|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
82-361 |
0e+00 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 595.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 82 TSLRLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSN 161
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 162 STREAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVLPMGPTIIYNVPSRSAQDISPEVIVAISGYTNMAGVKE 241
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 242 CVGHERIQQYADKGITIWSGNDDECHDSRWKYGATGVISVTSNLVPGLMHSLMYKGENAMLNEKLLPLMKWLFCQPNPIA 321
Cdd:PLN02417 161 CTGNDRVKQYTEKGILLWSGNDDECHDARWDYGADGVISVTSNLVPGLMHKLMFAGKNKELNDKLLPLMDWLFCEPNPIG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 242093822 322 VNTALAQLGVARPVFRLPYVPLPLEKRIEFVRIVEAIGRE 361
Cdd:PLN02417 241 LNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
83-358 |
9.17e-126 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 363.61 E-value: 9.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 83 SLRLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNS 162
Cdd:pfam00701 2 FSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 163 TREAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVLPMG--PTIIYNVPSRSAQDISPEVIVAISGYTNMAGVK 240
Cdd:pfam00701 82 TSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATdlPMILYNVPSRTGVDLTPETVGRLATNPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 241 ECVG----HERIQQYADKGITIWSGnDDECHDSRWKYGATGVISVTSNLVPGLMHSLMYKGEN------AMLNEKLLPLM 310
Cdd:pfam00701 162 EASGdldrMINIKKEAGPDFVILSG-DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNgdlataALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 242093822 311 KWLFCQPNPIAVNTALAQLGV-ARPVFRLPYVPLPLEKRIEFVRIVEAI 358
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLvVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
85-355 |
5.00e-122 |
|
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: 354.11 E-value: 5.00e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 85 RLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTR 164
Cdd:cd00950 3 GSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 165 EAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVL--PMGPTIIYNVPSRSAQDISPEVIVAISGYTNMAGVKEC 242
Cdd:cd00950 83 EAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAeaTDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIKEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 243 VG-HERIQQY---ADKGITIWSGnDDECHDSRWKYGATGVISVTSNLVPGLMHSLMYKGEN------AMLNEKLLPLMKW 312
Cdd:cd00950 163 TGdLDRVSELialCPDDFAVLSG-DDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAgdlekaRELHRKLLPLIKA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 242093822 313 LFCQPNPIAVNTALAQLGVARPVFRLPYVPLPLEKRIEFVRIV 355
Cdd:cd00950 242 LFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
85-359 |
3.11e-79 |
|
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: 245.06 E-value: 3.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 85 RLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTR 164
Cdd:COG0329 4 GVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 165 EAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAV-----LPMgptIIYNVPSRSAQDISPEVIVAISGYTNMAGV 239
Cdd:COG0329 84 EAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIaeavdLPI---ILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 240 KECVG-HERIQQY---ADKGITIWSGNDDECHDSRwKYGATGVISVTSNLVPGLMHSL---MYKG--ENAM-LNEKLLPL 309
Cdd:COG0329 161 KEASGdLDRIAELiraTGDDFAVLSGDDALALPAL-ALGADGVISVTANVAPELMVALyeaALAGdlAEARaLQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 242093822 310 MKWLFCQPNPIAVNTALAQLGVARPVFRLPYVPLPLEKRIEFVRIVEAIG 359
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
86-348 |
1.12e-71 |
|
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: 225.67 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 86 LITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTRE 165
Cdd:TIGR00674 2 VITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 166 AVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVLPMG--PTIIYNVPSRSAQDISPEVIVAISGYTNMAGVKECV 243
Cdd:TIGR00674 82 AISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVdlPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 244 GH-ERIQQY---ADKGITIWSGNDDECHDSRwKYGATGVISVTSNLVPGLMHSLM---YKG---ENAMLNEKLLPLMKWL 313
Cdd:TIGR00674 162 GNlERISEIkaiAPDDFVVLSGDDALTLPMM-ALGGKGVISVTANVAPKLMKEMVnnaLEGdfaEAREIHQKLMPLHKAL 240
|
250 260 270
....*....|....*....|....*....|....*
