|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
5-295 |
9.49e-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: 299.38 E-value: 9.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 5 IEGVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEIS 83
Cdd:COG0329 2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGvDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 84 TRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIK 163
Cdd:COG0329 82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 164 DSDGSDESLKGFLDAVRdiDGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESVTGL 243
Cdd:COG0329 162 EASGDLDRIAELIRATG--DDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447049703 244 RTDLYKVAFsPAAVKKALQLMGHDVGDSRY-AVNFTPEQISEIQQIIRHYNIN 295
Cdd:COG0329 240 IRALFAEGN-PAPVKAALALLGLPSGPVRLpLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-289 |
3.83e-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: 279.43 E-value: 3.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 8 VLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEISTRE 86
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGvDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 87 TIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIKDSD 166
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 167 GSDESLKGFLDAVRdiDGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESVTGLRTD 246
Cdd:cd00408 161 GDLDRLTRLIALLG--PDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447049703 247 LYKVAFsPAAVKKALQLMGHDVGDSRY-AVNFTPEQISEIQQII 289
Cdd:cd00408 239 LFKEGN-PAPVKAALALLGLDAGPVRLpLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-292 |
7.52e-62 |
|
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: 197.17 E-value: 7.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 7 GVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEISTR 85
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGtDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 86 ETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIKDS 165
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 166 DGSdeslkgfLDAVRDI-----DGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESV 240
Cdd:TIGR00674 161 TGN-------LERISEIkaiapDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447049703 241 TGLRTDLYkVAFSPAAVKKALQLMGHDVGDSRYA-VNFTPEQISEIQQIIRHY 292
Cdd:TIGR00674 234 MPLHKALF-IETNPIPVKTALALLGLIEGELRLPlTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-270 |
1.61e-59 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 191.43 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 7 GVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEISTR 85
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGvDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 86 ETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIKDS 165
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIKEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 166 DGSdeslkgfLDAVRDI-----DGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESV 240
Cdd:pfam00701 164 SGD-------LDRMINIkkeagPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKL 236
|
250 260 270
....*....|....*....|....*....|
gi 447049703 241 TGLrTDLYKVAFSPAAVKKALQLMGHDVGD 270
Cdd:pfam00701 237 LPL-IKILFAEPNPIPIKTALELLGLVVGP 265
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
3-295 |
1.37e-48 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 163.24 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 3 KTIEGVLTAIVTPFTATGSLNIPALK--VQVNRQLEAGNAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIG 80
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRrlVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 81 EISTRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNII 160
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 161 GIKDSDGSDESL----KGFLDAVrdidgfnVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEA 236
Cdd:PRK04147 162 GVKQTAGDLYQLerirKAFPDKL-------IYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQEL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 237 QESVTGLRTDLYKVAFSPaAVKKALQLMGHDVGDSRYAVN-FTPEQISEIQQIIRHYNIN 295
Cdd:PRK04147 235 QHECNDVIDLLIKNGVYP-GLKEILHYMGVDAGLCRKPFKpVDEKYLPALKALAAKYLKE 293
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
5-295 |
9.49e-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: 299.38 E-value: 9.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 5 IEGVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEIS 83
Cdd:COG0329 2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGvDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 84 TRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIK 163
Cdd:COG0329 82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 164 DSDGSDESLKGFLDAVRdiDGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESVTGL 243
Cdd:COG0329 162 EASGDLDRIAELIRATG--DDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447049703 244 RTDLYKVAFsPAAVKKALQLMGHDVGDSRY-AVNFTPEQISEIQQIIRHYNIN 295
Cdd:COG0329 240 IRALFAEGN-PAPVKAALALLGLPSGPVRLpLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-289 |
3.83e-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: 279.43 E-value: 3.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 8 VLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEISTRE 86
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGvDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 87 TIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIKDSD 166
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 167 GSDESLKGFLDAVRdiDGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESVTGLRTD 246
Cdd:cd00408 161 GDLDRLTRLIALLG--PDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447049703 247 LYKVAFsPAAVKKALQLMGHDVGDSRY-AVNFTPEQISEIQQII 289
Cdd:cd00408 239 LFKEGN-PAPVKAALALLGLDAGPVRLpLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
5-272 |
9.42e-76 |
|
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: 232.77 E-value: 9.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 5 IEGVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEIS 83
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGtDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 84 TRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIK 163
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 164 DSDGsdeSLKGFLDAVRDI-DGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESVtg 242
Cdd:cd00950 161 EATG---DLDRVSELIALCpDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKL-- 235
|
250 260 270
....*....|....*....|....*....|...
