALGADGVISVTANVAPELMVALYEAALAGDLA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669178896 232 LVASLNREFFhPLVRLRDTTPGYAValVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVAA 294
Cdd:COG0329 228 EARALQDRLL-PLIRALFAEGNPAP--VKAALALLGLPSGPVRLPLLPLSEEERAELRAALKE 287
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-294 |
3.27e-53 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 175.63 E-value: 3.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 1 MLDGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG- 79
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 80 ALPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYH---RANGQFTEQSALAVARLPKVVGF 156
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNvpsRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 157 KDGVGDLDLTSRIVRTLRDSLGdkefqFFNGlptAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASL 236
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFV-----ILSG---DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 669178896 237 NREFFhPLVRLRDTTPgyAVALVKAGVTFTGLDAGS-VRAPLVDASAQHRYELEQIVAA 294
Cdd:pfam00701 233 NHKLL-PLIKILFAEP--NPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKA 288
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
1-300 |
1.20e-148 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 418.84 E-value: 1.20e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 1 MLDGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGGA 80
Cdd:PRK03620 7 LGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 81 LPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYHRANGQFTEQSALAVA-RLPKVVGFKDG 159
Cdd:PRK03620 87 TAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNRDNAVLTADTLARLAeRCPNLVGFKDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 160 VGDLDLTSRIVRTLRDslgdkEFQFFNGLPTAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNRE 239
Cdd:PRK03620 167 VGDIELMQRIVRALGD-----RLLYLGGLPTAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLDD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 669178896 240 FFHPLVRLRDTTPGYAVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVAAGRKVLA 300
Cdd:PRK03620 242 FFLPYVALRNRKKGYAVSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGGAQLP 302
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
3-294 |
1.30e-117 |
|
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: 339.68 E-value: 1.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 3 DGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGGALP 82
Cdd:cd00951 2 SGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 83 VAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYHRANGQFTEQSALAVA-RLPKVVGFKDGVG 161
Cdd:cd00951 82 TAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRANAVLTADSLARLAeRCPNLVGFKDGVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 162 DLDLTSRIVRTLRDSLGdkefqFFNGLPTAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNREFF 241
Cdd:cd00951 162 DIELMRRIVAKLGDRLL-----YLGGLPTAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 669178896 242 HPLVRLRDTTPGYAVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVAA 294
Cdd:cd00951 237 LPYVDIRNRRKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| KdgD |
TIGR03249 |
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only ... |
4-292 |
8.14e-99 |
|
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only catalyzes the dehydration of the substrate (diol to ketone + water), but causes the decarboxylation of the intermediate product to yield 2-oxoglutarate semialdehyde (2,5-dioxopentanoate). The gene for the enzyme is usually observed in the vicinity of transporters and dehydratases handling D-galactarate and D-gluconate as well as aldehyde dehydrogenases which convert the product to alpha-ketoglutarate.
Pssm-ID: 132293 Cd Length: 296 Bit Score: 292.38 E-value: 8.14e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 4 GVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGGALPV 83
Cdd:TIGR03249 8 GLLSFPVTPFDADGSFDEAAYRENIEWLLGYGLEALFAAGGTGEFFSLTPAEYEQVVEIAVSTAKGKVPVYTGVGGNTSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 84 AKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYHRANGQFT-EQSALAVARLPKVVGFKDGVGD 162
Cdd:TIGR03249 88 AIEIARLAEKAGADGYLLLPPYLINGEQEGLYAHVEAVCESTDLGVIVYQRDNAVLNaDTLERLADRCPNLVGFKDGIGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 163 LDLTSRIVRTLRDSLGdkefqFFNGLPTAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNREFFH 242
Cdd:TIGR03249 168 MEQMIEITQRLGDRLG-----YLGGMPTAEVTAPAYLPLGVTSYSSAIFNFIPHIARAFYEALRRGDHATVGEIYKEFIL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 669178896 243 PLVRLRDTTPGYAVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIV 292
Cdd:TIGR03249 243 PINEIRNRKKGYAVSIIKAGMEIVGLPAGPVRPPLTDLTKEEYAQLEVIL 292
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
5-292 |
6.40e-60 |
|
