|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
3-286 |
1.78e-167 |
|
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: 465.43 E-value: 1.78e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 3 FQGAFTALVTPFRN-GAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNN 81
Cdd:cd00950 1 FGGSITALVTPFKDdGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 82 TREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKRDiPEVIGI 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEH-PNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 162 KEATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASIN 241
Cdd:cd00950 160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 347519967 242 RAMFLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDIL 286
Cdd:cd00950 240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
2-292 |
3.78e-150 |
|
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: 421.87 E-value: 3.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 2 QFQGAFTALVTPFR-NGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSN 80
Cdd:COG0329 1 KFRGVIPALVTPFDaDGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 81 NTREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKrDIPEVIG 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 161 IKEATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASI 240
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 347519967 241 NRAMFLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDILSAAGIV 292
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-287 |
1.16e-137 |
|
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: 390.15 E-value: 1.16e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 5 GAFTALVTPFR-NGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNNTR 83
Cdd:TIGR00674 1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 84 EAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKRdIPEVIGIKE 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAE-EPNIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 164 ATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASINRA 243
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 347519967 244 MFLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDILS 287
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLK 283
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-289 |
2.98e-119 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 343.58 E-value: 2.98e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 3 FQGAFTALVTPF-RNGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNN 81
Cdd:pfam00701 2 FSGIITALVTPFdTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 82 TREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKRdIPEVIGI 161
Cdd:pfam00701 82 TSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 162 KEATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASIN 241
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 347519967 242 RAMFLETNPIPVKTALSMMG-KMELELRLPMVPLQPANQSRLRDILSAA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGlVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
4-290 |
9.14e-80 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 243.01 E-value: 9.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 4 QGAFTALVTPF-RNGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNNT 82
Cdd:PLN02417 3 LRLITAIKTPYlPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 83 REAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAaevPM-PFIVYNVPSRTGTNLCPETLARMKRDiPEVIGI 161
Cdd:PLN02417 83 REAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVL---DMgPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 162 KEATGNliqvSEIIEYCGADFQVLSGDDFTVLP-LLAVGGCGVISVSSNVVPAKMAELcraFFEGdlatarrvhyEIASI 240
Cdd:PLN02417 159 KECTGN----DRVKQYTEKGILLWSGNDDECHDaRWDYGADGVISVTSNLVPGLMHKL---MFAG----------KNKEL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 347519967 241 NRAM-------FLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDILSAAG 290
Cdd:PLN02417 222 NDKLlplmdwlFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIG 278
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
3-286 |
1.78e-167 |
|
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: 465.43 E-value: 1.78e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 3 FQGAFTALVTPFRN-GAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNN 81
Cdd:cd00950 1 FGGSITALVTPFKDdGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 82 TREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKRDiPEVIGI 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEH-PNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 162 KEATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASIN 241
Cdd:cd00950 160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 347519967 242 RAMFLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDIL 286
Cdd:cd00950 240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
2-292 |
3.78e-150 |
|
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: 421.87 E-value: 3.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 2 QFQGAFTALVTPFR-NGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSN 80
Cdd:COG0329 1 KFRGVIPALVTPFDaDGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 81 NTREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKrDIPEVIG 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 161 IKEATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASI 240
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 347519967 241 NRAMFLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDILSAAGIV 292
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-287 |
1.16e-137 |
|
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: 390.15 E-value: 1.16e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 5 GAFTALVTPFR-NGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNNTR 83
Cdd:TIGR00674 1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 84 EAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKRdIPEVIGIKE 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAE-EPNIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 164 ATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASINRA 243
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 347519967 244 MFLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDILS 287
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLK 283
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
7-286 |
4.78e-131 |
|
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: 373.04 E-value: 4.78e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 7 FTALVTPFR-NGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNNTREA 85
Cdd:cd00408 2 IPALVTPFTaDGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 86 VELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMkRDIPEVIGIKEAT 165
Cdd:cd00408 82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARL-AEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 166 GNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASINRAMF 245
Cdd:cd00408 161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 347519967 246 LETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDIL 286
Cdd:cd00408 241 KEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-289 |
2.98e-119 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 343.58 E-value: 2.98e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 3 FQGAFTALVTPF-RNGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNN 81
