|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
6-301 |
1.52e-164 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 459.28 E-value: 1.52e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 6 ELREIIRNGLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAA-RAVSGDAPVIA 84
Cdd:PRK03620 2 ELKQILGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAvETTAGRVPVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 85 GCGYGTRIACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYNRGQARVSAEQLAQLADECPNLI 164
Cdd:PRK03620 82 GAGGGTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNRDNAVLTADTLARLAERCPNLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 165 GFKDGTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGMPTYSSAVFNFVPETALKFHKAFLAGDDAACEQMLRD 244
Cdd:PRK03620 162 GFKDGVGDIELMQRIVRALGDRLLYLGGLPTAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLDD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 636785236 245 FYYPFARIRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIASAR 301
Cdd:PRK03620 242 FFLPYVALRNRKKGYAVSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGG 298
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
13-298 |
8.02e-153 |
|
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: 429.05 E-value: 8.02e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 13 NGLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAARAVS-GDAPVIAGCGYGTR 91
Cdd:cd00951 2 SGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETaGRVPVLAGAGYGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 92 IACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYNRGQARVSAEQLAQLADECPNLIGFKDGTG 171
Cdd:cd00951 82 TAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRANAVLTADSLARLAERCPNLVGFKDGVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 172 DIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGMPTYSSAVFNFVPETALKFHKAFLAGDDAACEQMLRDFYYPFAR 251
Cdd:cd00951 162 DIELMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFFLPYVD 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 636785236 252 IRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIA 298
Cdd:cd00951 242 IRNRRKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIK 288
|
|
| KdgD |
TIGR03249 |
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only ... |
7-300 |
2.88e-125 |
|
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: 359.41 E-value: 2.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 7 LREIIRNGLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAA-RAVSGDAPVIAG 85
Cdd:TIGR03249 1 MKRKAGSGLLSFPVTPFDADGSFDEAAYRENIEWLLGYGLEALFAAGGTGEFFSLTPAEYEQVVEIAvSTAKGKVPVYTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 86 CGYGTRIACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYNRGQARVSAEQLAQLADECPNLIG 165
Cdd:TIGR03249 81 VGGNTSDAIEIARLAEKAGADGYLLLPPYLINGEQEGLYAHVEAVCESTDLGVIVYQRDNAVLNADTLERLADRCPNLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 166 FKDGTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGMPTYSSAVFNFVPETALKFHKAFLAGDDAACEQMLRDF 245
Cdd:TIGR03249 161 FKDGIGDMEQMIEITQRLGDRLGYLGGMPTAEVTAPAYLPLGVTSYSSAIFNFIPHIARAFYEALRRGDHATVGEIYKEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 636785236 246 YYPFARIRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIASA 300
Cdd:TIGR03249 241 ILPINEIRNRKKGYAVSIIKAGMEIVGLPAGPVRPPLTDLTKEEYAQLEVILKKA 295
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
14-300 |
1.90e-57 |
|
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: 186.51 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 14 GLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAA-RAVSGDAPVIAGCG-YGTR 91
Cdd:COG0329 4 GVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVvEAAAGRVPVIAGVGsNSTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 92 IACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYN---RGQARVSAEQLAQLAdECPNLIGFKD 168
Cdd:COG0329 84 EAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNipgRTGVDLSPETLARLA-EIPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 169 GTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGmptYSSAVFNFVPETALKFHKAFLAGDDAACEQmLRDFYYP 248
