|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
4-301 |
1.39e-178 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 494.72 E-value: 1.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 4 QQIKAALGSGLLSFPVTPFDAENRFAAAPYQKHVEWLSGFDAPVLFAAGGTGEFFSLTPDEIPAIVKAA-KESAGKTAIV 82
Cdd:PRK03620 1 QELKQILGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAvETTAGRVPVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 83 SGCGYGTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRDNAVLQADTLARLCDDCPNL 162
Cdd:PRK03620 81 AGAGGGTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNRDNAVLTADTLARLAERCPNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 163 VGFKDGTGDIGLVRQITAKMGDRLTYLGGMPTAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESILN 242
Cdd:PRK03620 161 VGFKDGVGDIELMQRIVRALGDRLLYLGGLPTAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499658772 243 SFFYPFMELRSRRKGYAVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALIDAHRE 301
Cdd:PRK03620 241 DFFLPYVALRNRKKGYAVSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGGA 299
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
11-298 |
4.33e-166 |
|
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: 462.56 E-value: 4.33e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 11 GSGLLSFPVTPFDAENRFAAAPYQKHVEWLSGFDAPVLFAAGGTGEFFSLTPDEIPAIVKAAKE-SAGKTAIVSGCGYGT 89
Cdd:cd00951 1 GSGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEeTAGRVPVLAGAGYGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 90 EIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRDNAVLQADTLARLCDDCPNLVGFKDGT 169
Cdd:cd00951 81 ATAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRANAVLTADSLARLAERCPNLVGFKDGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 170 GDIGLVRQITAKMGDRLTYLGGMPTAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESILNSFFYPFM 249
Cdd:cd00951 161 GDIELMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFFLPYV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499658772 250 ELRSRRKGYAVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALIDA 298
Cdd:cd00951 241 DIRNRRKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| KdgD |
TIGR03249 |
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only ... |
6-296 |
2.42e-141 |
|
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: 400.24 E-value: 2.42e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 6 IKAALGSGLLSFPVTPFDAENRFAAAPYQKHVEWLSGFDAPVLFAAGGTGEFFSLTPDEIPAIVKAA-KESAGKTAIVSG 84
Cdd:TIGR03249 1 MKRKAGSGLLSFPVTPFDADGSFDEAAYRENIEWLLGYGLEALFAAGGTGEFFSLTPAEYEQVVEIAvSTAKGKVPVYTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 85 CGYGTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRDNAVLQADTLARLCDDCPNLVG 164
Cdd:TIGR03249 81 VGGNTSDAIEIARLAEKAGADGYLLLPPYLINGEQEGLYAHVEAVCESTDLGVIVYQRDNAVLNADTLERLADRCPNLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 165 FKDGTGDIGLVRQITAKMGDRLTYLGGMPTAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESILNSF 244
Cdd:TIGR03249 161 FKDGIGDMEQMIEITQRLGDRLGYLGGMPTAEVTAPAYLPLGVTSYSSAIFNFIPHIARAFYEALRRGDHATVGEIYKEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499658772 245 FYPFMELRSRRKGYAVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALI 296
Cdd:TIGR03249 241 ILPINEIRNRKKGYAVSIIKAGMEIVGLPAGPVRPPLTDLTKEEYAQLEVIL 292
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
12-298 |
6.01e-58 |
|
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: 187.67 E-value: 6.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 12 SGLLSFPVTPFDAENRFAAAPYQKHVEWL--SGFDApvLFAAGGTGEFFSLTPDEIPAIVKAAKE-SAGKTAIVSGCG-Y 87
Cdd:COG0329 3 RGVIPALVTPFDADGSVDEEALRRLVEFLidAGVDG--LVVLGTTGESATLTDEERKRVLEAVVEaAAGRVPVIAGVGsN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 88 GTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYN---RDNAVLQADTLARLCdDCPNLVG 164
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNipgRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 165 FKDGTGDIGLVRQITAKMGDRLTYLGGMptAELFAEAY-LGASFTTysSAVFNFVPALANKFYAALRAGDRATCESIlNS 243
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFAVLSGD--DALALPALaLGADGVI--SVTANVAPELMVALYEAALAGDLAEARAL-QD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499658772 244 FFYPFMELRSRRKGyaVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALIDA 298
