|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
2-288 |
4.29e-102 |
|
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: 299.76 E-value: 4.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 2 KLKGIYCPMITPF-KNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGATSM 78
Cdd:COG0329 1 KFRGVIPALVTPFdADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAgrVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIV 237
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAgDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKKMEV 288
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSG-PVRLPLLPLSEEERAELRAALKELGL 290
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-283 |
2.51e-94 |
|
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: 279.82 E-value: 2.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 6 IYCPMITPFKNGG-IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRMEE 82
Cdd:cd00408 1 VIPALVTPFTADGeVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVagRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 83 ALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDTS 162
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 163 GDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIVKIMD 241
Cdd:cd00408 161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAgDLEEARALQDRLLPLIEALF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1313375691 242 TGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLL 283
Cdd:cd00408 241 KEGNPAPVKAALALLGLDAG-PVRLPLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-285 |
2.81e-73 |
|
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: 226.44 E-value: 2.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 5 GIYCPMITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRME 81
Cdd:TIGR00674 1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVngRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 82 EALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDT 161
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 162 SGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIVKIM 240
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNAlEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1313375691 241 DTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEG-ELRLPLTELSEEHRNKLRDVLKD 284
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
2-284 |
2.33e-72 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 224.17 E-value: 2.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 2 KLKGIYCPMITPFKN-GGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDT--TSLPVIAGATSM 78
Cdd:pfam00701 1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEakGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIV 237
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALkNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGDDVRAPLLNLTSEEKDTVDGLLK 284
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILK 287
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-285 |
3.32e-39 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 138.97 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 1 MKLKGIYCPMITPF-KNGGIDLEGLEKNIAF-LEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGAT 76
Cdd:PRK04147 2 KNLKGVYAALLTPFdEDGQIDEQGLRRLVRFnIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKgkVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 77 SMRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNII 156
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 157 GIKDTSGDMKKFQVIVNLVPeDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMN 235
Cdd:PRK04147 162 GVKQTAGDLYQLERIRKAFP-DKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAgDIQEAQELQHECND 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 236 IV-KIMDTGTFPaGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:PRK04147 241 VIdLLIKNGVYP-GLKEILHYMGVDAG-LCRKPFKPVDEKYLPALKALAAK 289
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
2-288 |
4.29e-102 |
|
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: 299.76 E-value: 4.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 2 KLKGIYCPMITPF-KNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGATSM 78
Cdd:COG0329 1 KFRGVIPALVTPFdADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAgrVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIV 237
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAgDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKKMEV 288
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSG-PVRLPLLPLSEEERAELRAALKELGL 290
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
6-283 |
2.51e-94 |
|
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: 279.82 E-value: 2.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 6 IYCPMITPFKNGG-IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRMEE 82
Cdd:cd00408 1 VIPALVTPFTADGeVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVagRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 83 ALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDTS 162
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 163 GDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIVKIMD 241
Cdd:cd00408 161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAgDLEEARALQDRLLPLIEALF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1313375691 242 TGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLL 283
Cdd:cd00408 241 KEGNPAPVKAALALLGLDAG-PVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
3-280 |
1.25e-80 |
|
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: 245.10 E-value: 1.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 3 LKGIYCPMITPFKNGG-IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMR 79
Cdd:cd00950 1 FGGSITALVTPFKDDGsVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVngRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 80 MEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIK 159
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 160 DTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIVK 238
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAgDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1313375691 239 IMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVD 280
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISG-ELRLPLVPLSEELRAKLR 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-285 |
2.81e-73 |
|
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: 226.44 E-value: 2.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 5 GIYCPMITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRME 81
Cdd:TIGR00674 1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVngRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 82 EALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDT 161
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 162 SGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIVKIM 240
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNAlEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1313375691 241 DTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEG-ELRLPLTELSEEHRNKLRDVLKD 284
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
2-284 |
2.33e-72 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 224.17 E-value: 2.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 2 KLKGIYCPMITPFKN-GGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDT--TSLPVIAGATSM 78
Cdd:pfam00701 1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEakGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIV 237