gi 447049703 243 lrTDLYKVAF---SPAAVKKALQLMGHDVGDSR 272
Cdd:cd00950 236 --LPLIKALFaepNPIPVKAALALLGLISGELR 266
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-292 |
7.52e-62 |
|
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: 197.17 E-value: 7.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 7 GVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEISTR 85
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGtDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 86 ETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIKDS 165
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 166 DGSdeslkgfLDAVRDI-----DGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESV 240
Cdd:TIGR00674 161 TGN-------LERISEIkaiapDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447049703 241 TGLRTDLYkVAFSPAAVKKALQLMGHDVGDSRYA-VNFTPEQISEIQQIIRHY 292
Cdd:TIGR00674 234 MPLHKALF-IETNPIPVKTALALLGLIEGELRLPlTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-270 |
1.61e-59 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 191.43 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 7 GVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEISTR 85
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGvDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 86 ETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNIIGIKDS 165
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIKEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 166 DGSdeslkgfLDAVRDI-----DGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESV 240
Cdd:pfam00701 164 SGD-------LDRMINIkkeagPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKL 236
|
250 260 270
....*....|....*....|....*....|
gi 447049703 241 TGLrTDLYKVAFSPAAVKKALQLMGHDVGD 270
Cdd:pfam00701 237 LPL-IKILFAEPNPIPIKTALELLGLVVGP 265
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
6-289 |
7.27e-54 |
|
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: 176.73 E-value: 7.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 6 EGVLTAIVTPFTATGSLNIPALKVQVNRQLEAGN--AIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEIS 83
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGvdGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 84 TRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIAD-TLSIPMFLYNIPARTGNTIQPETARALASHPNIIGI 162
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAaAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 163 KDSDGSDESLKGFLDAVRdiDGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEAQESVTG 242
Cdd:cd00954 162 KFTATDLYDLERIRAASP--EDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVIND 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447049703 243 LRTDLYKVAFSPAAvKKALQLMGHDVGDSRYAVN-FTPEQISEIQQII 289
Cdd:cd00954 240 VITVLIKNGLYPTL-KAILRLMGLDAGPCRLPLRkVTEKALAKAKELA 286
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
3-295 |
1.37e-48 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 163.24 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 3 KTIEGVLTAIVTPFTATGSLNIPALK--VQVNRQLEAGNAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIG 80
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRrlVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 81 EISTRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNIPARTGNTIQPETARALASHPNII 160
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 161 GIKDSDGSDESL----KGFLDAVrdidgfnVLNGPDSLIHKGFVEGCSACISGLANVAPREINAIWSRFHAGDIEGSYEA 236
Cdd:PRK04147 162 GVKQTAGDLYQLerirKAFPDKL-------IYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQEL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 237 QESVTGLRTDLYKVAFSPaAVKKALQLMGHDVGDSRYAVN-FTPEQISEIQQIIRHYNIN 295
Cdd:PRK04147 235 QHECNDVIDLLIKNGVYP-GLKEILHYMGVDAGLCRKPFKpVDEKYLPALKALAAKYLKE 293
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
7-219 |
3.58e-44 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 151.72 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 7 GVLTAIVTPFTATGSLNIPALKVQVNRQLEAGNAIFC-GGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEISTR 85