Cdd:COG0329 163 ASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADG---VISVTANVAPELMVALYEAALAGDLAEARA-LQDRLLP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 636785236 249 FARIrDRKAGYaVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIASA 300
Cdd:COG0329 239 LIRA-LFAEGN-PAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
14-300 |
8.62e-38 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 135.19 E-value: 8.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 14 GLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVV-KAARAVSGDAPVIAGCG-YGTR 91
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVeITVNEAKGRIPVIAGVGsNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 92 IACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYN---RGQARVSAEQLAQLAdECPNLIGFKD 168
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNvpsRTGVDLTPETVGRLA-TNPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 169 GTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGmptYSSAVFNFVPETALKFHKAFLAGDDAACEQmLRDFYYP 248
Cdd:pfam00701 163 ASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADG---VISVTSNIAGHRMRQMYKALKNGDLATAAL-INHKLLP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 636785236 249 FarIRDRKAGYAVSAVKAGVRLRGFEAGP-VRAPLTDLTDEEVEMMRELIASA 300
Cdd:pfam00701 239 L--IKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
6-301 |
1.52e-164 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 459.28 E-value: 1.52e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 6 ELREIIRNGLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAA-RAVSGDAPVIA 84
Cdd:PRK03620 2 ELKQILGSGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAvETTAGRVPVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 85 GCGYGTRIACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYNRGQARVSAEQLAQLADECPNLI 164
Cdd:PRK03620 82 GAGGGTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNRDNAVLTADTLARLAERCPNLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 165 GFKDGTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGMPTYSSAVFNFVPETALKFHKAFLAGDDAACEQMLRD 244
Cdd:PRK03620 162 GFKDGVGDIELMQRIVRALGDRLLYLGGLPTAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLDD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 636785236 245 FYYPFARIRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIASAR 301
Cdd:PRK03620 242 FFLPYVALRNRKKGYAVSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGG 298
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
13-298 |
8.02e-153 |
|
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: 429.05 E-value: 8.02e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 13 NGLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAARAVS-GDAPVIAGCGYGTR 91
Cdd:cd00951 2 SGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETaGRVPVLAGAGYGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 92 IACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYNRGQARVSAEQLAQLADECPNLIGFKDGTG 171
Cdd:cd00951 82 TAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNRANAVLTADSLARLAERCPNLVGFKDGVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 172 DIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGMPTYSSAVFNFVPETALKFHKAFLAGDDAACEQMLRDFYYPFAR 251
Cdd:cd00951 162 DIELMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFFLPYVD 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 636785236 252 IRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIA 298
Cdd:cd00951 242 IRNRRKGYAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIK 288
|
|
| KdgD |
TIGR03249 |
5-dehydro-4-deoxyglucarate dehydratase; 5-dehydro-4-deoxyglucarate dehydratase not only ... |
7-300 |
2.88e-125 |
|
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: 359.41 E-value: 2.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 7 LREIIRNGLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAA-RAVSGDAPVIAG 85
Cdd:TIGR03249 1 MKRKAGSGLLSFPVTPFDADGSFDEAAYRENIEWLLGYGLEALFAAGGTGEFFSLTPAEYEQVVEIAvSTAKGKVPVYTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 86 CGYGTRIACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYNRGQARVSAEQLAQLADECPNLIG 165
Cdd:TIGR03249 81 VGGNTSDAIEIARLAEKAGADGYLLLPPYLINGEQEGLYAHVEAVCESTDLGVIVYQRDNAVLNADTLERLADRCPNLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 166 FKDGTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGMPTYSSAVFNFVPETALKFHKAFLAGDDAACEQMLRDF 245