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALkNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGDDVRAPLLNLTSEEKDTVDGLLK 284
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILK 287
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
3-285 |
4.53e-50 |
|
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: 167.10 E-value: 4.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 3 LKGIYCPMITPF-KNGGIDLEGLEKNIAFL-EKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGATSM 78
Cdd:cd00954 1 LKGLIAALLTPFdENGEINEDVLRAIVDYLiEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKgkVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLS-SHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIG 157
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIaAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 158 IKDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNI 236
Cdd:cd00954 161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFnAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1313375691 237 VKIMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:cd00954 241 ITVLIKNGLYPTLKAILRLMGLDAG-PCRLPLRKVTEKALAKAKELAAK 288
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-285 |
3.32e-39 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 138.97 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 1 MKLKGIYCPMITPF-KNGGIDLEGLEKNIAF-LEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGAT 76
Cdd:PRK04147 2 KNLKGVYAALLTPFdEDGQIDEQGLRRLVRFnIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKgkVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 77 SMRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNII 156
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 157 GIKDTSGDMKKFQVIVNLVPeDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMN 235
Cdd:PRK04147 162 GVKQTAGDLYQLERIRKAFP-DKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAgDIQEAQELQHECND 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 236 IV-KIMDTGTFPaGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:PRK04147 241 VIdLLIKNGVYP-GLKEILHYMGVDAG-LCRKPFKPVDEKYLPALKALAAK 289
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
9-287 |
4.66e-34 |
|
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: 124.80 E-value: 4.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 9 PMITPFKNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTSlPVIAGATSMRMEEALEIIA 88
Cdd:cd00953 7 PVITPFTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD-KVIFQVGSLNLEESIELAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 89 YSADMGAEAALVAPPYYF-RTSQEGLFSYYSNLSSHstLPIILYNIPVFTGNPFLPPLVKRL-SVLDNIIGIKDTSGDMK 166
Cdd:cd00953 86 AAKSFGIYAIASLPPYYFpGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIkKAGGDIIGVKDTNEDIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 167 KFQVIVNLVPeDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRtwERDIDRAVGLQKLLMNIVKIMDT-GTF 245
Cdd:cd00953 164 HMLEYKRLVP-DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKD--HVAIEDAFKLQFLINEVLDASRKyGSW 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1313375691 246 PAGLKYAMNMLDIAGGDDvRAPLLNLTSEEKDTvdgLLKKME 287
Cdd:cd00953 241 SANYSLVKIFQGYDAGEP-RPPFYPLDEEEEEK---LRKEVN 278
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
11-286 |
7.30e-31 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 117.22 E-value: 7.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 11 ITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGA---TSMrmeeAL 84
Cdd:PRK03620 16 VTPFDaDGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTagRVPVIAGAgggTAQ----AI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 85 EIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYN--IPVFTgnpflPPLVKRLS-VLDNIIGIKDT 161
Cdd:PRK03620 92 EYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNrdNAVLT-----ADTLARLAeRCPNLVGFKDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 162 SGDMKKFQVIVNLVPEDFSCLIGadhllLP-ALVTGASGAILG----SS---NLVPDIPVGIYRTWERDIDRAVG--LQK 231
Cdd:PRK03620 167 VGDIELMQRIVRALGDRLLYLGG-----LPtAEVFAAAYLALGvptySSavfNFVPEIALAFYRALRAGDHATVDrlLDD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 232 LLMNIVKIMDTGtfpAGlkYAMNM----LDIAGGD--DVRAPLLNLTSEEKDTVDGLLKKM 286
Cdd:PRK03620 242 FFLPYVALRNRK---KG--YAVSIvkagARLVGLDagPVRAPLTDLTPEELAELAALIAKG 297
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
11-285 |
2.87e-29 |
|
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: 112.42 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 11 ITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGA---TSMrmeeAL 84
Cdd:cd00951 9 VTHFDaDGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAgrVPVLAGAgygTAT----AI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 85 EIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNipvfTGNPFLPP-LVKRLS-VLDNIIGIKDTS 162
Cdd:cd00951 85 AYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN----RANAVLTAdSLARLAeRCPNLVGFKDGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 163 GDMKKFQVIVNLVPEDFSCLIGAD------HLLLPALVTGASGAIlgsSNLVPDIPVGIYRTWeRDIDRAVGLQKLLMNI 236
Cdd:cd00951 161 GDIELMRRIVAKLGDRLLYLGGLPtaevfaLAYLAMGVPTYSSAV---FNFVPEIALAFYAAV-RAGDHATVKRLLRDFF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1313375691 237 VKIMDTGTFPAGlkYAMNM----LDIAGGD--DVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:cd00951 237 LPYVDIRNRRKG--YAVSIvkagARLVGRDagPVRPPLTDLTEEELAQLTALIKT 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
1-285 |
5.48e-28 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 108.96 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 1 MKLkGIYCPMITPF-KNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDT--TSLPVIAGATS 77
Cdd:PLN02417 1 KKL-RLITAIKTPYlPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCfgGKIKVIGNTGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 78 MRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSnlsshSTL---PIILYNIPVFTGNPFLPPLVKRLSVLDN 154
Cdd:PLN02417 80 NSTREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFE-----TVLdmgPTIIYNVPGRTGQDIPPEVIFKIAQHPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 155 IIGIKDTSGDMKkfqvIVNLVPEDFSCLIGADHLLLPA-LVTGASGAILGSSNLVPDIpvgiyrtwERDIDRAV---GLQ 230
Cdd:PLN02417 155 FAGVKECTGNDR----VKQYTEKGILLWSGNDDECHDArWDYGADGVISVTSNLVPGL--------MHKLMFAGknkELN 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1313375691 231 KLLMNIVKIMDTGTFPAGLKYAMNMLDIAggDDV-RAPLLNLTSEEKDTVDGLLKK 285
Cdd:PLN02417 223 DKLLPLMDWLFCEPNPIGLNTALAQLGLI--RPVfRLPYVPLDLAKRAEFVALVKA 276
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
3-203 |
1.20e-12 |
|
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA); Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188639 Cd Length: 309 Bit Score: 67.09 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 3 LKGIYCPMITPFKNGG--------IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVI 72
Cdd:cd00952 2 IKGVWAIVPTPSKPDAsdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAgrVPVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 73 AGATSMRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSshSTLP---IILY-NIPVFTGnPFLPPLVKR 148
Cdd:cd00952 82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVA--EAVPemaIAIYaNPEAFKF-DFPRAAWAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1313375691 149 LSVLDNIIGIKDTS------GDMKKFQVIVNLVPEDFSCLIGAdhLLLPALVTGA--SGAILG 203
Cdd:cd00952 159 LAQIPQVVAAKYLGdigallSDLAAVKGRMRLLPLEDDYYAAA--RLFPEEVTAFwsSGAACG 219
|
|
|