|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
10-260 |
1.09e-84 |
|
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: 254.39 E-value: 1.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:cd00408 34 GLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREAIELARHAEEAGADGVLVVPPYYNK--PSQEGI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:cd00408 112 VAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSGDLDRLTRLIALLGP-DFAVLSGDDDLLLPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:cd00408 191 LALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLS 270
|
250
....*....|.
gi 55725758 250 PAEEEALRMDF 260
Cdd:cd00408 271 EEERAKLEALL 281
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
10-257 |
6.08e-78 |
|
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: 237.36 E-value: 6.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:COG0329 38 GLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTAEAIELARHAEEAGADAVLVVPPYYNK--PTQEGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:COG0329 116 YAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIKEASGDLDRIAELIRATGD-DFAVLSGDDALALPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:COG0329 195 LALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLS 274
|
....*...
gi 55725758 250 PAEEEALR 257
Cdd:COG0329 275 EEERAELR 282
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
10-257 |
3.69e-45 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 153.29 E-value: 3.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRGrmSSAAL 89
Cdd:pfam00701 38 GLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTSEAIHLAQLAEEYGADGALAVTPYYNKP--SQEGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:pfam00701 116 YQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIKEASGDLDRMINIKKEAGP-DFVILSGDDETMLPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGP-CRAPLQEL 248
Cdd:pfam00701 195 LSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPL 274
|
....*....
gi 55725758 249 SPAEEEALR 257
Cdd:pfam00701 275 SEEERPELE 283
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
10-257 |
8.90e-31 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 115.86 E-value: 8.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:PRK04147 41 GLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSVNTAEAQELAKYATELGYDAISAVTPFYYP--FSFEEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGD---VTRIglivhKTRKQDFQVLAGSAGFL 166
Cdd:PRK04147 119 CDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGVKQTAGDlyqLERI-----RKAFPDKLIYNGFDEMF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 167 MASYALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQH---RLIEPNAAVtrrfGI-PGLKKIMDWFGYYGGPCR 242
Cdd:PRK04147 194 ASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHecnDVIDLLIKN----GVyPGLKEILHYMGVDAGLCR 269
|
250
....*....|....*
gi 55725758 243 APLQELSPAEEEALR 257
Cdd:PRK04147 270 KPFKPVDEKYLPALK 284
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
10-260 |
1.09e-84 |
|
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: 254.39 E-value: 1.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:cd00408 34 GLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREAIELARHAEEAGADGVLVVPPYYNK--PSQEGI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:cd00408 112 VAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSGDLDRLTRLIALLGP-DFAVLSGDDDLLLPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:cd00408 191 LALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLS 270
|
250
....*....|.
gi 55725758 250 PAEEEALRMDF 260
Cdd:cd00408 271 EEERAKLEALL 281
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
10-257 |
6.08e-78 |
|
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: 237.36 E-value: 6.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:COG0329 38 GLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTAEAIELARHAEEAGADAVLVVPPYYNK--PTQEGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:COG0329 116 YAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIKEASGDLDRIAELIRATGD-DFAVLSGDDALALPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:COG0329 195 LALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLS 274
|
....*...
gi 55725758 250 PAEEEALR 257
Cdd:COG0329 275 EEERAELR 282
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
10-257 |
8.10e-62 |
|
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: 196.18 E-value: 8.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYyrGRMSSAAL 89
Cdd:cd00950 37 GLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTAEAIELTKRAEKAGADAALVVTPYY--NKPSQEGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:cd00950 115 YAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIKEATGDLDRVSELIALCPD-DFAVLSGDDALTLPF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRL--------IEPNAAvtrrfgipGLKKIMDWFGYYGGPC 241
Cdd:cd00950 194 LALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLlplikalfAEPNPI--------PVKAALALLGLISGEL 265
|
250
....*....|....*.
gi 55725758 242 RAPLQELSPAEEEALR 257
Cdd:cd00950 266 RLPLVPLSEELRAKLR 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
10-257 |
3.69e-45 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 153.29 E-value: 3.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRGrmSSAAL 89
Cdd:pfam00701 38 GLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTSEAIHLAQLAEEYGADGALAVTPYYNKP--SQEGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:pfam00701 116 YQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIKEASGDLDRMINIKKEAGP-DFVILSGDDETMLPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGP-CRAPLQEL 248
Cdd:pfam00701 195 LSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPL 274
|
....*....
gi 55725758 249 SPAEEEALR 257
Cdd:pfam00701 275 SEEERPELE 283
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
10-258 |
3.50e-44 |
|
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: 150.92 E-value: 3.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYrgRMSSAAL 89
Cdd:cd00954 38 GLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLNLKESQELAKHAEELGYDAISAITPFYY--KFSFEEI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSP-IPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRkQDFQVLAGSAGFLMA 168
Cdd:cd00954 116 KDYYREIIAAAAsLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGVKFTATDLYDLERIRAASP-EDKLVLNGFDEMLLS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 169 SYALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQEL 248
Cdd:cd00954 195 ALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKV 274
|
250
....*....|
gi 55725758 249 SPAEEEALRM 258
Cdd:cd00954 275 TEKALAKAKE 284
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
10-257 |
8.90e-31 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 115.86 E-value: 8.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:PRK04147 41 GLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSVNTAEAQELAKYATELGYDAISAVTPFYYP--FSFEEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGD---VTRIglivhKTRKQDFQVLAGSAGFL 166
Cdd:PRK04147 119 CDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGVKQTAGDlyqLERI-----RKAFPDKLIYNGFDEMF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 167 MASYALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQH---RLIEPNAAVtrrfGI-PGLKKIMDWFGYYGGPCR 242
Cdd:PRK04147 194 ASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHecnDVIDLLIKN----GVyPGLKEILHYMGVDAGLCR 269
|
250
....*....|....*
gi 55725758 243 APLQELSPAEEEALR 257
Cdd:PRK04147 270 KPFKPVDEKYLPALK 284
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
10-192 |
1.02e-28 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 110.12 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEV----VSRVRQAMPknrlLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPcYYrGRMS 85
Cdd:PLN02417 38 GLIVGGTTGEGQLMSWDEHIMLightVNCFGGKIK----VIGNTGSNSTREAIHATEQGFAVGMHAALHINP-YY-GKTS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 86 SAALIHHYTKVADFSPipVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDvTRIGLIVhktrKQDFQVLAGSAG- 164
Cdd:PLN02417 112 QEGLIKHFETVLDMGP--TIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKECTGN-DRVKQYT----EKGILLWSGNDDe 184
|
170 180
....*....|....*....|....*...