Cdd:TIGR03249 161 FKDGIGDMEQMIEITQRLGDRLGYLGGMPTAEVTAPAYLPLGVTSYSSAIFNFIPHIARAFYEALRRGDHATVGEIYKEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 636785236 246 YYPFARIRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIASA 300
Cdd:TIGR03249 241 ILPINEIRNRKKGYAVSIIKAGMEIVGLPAGPVRPPLTDLTKEEYAQLEVILKKA 295
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
15-297 |
5.32e-64 |
|
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: 202.78 E-value: 5.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 15 LLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAAR-AVSGDAPVIAGCGY-GTRI 92
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVeAVAGRVPVIAGVGAnSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 93 ACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYNRGQA---RVSAEQLAQLAdECPNLIGFKDG 169
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRtgvDLSPETIARLA-EHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 170 TGDIDTVRRVTIALGDRLSYIGGmptHELFAQAYRGAGMPTYSSAVFNFVPETALKFHKAFLAGDDAACEQMLRDFYYPf 249
Cdd:cd00408 160 SGDLDRLTRLIALLGPDFAVLSG---DDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPL- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 636785236 250 arIRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELI 297
Cdd:cd00408 236 --IEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
14-300 |
1.90e-57 |
|
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: 186.51 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 14 GLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAA-RAVSGDAPVIAGCG-YGTR 91
Cdd:COG0329 4 GVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVvEAAAGRVPVIAGVGsNSTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 92 IACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYN---RGQARVSAEQLAQLAdECPNLIGFKD 168
Cdd:COG0329 84 EAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNipgRTGVDLSPETLARLA-EIPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 169 GTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGmptYSSAVFNFVPETALKFHKAFLAGDDAACEQmLRDFYYP 248
Cdd:COG0329 163 ASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADG---VISVTANVAPELMVALYEAALAGDLAEARA-LQDRLLP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 636785236 249 FARIrDRKAGYaVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIASA 300
Cdd:COG0329 239 LIRA-LFAEGN-PAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
14-300 |
8.62e-38 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 135.19 E-value: 8.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 14 GLLSFPVTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVV-KAARAVSGDAPVIAGCG-YGTR 91
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVeITVNEAKGRIPVIAGVGsNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 92 IACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYN---RGQARVSAEQLAQLAdECPNLIGFKD 168
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNvpsRTGVDLTPETVGRLA-TNPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 169 GTGDIDTVRRVTIALGDRLSYIGGMPTHELFAQAYRGAGmptYSSAVFNFVPETALKFHKAFLAGDDAACEQmLRDFYYP 248
Cdd:pfam00701 163 ASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADG---VISVTSNIAGHRMRQMYKALKNGDLATAAL-INHKLLP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 636785236 249 FarIRDRKAGYAVSAVKAGVRLRGFEAGP-VRAPLTDLTDEEVEMMRELIASA 300
Cdd:pfam00701 239 L--IKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
20-297 |
2.11e-37 |
|
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: 134.16 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 20 VTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAAR-AVSGDAPVIAGCG-YGTRIACDMA 97
Cdd:cd00950 9 VTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVeAVNGRVPVIAGTGsNNTAEAIELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 98 REIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYN---RGQARVSAEQLAQLAdECPNLIGFKDGTGDID 174
Cdd:cd00950 89 KRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNvpgRTGVNIEPETVLRLA-EHPNIVGIKEATGDLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 175 TVRRVTIALGDRLSYIGG-----MPTHelfaqAYRGAGMptySSAVFNFVPETALKFHKAFLAGDDAACEQmLRDFYYPF 249