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: 192.38 E-value: 6.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 5 VLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG-ALPV 83
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGAnSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 84 AKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYH---RANGQFTEQSALAVARLPKVVGFKDGV 160
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNipgRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 161 GDLDLTSRIVRTLRDslgdkEFQFFNGLptaevSQQA--YRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNR 238
Cdd:cd00408 161 GDLDRLTRLIALLGP-----DFAVLSGD-----DDLLlpALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQD 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 669178896 239 EFFhPLVRLRDTTPGyaVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIV 292
Cdd:cd00408 231 RLL-PLIEALFKEGN--PAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-294 |
5.35e-56 |
|
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: 182.66 E-value: 5.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 1 MLDGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG- 79
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 80 ALPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYH---RANGQFTEQSALAVARLPKVVGF 156
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNipgRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 157 KDGVGDLDLTSRIVRTLRDslgdkEFQFFNG-----LPTaevsqqayRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTE 231
Cdd:COG0329 161 KEASGDLDRIAELIRATGD-----DFAVLSGddalaLPA--------LALGADGVISVTANVAPELMVALYEAALAGDLA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669178896 232 LVASLNREFFhPLVRLRDTTPGYAValVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVAA 294
Cdd:COG0329 228 EARALQDRLL-PLIRALFAEGNPAP--VKAALALLGLPSGPVRLPLLPLSEEERAELRAALKE 287
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-294 |
3.27e-53 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 175.63 E-value: 3.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 1 MLDGVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG- 79
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 80 ALPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYH---RANGQFTEQSALAVARLPKVVGF 156
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNvpsRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 157 KDGVGDLDLTSRIVRTLRDSLGdkefqFFNGlptAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASL 236
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFV-----ILSG---DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 669178896 237 NREFFhPLVRLRDTTPgyAVALVKAGVTFTGLDAGS-VRAPLVDASAQHRYELEQIVAA 294
Cdd:pfam00701 233 NHKLL-PLIKILFAEP--NPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKA 288
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
10-292 |
5.11e-43 |
|
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: 148.80 E-value: 5.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 10 VTPFDSNGDVDLPALAQ----HIESGVAAgpggvFAACG-TGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG-ALPV 83
Cdd:cd00950 9 VTPFKDDGSVDFDALERliefQIENGTDG-----LVVCGtTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSnNTAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 84 AKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVY---HRANGQFTEQSALAVARLPKVVGFKDGV 160
Cdd:cd00950 84 AIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYnvpGRTGVNIEPETVLRLAEHPNIVGIKEAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 161 GDLDLTSRIVRTLRDslgdkEFQFFNG-----LPTAevsqqayrSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVAS 235
Cdd:cd00950 164 GDLDRVSELIALCPD-----DFAVLSGddaltLPFL--------ALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 669178896 236 LNREFFhPLVRLRDTTPGyaVALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIV 292
Cdd:cd00950 231 LHRKLL-PLIKALFAEPN--PIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
4-293 |
4.14e-34 |
|
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: 125.52 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 4 GVLFFPVTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG-ALP 82
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSnATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 83 VAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYH---RANGQFTEQSALAVARLPKVVGFKDG 159
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNvpsRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 160 VGDLDLTSRIVRTLRDSlgdkeFQFFNGlptAEVSQQAYRSIGVTLYSSATFAFAPDVSLAYYRALEEDDTELVASLNRE 239
Cdd:TIGR00674 161 TGNLERISEIKAIAPDD-----FVVLSG---DDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 669178896 240 FFhPLVR--LRDTTPgyavALVKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVA 293
Cdd:TIGR00674 233 LM-PLHKalFIETNP----IPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLK 283