gi 55725758 165 FLMASYALGAVGGVCALANVLGAQVCQL 192
Cdd:PLN02417 185 CHDARWDYGADGVISVTSNLVPGLMHKL 212
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
13-257 |
2.19e-19 |
|
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: 85.13 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 13 VQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAamvvTPCYYRGRMSSAALIHH 92
Cdd:cd00953 39 VAGTTGLGPSLSFQEKLELLKAYSDITDKVIFQVGSLNLEESIELARAAKSFGIYAIAS----LPPYYFPGIPEEWLIKY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 93 YTKVAdfSPIPVVLYSVPANTGLDLPVDAVVTLSQHP-NIVGMKDSGGDVTRIglIVHKTRKQDFQVLAGSAGFLMASYA 171
Cdd:cd00953 115 FTDIS--SPYPTFIYNYPKATGYDINARMAKEIKKAGgDIIGVKDTNEDISHM--LEYKRLVPDFKVYSGPDSLIFSALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 172 LGAVGGVCALANVLGAQVCQLERLCCTgqwEEAQKLQhRLIEPNAAVTRRFG----IPGLKKIMDwfGYYGGPCRAPLQE 247
Cdd:cd00953 191 SGLDGSVAAASNYLPEVFVKIKDHVAI---EDAFKLQ-FLINEVLDASRKYGswsaNYSLVKIFQ--GYDAGEPRPPFYP 264
|
250
....*....|
gi 55725758 248 LSPAEEEALR 257
Cdd:cd00953 265 LDEEEEEKLR 274
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
10-244 |
3.04e-14 |
|
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: 70.94 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMpKNRL-LLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYyrGRMSSAA 88
Cdd:cd00952 45 GILTMGTFGECATLTWEEKQAFVATVVETV-AGRVpVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMW--LPLDVDT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 89 LIHHYTKVADFSP-IPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSG------GDVT----RIGLIVHktrkqDFQ 157
Cdd:cd00952 122 AVQFYRDVAEAVPeMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKYLGdigallSDLAavkgRMRLLPL-----EDD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 158 VLAGSAGFLMASYALGAVGGVCALANVLgaqvcQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIP-------GLKKI 230
Cdd:cd00952 197 YYAAARLFPEEVTAFWSSGAACGPAPVT-----ALRDAVATGDWTDARALTDRMRWAAEPLFPRGDFSefskyniALEKA 271
|
250
....*....|....*.
gi 55725758 231 -MDWFGYY-GGPCRAP 244
Cdd:cd00952 272 rFDAAGYMrAGPARPP 287
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
15-257 |
1.41e-09 |
|
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: 57.33 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 15 GSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQAtVEMTVSMAQVGADAAMVVTPcyYRGRMSSAALIHHYT 94
Cdd:cd00951 42 GGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYGTATA-IAYAQAAEKAGADGILLLPP--YLTEAPQEGLYAHVE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 95 KVADFSPIPVVLYSvPANTGLDlpVDAVVTLSQH-PNIVGMKDSGGDVTRIGLIVHKtRKQDFQVLAG--SAGFLMASY- 170
Cdd:cd00951 119 AVCKSTDLGVIVYN-RANAVLT--ADSLARLAERcPNLVGFKDGVGDIELMRRIVAK-LGDRLLYLGGlpTAEVFALAYl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 171 ALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRR---FGIPGLKKIMDWFGYYGGPCRAPLQE 247
Cdd:cd00951 195 AMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFFLPYVDIRNRrkgYAVSIVKAGARLVGRDAGPVRPPLTD 274
|
250
....*....|
gi 55725758 248 LSPAEEEALR 257
Cdd:cd00951 275 LTEEELAQLT 284
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
15-256 |
4.86e-07 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 49.81 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 15 GSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGcESTQATVEMTVSMAQVGADAAMVVTPcyYRGRMSSAALIHHYT 94
Cdd:PRK03620 49 GGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTAQAIEYAQAAERAGADGILLLPP--YLTEAPQEGLAAHVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 95 KVADFSPIPVVLYSvPANTGLDLpvDAVVTLS-QHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAG--SAGFLMASY- 170
Cdd:PRK03620 126 AVCKSTDLGVIVYN-RDNAVLTA--DTLARLAeRCPNLVGFKDGVGDIELMQRIVRALGD-RLLYLGGlpTAEVFAAAYl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 171 ALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRR---FGIPGLKKIMDWFGYYGGPCRAPLQE 247
Cdd:PRK03620 202 ALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLDDFFLPYVALRNRkkgYAVSIVKAGARLVGLDAGPVRAPLTD 281
|
....*....
gi 55725758 248 LSPAEEEAL 256
Cdd:PRK03620 282 LTPEELAEL 290
|
|
|