Cdd:pfam00701 2 FSGIITALVTPFdTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 82 TREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMKRdIPEVIGI 161
Cdd:pfam00701 82 TSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 162 KEATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASIN 241
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 347519967 242 RAMFLETNPIPVKTALSMMG-KMELELRLPMVPLQPANQSRLRDILSAA 289
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGlVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
4-290 |
9.14e-80 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 243.01 E-value: 9.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 4 QGAFTALVTPF-RNGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNNT 82
Cdd:PLN02417 3 LRLITAIKTPYlPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 83 REAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAaevPM-PFIVYNVPSRTGTNLCPETLARMKRDiPEVIGI 161
Cdd:PLN02417 83 REAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVL---DMgPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 162 KEATGNliqvSEIIEYCGADFQVLSGDDFTVLP-LLAVGGCGVISVSSNVVPAKMAELcraFFEGdlatarrvhyEIASI 240
Cdd:PLN02417 159 KECTGN----DRVKQYTEKGILLWSGNDDECHDaRWDYGADGVISVTSNLVPGLMHKL---MFAG----------KNKEL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 347519967 241 NRAM-------FLETNPIPVKTALSMMGKMELELRLPMVPLQPANQSRLRDILSAAG 290
Cdd:PLN02417 222 NDKLlplmdwlFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIG 278
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
4-285 |
9.75e-61 |
|
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: 194.45 E-value: 9.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 4 QGAFTALVTPF-RNGAVDEERYRAFIEWQIE-QGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSNN 81
Cdd:cd00954 2 KGLIAALLTPFdENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 82 TREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVP-MPFIVYNVPSRTGTNLCPETLARMkRDIPEVIG 160
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAAsLPMIIYHIPALTGVNLTLEQFLEL-FEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 161 IKEATGNLIQVSEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASI 240
Cdd:cd00954 161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 347519967 241 NRAMfLETNPIPV-KTALSMMGKMELELRLPMVPLQPANQSRLRDI 285
Cdd:cd00954 241 ITVL-IKNGLYPTlKAILRLMGLDAGPCRLPLRKVTEKALAKAKEL 285
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
11-292 |
4.21e-50 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 167.30 E-value: 4.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 11 VTPF-RNGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSnNTREAVELT 89
Cdd:PRK03620 16 VTPFdADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 90 RYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNvpsRTGTNLCPETLARMKRDIPEVIGIKEATGNLI 169
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAERCPNLVGFKDGVGDIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 170 QVSEIIEYCGADFQVLSG---DDFTVLPLLAVggcGVISVSS---NVVPakmaELCRAFFE----GDLATARRvhyeias 239
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGGlptAEVFAAAYLAL---GVPTYSSavfNFVP----EIALAFYRalraGDHATVDR------- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347519967 240 INRAMFLETNPIP----------VKTALSMMGKMELELRLPMVPLQPANQSRLRDILSAAGIV 292
Cdd:PRK03620 238 LLDDFFLPYVALRnrkkgyavsiVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGGAQ 300
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
11-286 |
1.30e-49 |
|
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: 165.96 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 11 VTPFR-NGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAGSnNTREAVELT 89
Cdd:cd00951 9 VTHFDaDGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 90 RYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNvpsRTGTNLCPETLARMKRDIPEVIGIKEATGNLI 169
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAERCPNLVGFKDGVGDIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 170 QVSEIIEYCGADFQVLSG---DDFTVLPLLAVggcGVISVSS---NVVPAKMAELCRAFFEGDLATARRvhyeiasINRA 243
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGGlptAEVFALAYLAM---GVPTYSSavfNFVPEIALAFYAAVRAGDHATVKR-------LLRD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 347519967 244 MFLETNPIP----------VKTALSMMGKMELELRLPMVPLQPANQSRLRDIL 286
Cdd:cd00951 235 FFLPYVDIRnrrkgyavsiVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALI 287
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-285 |
7.71e-48 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 161.31 E-value: 7.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 1 MQFQGAFTALVTPF-RNGAVDEERYRAFIEWQIE-QGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAGAG 78
Cdd:PRK04147 2 KNLKGVYAALLTPFdEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 79 SNNTREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVPMPFIVYNVPSRTGTNLCPETLARMkRDIPEV 158
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNEL-FTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 159 IGIKEATGNLIQVsEIIEYCGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEia 238
Cdd:PRK04147 161 IGVKQTAGDLYQL-ERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHE-- 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 347519967 239 sINRAM--FLETNPIP-VKTALSMMGKMELELRLPMVPLQPANQSRLRDI 285
Cdd:PRK04147 238 -CNDVIdlLIKNGVYPgLKEILHYMGVDAGLCRKPFKPVDEKYLPALKAL 286
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
5-249 |
2.22e-27 |
|
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: 107.92 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 5 GAFTALVTPFRNGA--------VDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICVEQVKGRVPVLAG 76
Cdd:cd00952 4 GVWAIVPTPSKPDAsdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 77 AGSNNTREAVELTRYAKQAGADGALLITPYYNKPTQEGLYQHFKAIAAEVP-MPFIVYNVPSRTGTNLCPETLARMKRdI 155
Cdd:cd00952 84 ATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVPeMAIAIYANPEAFKFDFPRAAWAELAQ-I 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 156 PEVIGIKE--ATGNLIQvseiieycgaDFQVLSGdDFTVLPL------LAVGGCGVISV--SSNVV--PAKMAELCRAFF 223
Cdd:cd00952 163 PQVVAAKYlgDIGALLS----------DLAAVKG-RMRLLPLeddyyaAARLFPEEVTAfwSSGAAcgPAPVTALRDAVA 231
|
250 260
....*....|....*....|....*.
gi 347519967 224 EGDLATARRVHYEIASINRAMFLETN 249
Cdd:cd00952 232 TGDWTDARALTDRMRWAAEPLFPRGD 257
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
8-242 |
1.50e-26 |
|
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: 105.16 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 8 TALVTPFRNGAVDEERYRAFIEWQIEQGINGLVPCGTTGESATLTHQEHKDVIRICvEQVKGRvpVLAGAGSNNTREAVE 87
Cdd:cd00953 6 TPVITPFTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAY-SDITDK--VIFQVGSLNLEESIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519967 88 LTRYAKQAGADGALLITPYY-NKPTQEGLYQHFKAIAAevPMPFIVYNVPSRTGTNLCPETLARMKRDIPEVIGIKEATG 166
Cdd:cd00953 83 LARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISS--PYPTFIYNYPKATGYDINARMAKEIKKAGGDIIGVKDTNE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347519967 167 NLiqvSEIIEY--CGADFQVLSGDDFTVLPLLAVGGCGVISVSSNVVPAKMAELCRAFFEGDLATARRVHYEIASINR 242
Cdd:cd00953 161 DI---SHMLEYkrLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIEDAFKLQFLINEVLDASR 235
|
|
| |