Cdd:COG0329 235 RLLPLIRALFAEGN--PAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKE 287
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
12-298 |
2.55e-47 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 160.23 E-value: 2.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 12 SGLLSFPVTPFDAENRFAAAPYQKHVEWL--SGFDApvLFAAGGTGEFFSLTPDEIPAIVKAAKESA-GKTAIVSGCG-Y 87
Cdd:pfam00701 3 SGIITALVTPFDTDGTLDFAALRQLIDFLinKGVDG--LVVGGTTGESFTLSTEEREQLVEITVNEAkGRIPVIAGVGsN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 88 GTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRD---NAVLQADTLARLCdDCPNLVG 164
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPsrtGVDLTPETVGRLA-TNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 165 FKDGTGDIGLVRQITAKMGDRLTYLGGmptAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESIlNSF 244
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSG---DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALI-NHK 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499658772 245 FYPFMELRSRRkgYAVAAVKAGVRLVGFDAGP-VRAPLSDLTGEEEEILKALIDA 298
Cdd:pfam00701 236 LLPLIKILFAE--PNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKA 288
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
4-301 |
1.39e-178 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 494.72 E-value: 1.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 4 QQIKAALGSGLLSFPVTPFDAENRFAAAPYQKHVEWLSGFDAPVLFAAGGTGEFFSLTPDEIPAIVKAA-KESAGKTAIV 82
Cdd:PRK03620 1 QELKQILGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAvETTAGRVPVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 83 SGCGYGTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRDNAVLQADTLARLCDDCPNL 162
Cdd:PRK03620 81 AGAGGGTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNRDNAVLTADTLARLAERCPNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 163 VGFKDGTGDIGLVRQITAKMGDRLTYLGGMPTAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESILN 242
Cdd:PRK03620 161 VGFKDGVGDIELMQRIVRALGDRLLYLGGLPTAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499658772 243 SFFYPFMELRSRRKGYAVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALIDAHRE 301
Cdd:PRK03620 241 DFFLPYVALRNRKKGYAVSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGGA 299
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
11-298 |
4.33e-166 |
|
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: 462.56 E-value: 4.33e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 11 GSGLLSFPVTPFDAENRFAAAPYQKHVEWLSGFDAPVLFAAGGTGEFFSLTPDEIPAIVKAAKE-SAGKTAIVSGCGYGT 89
Cdd:cd00951 1 GSGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEeTAGRVPVLAGAGYGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 90 EIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRDNAVLQADTLARLCDDCPNLVGFKDGT 169
Cdd:cd00951 81 ATAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRANAVLTADSLARLAERCPNLVGFKDGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 170 GDIGLVRQITAKMGDRLTYLGGMPTAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESILNSFFYPFM 249
Cdd:cd00951 161 GDIELMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFFLPYV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499658772 250 ELRSRRKGYAVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALIDA 298
Cdd:cd00951 241 DIRNRRKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| KdgD |
TIGR03249 |
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only ... |
6-296 |
2.42e-141 |
|
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: 400.24 E-value: 2.42e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 6 IKAALGSGLLSFPVTPFDAENRFAAAPYQKHVEWLSGFDAPVLFAAGGTGEFFSLTPDEIPAIVKAA-KESAGKTAIVSG 84
Cdd:TIGR03249 1 MKRKAGSGLLSFPVTPFDADGSFDEAAYRENIEWLLGYGLEALFAAGGTGEFFSLTPAEYEQVVEIAvSTAKGKVPVYTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 85 CGYGTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRDNAVLQADTLARLCDDCPNLVG 164
Cdd:TIGR03249 81 VGGNTSDAIEIARLAEKAGADGYLLLPPYLINGEQEGLYAHVEAVCESTDLGVIVYQRDNAVLNADTLERLADRCPNLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 165 FKDGTGDIGLVRQITAKMGDRLTYLGGMPTAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESILNSF 244