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIvGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 86 ETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLsiPMFLYNIPARTGNTIQPETARALASHPNIIGIKDS 165
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447049703 166 DGsDESLKGFLDavrdiDGFNVLNGPDSLIHKGFVE-GCSACISGLANVAPREIN 219
Cdd:PLN02417 162 TG-NDRVKQYTE-----KGILLWSGNDDECHDARWDyGADGVISVTSNLVPGLMH 210
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
6-290 |
9.12e-33 |
|
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: 122.05 E-value: 9.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 6 EGVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIF-CGGTnGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEiS 83
Cdd:cd00951 2 SGLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGaAALFaAGGT-GEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 84 TRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNipaRTGNTIQPETARALASH-PNIIGI 162
Cdd:cd00951 80 TATAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAERcPNLVGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 163 KDSDGSdeslkgfLDAVRDI-----DGFNVLNG-PdslIHKGFVE-----GCSACISGLANVAPREINAIWSRFHAGDie 231
Cdd:cd00951 157 KDGVGD-------IELMRRIvaklgDRLLYLGGlP---TAEVFALaylamGVPTYSSAVFNFVPEIALAFYAAVRAGD-- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447049703 232 gsyeaQESVTGLRTDLY---------KVAFSPAAVKKALQLMGHDVGDSRYAV-NFTPEQISEIQQIIR 290
Cdd:cd00951 225 -----HATVKRLLRDFFlpyvdirnrRKGYAVSIVKAGARLVGRDAGPVRPPLtDLTEEELAQLTALIK 288
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
6-291 |
1.58e-32 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 121.46 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 6 EGVLTAIVTPFTATGSLNIPALKVQVNRQLEAG-NAIF-CGGTnGEFFVLNEQEKLSVTQTCVDEVAGRAPVVAHIGEiS 83
Cdd:PRK03620 9 SGLLSFPVTPFDADGSFDEAAYREHLEWLAPYGaAALFaAGGT-GEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 84 TRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTLSIPMFLYNipaRTGNTIQPETARALAS-HPNIIGI 162
Cdd:PRK03620 87 TAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAErCPNLVGF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 163 KDSDGSDESLKGFLDAVRdiDGFNVLNG-PdslIHKGFVE-----GCSACISGLANVAPREINAIWSRFHAGDiegsyea 236
Cdd:PRK03620 164 KDGVGDIELMQRIVRALG--DRLLYLGGlP---TAEVFAAaylalGVPTYSSAVFNFVPEIALAFYRALRAGD------- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447049703 237 QESVTGLRTDLY---------KVAFSPAAVKKALQLMGHDVGDSRYA-VNFTPEQISEIQQIIRH 291
Cdd:PRK03620 232 HATVDRLLDDFFlpyvalrnrKKGYAVSIVKAGARLVGLDAGPVRAPlTDLTPEELAELAALIAK 296
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
1-221 |
8.52e-25 |
|
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: 100.53 E-value: 8.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 1 MPKTIegvlTAIVTPFTAtGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDeVAGRapVVAHI 79
Cdd:cd00953 1 MPDKI----TPVITPFTG-NKIDKEKFKKHCENLISKGiDYVFVAGTTGLGPSLSFQEKLELLKAYSD-ITDK--VIFQV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 80 GEISTRETIRLGQQIEKLGVDAVSVIAPYFVP-LKQEELIAHYSAIADtlSIPMFLYNIPARTGNTIQPETARAL-ASHP 157
Cdd:cd00953 73 GSLNLEESIELARAAKSFGIYAIASLPPYYFPgIPEEWLIKYFTDISS--PYPTFIYNYPKATGYDINARMAKEIkKAGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447049703 158 NIIGIKDSDgsdESLKGFLDAVRDIDGFNVLNGPDSLIHKGFVEGCSACISGLANVAPREINAI 221
Cdd:cd00953 151 DIIGVKDTN---EDISHMLEYKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKI 211
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
5-181 |
1.12e-16 |
|
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: 78.64 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 5 IEGVLTAIVTPFT-------ATGSLNIPALKVQVNRQLEAG-NAIFCGGTNGEFFVLNEQEKLSVTQTCVDEVAGRAPVV 76
Cdd:cd00952 2 IKGVWAIVPTPSKpdasdwrATDTVDLDETARLVERLIAAGvDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049703 77 AHIGEISTRETIRLGQQIEKLGVDAVSVIAPYFVPLKQEELIAHYSAIADTL-SIPMFLYNIPARTGNTIQPETARALAS 155
Cdd:cd00952 82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELAQ 161
|
170 180
....*....|....*....|....*.
gi 447049703 156 HPNIIGIKDSdGSDESLKGFLDAVRD 181
Cdd:cd00952 162 IPQVVAAKYL-GDIGALLSDLAAVKG 186
|
|
| |