Cdd:cd00950 168 RVSELIALCPDDFAVLSGddaltLPFL-----ALGGVGV---ISVAANVAPKLMAEMVRAALAGDLEKARE-LHRKLLPL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 636785236 250 ARIRDRKAGyaVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELI 297
Cdd:cd00950 239 IKALFAEPN--PIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
14-300 |
1.20e-20 |
|
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: 89.31 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 14 GLLSFPVTPFDAEDR--FAAkpfsahLEWLSSYPVA----GLIVAGGTGELFSLTPGEVVEVV-KAARAVSGDAPVIAGC 86
Cdd:TIGR00674 1 GVITALITPFKEDGSvdFAA------LEKLIDFQIEngtdAIVVVGTTGESPTLSHEEHKKVIeFVVDLVNGRVPVIAGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 87 GY-GTRIACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKATNMGVIVYN---RGQARVSAEQLAQLADEcPN 162
Cdd:TIGR00674 75 GSnATEEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNvpsRTGVSLYPETVKRLAEE-PN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 163 LIGFKDGTGDIDTVRRVTIALGDRLSYIGG--MPTHELFAQAYRGAgmptySSAVFNFVPETALKFHKAFLAGD-DAACE 239
Cdd:TIGR00674 154 IVAIKEATGNLERISEIKAIAPDDFVVLSGddALTLPMMALGGKGV-----ISVTANVAPKLMKEMVNNALEGDfAEARE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636785236 240 --QMLRDFYypfarirdrKAGYAVS---AVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIASA 300
Cdd:TIGR00674 229 ihQKLMPLH---------KALFIETnpiPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
14-298 |
2.10e-16 |
|
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: 77.74 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 14 GLLSFPVTPFDAE---DRFAAKPFSAHLewLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKA-ARAVSGDAPVIA--GCg 87
Cdd:cd00954 3 GLIAALLTPFDENgeiNEDVLRAIVDYL--IEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIvAEAAKGKVTLIAhvGS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 88 YGTRIACDMAREIEAAGGDGILLLPHYLTEAPADGIAARVRAVCKAT-NMGVIVYNRGQ---ARVSAEQLAQLAdECPNL 163
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHIPAltgVNLTLEQFLELF-EIPNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 164 IGFKDGTGDIDTVRRVTIALGDRLSYIGGMptHELFAQAY----RGAGMPTYssavfNFVPETALKFHKAFLAGDdaacE 239
Cdd:cd00954 159 IGVKFTATDLYDLERIRAASPEDKLVLNGF--DEMLLSALalgaDGAIGSTY-----NVNGKRYRKIFEAFNAGD----I 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 240 QMLRDFYYPFAR-IRDRKAGYAVSAVKAGVRLRGFEAGPVRAPLTDLTDEEVEMMRELIA 298
Cdd:cd00954 228 DTARELQHVINDvITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAKELAA 287
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
20-299 |
3.21e-11 |
|
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: 62.40 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 20 VTPFdAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVKAARAVsGDAPVIAGCGYGTRIACDMARE 99
Cdd:cd00953 9 ITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDI-TDKVIFQVGSLNLEESIELARA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 100 IEAAGGDGILLL-PHYLTEAPADGIAARVRAVCKAtnMGVIVYNRGQAR---VSAEQLAQLADECPNLIGFKDGTGDIDT 175
Cdd:cd00953 87 AKSFGIYAIASLpPYYFPGIPEEWLIKYFTDISSP--YPTFIYNYPKATgydINARMAKEIKKAGGDIIGVKDTNEDISH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 176 VRRVTIALGDRLSYIGgmPTHELFAqAYRgAGMPTYSSAVFNFVPETALKFHKAFlAGDDAACEQMLRDFYYPFARirdr 255
Cdd:cd00953 165 MLEYKRLVPDFKVYSG--PDSLIFS-ALR-SGLDGSVAAASNYLPEVFVKIKDHV-AIEDAFKLQFLINEVLDASR---- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 636785236 256 KAGYAvSAVKAGVR-LRGFEAGPVRAPLTDLTDEEVEMMRELIAS 299
Cdd:cd00953 236 KYGSW-SANYSLVKiFQGYDAGEPRPPFYPLDEEEEEKLRKEVNE 279
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
20-172 |
2.18e-08 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 54.26 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636785236 20 VTPFDAEDRFAAKPFSAHLEWLSSYPVAGLIVAGGTGELFSLTPGEVVEVVK-AARAVSGDAPVIAGCGY-GTRIACDMA 97
Cdd:PLN02417 10 KTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGhTVNCFGGKIKVIGNTGSnSTREAIHAT 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636785236 98 REIEAAGGDGILLLPHYLTEAPADGIAARVRAVckaTNMG-VIVYN---RGQARVSAEQLAQLADEcPNLIGFKDGTGD 172
Cdd:PLN02417 90 EQGFAVGMHAALHINPYYGKTSQEGLIKHFETV---LDMGpTIIYNvpgRTGQDIPPEVIFKIAQH-PNFAGVKECTGN 164
|
|
| |