Cdd:TIGR03249 161 FKDGIGDMEQMIEITQRLGDRLGYLGGMPTAEVTAPAYLPLGVTSYSSAIFNFIPHIARAFYEALRRGDHATVGEIYKEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499658772 245 FYPFMELRSRRKGYAVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALI 296
Cdd:TIGR03249 241 ILPINEIRNRKKGYAVSIIKAGMEIVGLPAGPVRPPLTDLTKEEYAQLEVIL 292
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
14-296 |
2.14e-65 |
|
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: 206.63 E-value: 2.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 14 LLSFPVTPFDAENRFAAAPYQKHVEWLSGFDAPVLFAAGGTGEFFSLTPDEIPAIVKAAKESA-GKTAIVSGCGY-GTEI 91
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVaGRVPVIAGVGAnSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 92 ARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYN---RDNAVLQADTLARLCdDCPNLVGFKDG 168
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNipgRTGVDLSPETIARLA-EHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 169 TGDIGLVRQITAKMGDRLTYLGGMptaELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESiLNSFFYPF 248
Cdd:cd00408 160 SGDLDRLTRLIALLGPDFAVLSGD---DDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARA-LQDRLLPL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499658772 249 MELRSRRKGyaVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALI 296
Cdd:cd00408 236 IEALFKEGN--PAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
12-298 |
6.01e-58 |
|
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: 187.67 E-value: 6.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 12 SGLLSFPVTPFDAENRFAAAPYQKHVEWL--SGFDApvLFAAGGTGEFFSLTPDEIPAIVKAAKE-SAGKTAIVSGCG-Y 87
Cdd:COG0329 3 RGVIPALVTPFDADGSVDEEALRRLVEFLidAGVDG--LVVLGTTGESATLTDEERKRVLEAVVEaAAGRVPVIAGVGsN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 88 GTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYN---RDNAVLQADTLARLCdDCPNLVG 164
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNipgRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 165 FKDGTGDIGLVRQITAKMGDRLTYLGGMptAELFAEAY-LGASFTTysSAVFNFVPALANKFYAALRAGDRATCESIlNS 243
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFAVLSGD--DALALPALaLGADGVI--SVTANVAPELMVALYEAALAGDLAEARAL-QD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499658772 244 FFYPFMELRSRRKGyaVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALIDA 298
Cdd:COG0329 235 RLLPLIRALFAEGN--PAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKE 287
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
12-298 |
2.55e-47 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 160.23 E-value: 2.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 12 SGLLSFPVTPFDAENRFAAAPYQKHVEWL--SGFDApvLFAAGGTGEFFSLTPDEIPAIVKAAKESA-GKTAIVSGCG-Y 87
Cdd:pfam00701 3 SGIITALVTPFDTDGTLDFAALRQLIDFLinKGVDG--LVVGGTTGESFTLSTEEREQLVEITVNEAkGRIPVIAGVGsN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 88 GTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYNRD---NAVLQADTLARLCdDCPNLVG 164
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPsrtGVDLTPETVGRLA-TNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 165 FKDGTGDIGLVRQITAKMGDRLTYLGGmptAELFAEAYLGASFTTYSSAVFNFVPALANKFYAALRAGDRATCESIlNSF 244
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSG---DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALI-NHK 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499658772 245 FYPFMELRSRRkgYAVAAVKAGVRLVGFDAGP-VRAPLSDLTGEEEEILKALIDA 298
Cdd:pfam00701 236 LLPLIKILFAE--PNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKA 288
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
19-296 |
4.03e-39 |
|
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: 138.78 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 19 VTPFDAENRFAAAPYQKHVEWL--SGFDApvLFAAGGTGEFFSLTPDEIPAIVKAA-KESAGKTAIVSGCG-YGTEIARG 94
Cdd:cd00950 9 VTPFKDDGSVDFDALERLIEFQieNGTDG--LVVCGTTGESPTLSDEEHEAVIEAVvEAVNGRVPVIAGTGsNNTAEAIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 95 IARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYN---RDNAVLQADTLARLCdDCPNLVGFKDGTGD 171
Cdd:cd00950 87 LTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNvpgRTGVNIEPETVLRLA-EHPNIVGIKEATGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 172 IGLVRQITAKMGDRLTYLGGmpTAELFAEAY-LGASFTTysSAVFNFVPALANKFYAALRAGDRATCESIlNSFFYPFME 250