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
2-294 |
1.09e-20 |
|
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: 89.68 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 2 LDGVLFFPVTPFDSNGDVDLPALAQHIESGV-AAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG- 79
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIeKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 80 ALPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSE-ASDLPVIVYH---RANGQFTEQSALAVARLPKVVG 155
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAaAASLPMIIYHipaLTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 156 FKDGVGDLDLTSRIVRtlrdsLGDKEFQFFNGLPTAEVSQQAYRSIGVTlysSATFAFAPDVSLAYYRALEEDDTELVAS 235
Cdd:cd00954 161 VKFTATDLYDLERIRA-----ASPEDKLVLNGFDEMLLSALALGADGAI---GSTYNVNGKRYRKIFEAFNAGDIDTARE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 669178896 236 LNREfFHPLVRLRDTTPGYAVAlvKAGVTFTGLDAGSVRAPLVDASAQHRYELEQIVAA 294
Cdd:cd00954 233 LQHV-INDVITVLIKNGLYPTL--KAILRLMGLDAGPCRLPLRKVTEKALAKAKELAAK 288
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
10-162 |
2.97e-13 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 68.52 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 10 VTPFDSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGGALPvaKEFVA 89
Cdd:PLN02417 10 KTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNST--REAIH 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669178896 90 IAEEA---GADGILLLPPYLVGAPAQGLVEYVKQVSEASdlPVIVYH---RANGQFTEQSALAVARLPKVVGFKDGVGD 162
Cdd:PLN02417 88 ATEQGfavGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNvpgRTGQDIPPEVIFKIAQHPNFAGVKECTGN 164
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-293 |
1.21e-09 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 58.08 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 2 LDGVLFFPVTPFDSNGDVDLPALAQHIESGVAA-GPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAGG- 79
Cdd:PRK04147 4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 80 ALPVAKEFVAIAEEAGADGILLLPPYLVGAPAQGLVEYVKQVSEASDLPVIVYH---RANGQFT-EQSALAVArLPKVVG 155
Cdd:PRK04147 84 NTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNipaLTGVNLSlDQFNELFT-LPKVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 156 FKDGVGDLDLTSRIVRTLRDSLgdkefqFFNGLPTAEVSQQAYrsiGVTLYSSATFAFAPDVSLAYYRALEEDDTELVas 235
Cdd:PRK04147 163 VKQTAGDLYQLERIRKAFPDKL------IYNGFDEMFASGLLA---GADGAIGSTYNVNGWRARQIFEAAKAGDIQEA-- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669178896 236 lnreffhplVRLRDTTPGYAVALVKAGVTFT--------GLDAGSVRAPLVDASAQHRYELEQIVA 293
Cdd:PRK04147 232 ---------QELQHECNDVIDLLIKNGVYPGlkeilhymGVDAGLCRKPFKPVDEKYLPALKALAA 288
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
19-282 |
1.33e-09 |
|
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: 58.23 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 19 VDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEFRTVVDTVVTATKGRVPVFAGAgGALPvAKEFVA---IAEEAG 95
Cdd:cd00952 26 VDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGA-TTLN-TRDTIArtrALLDLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 96 ADGILLLPPYLVGAPAQGLVEYVKQVSEA-SDLPVIVY---HRANGQFTEQSALAVARLPKVVGFK--DGVGDLDLTSRI 169
Cdd:cd00952 104 ADGTMLGRPMWLPLDVDTAVQFYRDVAEAvPEMAIAIYanpEAFKFDFPRAAWAELAQIPQVVAAKylGDIGALLSDLAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 170 VRTlRDSLGDKEFQFFNGLPTAEVSQQAYRSIGVtlyssatfAFAPDVSLAYYRALEEDDTELVASLNREFFHPLVRLRD 249
Cdd:cd00952 184 VKG-RMRLLPLEDDYYAAARLFPEEVTAFWSSGA--------ACGPAPVTALRDAVATGDWTDARALTDRMRWAAEPLFP 254
|
250 260 270
....*....|....*....|....*....|....*....
gi 669178896 250 TTP-----GYAVALVKAGVTFTG-LDAGSVRAPLVDASA 282
Cdd:cd00952 255 RGDfsefsKYNIALEKARFDAAGyMRAGPARPPYNTAPE 293
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
10-293 |
8.40e-05 |
|
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: 43.14 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 10 VTPFdSNGDVDLPALAQHIESGVAAGPGGVFAACGTGEFHALSAAEfRTVVDTVVTATKGRVpVFAGAGGALPVAKEFVA 89
Cdd:cd00953 9 ITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQE-KLELLKAYSDITDKV-IFQVGSLNLEESIELAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 90 IAEEAGADGILLLPP-YLVGAPAQGLVEYVKQVSEAsdLPVIVYHRANGQFTEQSALAVARLPK----VVGFKDGVGDLD 164
Cdd:cd00953 86 AAKSFGIYAIASLPPyYFPGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIKKaggdIIGVKDTNEDIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669178896 165 LTSRIVRTLRDslgdkeFQFFNGlPTAEVSQqAYRSiGVTLYSSATFAFAPDVsLAYYRaleeDDTELVASLNREFFHPL 244
Cdd:cd00953 164 HMLEYKRLVPD------FKVYSG-PDSLIFS-ALRS-GLDGSVAAASNYLPEV-FVKIK----DHVAIEDAFKLQFLINE 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 669178896 245 VRLRDTTPGYAVA---LVKagvTFTGLDAGSVRAPLVDASAQHRYELEQIVA 293
Cdd:cd00953 230 VLDASRKYGSWSAnysLVK---IFQGYDAGEPRPPFYPLDEEEEEKLRKEVN 278
|
|
| |