Cdd:cd00950 166 LDRVSELIALCPDDFAVLSG--DDALTLPFLaLGGVGVI--SVAANVAPKLMAEMVRAALAGDLEKAREL-HRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499658772 251 LRSRRKGyaVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALI 296
Cdd:cd00950 241 ALFAEPN--PIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
13-296 |
5.02e-22 |
|
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: 93.16 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 13 GLLSFPVTPFDAENRFAAAPYQKHVEWL--SGFDAPVLfaAGGTGEFFSLTPDEIPAIV-KAAKESAGKTAIVSGCGYG- 88
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQieNGTDAIVV--VGTTGESPTLSHEEHKKVIeFVVDLVNGRVPVIAGTGSNa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 89 TEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQATGMGVMVYN---RDNAVLQADTLARLCDDcPNLVGF 165
Cdd:TIGR00674 79 TEEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNvpsRTGVSLYPETVKRLAEE-PNIVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 166 KDGTGDIGLVRQITAKMGDRLTYLGG--MPTAELFAeayLGASFTTysSAVFNFVPALANKFYAALRAGDRATCESILNS 243
Cdd:TIGR00674 158 KEATGNLERISEIKAIAPDDFVVLSGddALTLPMMA---LGGKGVI--SVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499658772 244 FFYPFMELRSRRKGyavAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALI 296
Cdd:TIGR00674 233 LMPLHKALFIETNP---IPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVL 282
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
12-298 |
2.39e-15 |
|
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: 74.65 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 12 SGLLSFPVTPFDAENRFAAAPYQKHVEWL---SGFDApvLFAAGGTGEFFSLTPDEIPAIVKAAKESA-GKTAIVSGCG- 86
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLiekQGVDG--LYVNGSTGEGFLLSVEERKQIAEIVAEAAkGKVTLIAHVGs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 87 YGTEIARGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQAT-GMGVMVYN---RDNAVLQADTLARLCDDcPNL 162
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHipaLTGVNLTLEQFLELFEI-PNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 163 VGFKDGTGDIGLVRQITAKMG-DRLTYLGgmptaelFAEAYLGASFTTYSSAV---FNFVPALANKFYAALRAGDRATCE 238
Cdd:cd00954 159 IGVKFTATDLYDLERIRAASPeDKLVLNG-------FDEMLLSALALGADGAIgstYNVNGKRYRKIFEAFNAGDIDTAR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499658772 239 SILnsffYPFMEL-RSRRKGYAVAAVKAGVRLVGFDAGPVRAPLSDLTGEEEEILKALIDA 298
Cdd:cd00954 232 ELQ----HVINDViTVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAKELAAK 288
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
19-296 |
3.49e-08 |
|
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: 53.54 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 19 VTPFdAENRFAAAPYQKHVEWL--SGFDapVLFAAGGTGEFFSLTPDEIPAIVKAAKESAGKtAIVSGCGYGTEIARGIA 96
Cdd:cd00953 9 ITPF-TGNKIDKEKFKKHCENLisKGID--YVFVAGTTGLGPSLSFQEKLELLKAYSDITDK-VIFQVGSLNLEESIELA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 97 RSVEAAGGDGILLL-PHYLIDAPQEGLYAHVRAVCQAtgMGVMVYNRDNAV---LQADTLARLCDDCPNLVGFKDGTGDI 172
Cdd:cd00953 85 RAAKSFGIYAIASLpPYYFPGIPEEWLIKYFTDISSP--YPTFIYNYPKATgydINARMAKEIKKAGGDIIGVKDTNEDI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 173 GLVRQITAKMGDRLTYLGgmPTAELFAEAYLGASFTTYSSAvfNFVPALANKF--YAALRAGDRAtcESILNSFFypfmE 250
Cdd:cd00953 163 SHMLEYKRLVPDFKVYSG--PDSLIFSALRSGLDGSVAAAS--NYLPEVFVKIkdHVAIEDAFKL--QFLINEVL----D 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499658772 251 LrSRRKGYAvAAVKAGVR-LVGFDAGPVRAPLSDLTGEEEEILKALI 296
Cdd:cd00953 233 A-SRKYGSW-SANYSLVKiFQGYDAGEPRPPFYPLDEEEEEKLRKEV 277
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
19-171 |
2.80e-07 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 50.80 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 19 VTPFDAENRFAAAPYQK----HVEwlSGFDApvLFAAGGTGEFFSLTPDE-IPAIVKAAKESAGKTAIVSGCGY-GTEIA 92
Cdd:PLN02417 10 KTPYLPDGRFDLEAYDSlvnmQIE--NGAEG--LIVGGTTGEGQLMSWDEhIMLIGHTVNCFGGKIKVIGNTGSnSTREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658772 93 RGIARSVEAAGGDGILLLPHYLIDAPQEGLYAHVRAVCQatgMG-VMVYN---RDNAVLQADTLARLCDDcPNLVGFKDG 168
Cdd:PLN02417 86 IHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD---MGpTIIYNvpgRTGQDIPPEVIFKIAQH-PNFAGVKEC 161
|
...
gi 499658772 169 TGD 171
Cdd:PLN02417 162 TGN 164
|
|
| |