gi 242093822 314 FCQPNPIAVNTALAQLGVARPVFRLPYVPLPLEKR 348
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHR 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
82-361 |
0e+00 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 595.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 82 TSLRLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSN 161
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 162 STREAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVLPMGPTIIYNVPSRSAQDISPEVIVAISGYTNMAGVKE 241
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 242 CVGHERIQQYADKGITIWSGNDDECHDSRWKYGATGVISVTSNLVPGLMHSLMYKGENAMLNEKLLPLMKWLFCQPNPIA 321
Cdd:PLN02417 161 CTGNDRVKQYTEKGILLWSGNDDECHDARWDYGADGVISVTSNLVPGLMHKLMFAGKNKELNDKLLPLMDWLFCEPNPIG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 242093822 322 VNTALAQLGVARPVFRLPYVPLPLEKRIEFVRIVEAIGRE 361
Cdd:PLN02417 241 LNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
83-358 |
9.17e-126 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 363.61 E-value: 9.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 83 SLRLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNS 162
Cdd:pfam00701 2 FSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 163 TREAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVLPMG--PTIIYNVPSRSAQDISPEVIVAISGYTNMAGVK 240
Cdd:pfam00701 82 TSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATdlPMILYNVPSRTGVDLTPETVGRLATNPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 241 ECVG----HERIQQYADKGITIWSGnDDECHDSRWKYGATGVISVTSNLVPGLMHSLMYKGEN------AMLNEKLLPLM 310
Cdd:pfam00701 162 EASGdldrMINIKKEAGPDFVILSG-DDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNgdlataALINHKLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 242093822 311 KWLFCQPNPIAVNTALAQLGV-ARPVFRLPYVPLPLEKRIEFVRIVEAI 358
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLvVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
85-355 |
5.00e-122 |
|
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: 354.11 E-value: 5.00e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 85 RLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTR 164
Cdd:cd00950 3 GSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 165 EAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVL--PMGPTIIYNVPSRSAQDISPEVIVAISGYTNMAGVKEC 242
Cdd:cd00950 83 EAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAeaTDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIKEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 243 VG-HERIQQY---ADKGITIWSGnDDECHDSRWKYGATGVISVTSNLVPGLMHSLMYKGEN------AMLNEKLLPLMKW 312
Cdd:cd00950 163 TGdLDRVSELialCPDDFAVLSG-DDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAgdlekaRELHRKLLPLIKA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 242093822 313 LFCQPNPIAVNTALAQLGVARPVFRLPYVPLPLEKRIEFVRIV 355
Cdd:cd00950 242 LFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
86-355 |
5.05e-85 |
|
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: 259.79 E-value: 5.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 86 LITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTRE 165
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 166 AVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVL--PMGPTIIYNVPSRSAQDISPEVIVAISGYTNMAGVKECV 243
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVAdaSDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 244 G----HERIQQYADKGITIWSGnDDECHDSRWKYGATGVISVTSNLVPGLMHSLMYKGEN------AMLNEKLLPLMKWL 313
Cdd:cd00408 161 GdldrLTRLIALLGPDFAVLSG-DDDLLLPALALGADGAISGAANVAPKLAVALYEAARAgdleeaRALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 242093822 314 FCQPNPIAVNTALAQLGVARPVFRLPYVPLPLEKRIEFVRIV 355
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
85-359 |
3.11e-79 |
|
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: 245.06 E-value: 3.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 85 RLITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTR 164
Cdd:COG0329 4 GVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 165 EAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAV-----LPMgptIIYNVPSRSAQDISPEVIVAISGYTNMAGV 239
Cdd:COG0329 84 EAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIaeavdLPI---ILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 240 KECVG-HERIQQY---ADKGITIWSGNDDECHDSRwKYGATGVISVTSNLVPGLMHSL---MYKG--ENAM-LNEKLLPL 309
Cdd:COG0329 161 KEASGdLDRIAELiraTGDDFAVLSGDDALALPAL-ALGADGVISVTANVAPELMVALyeaALAGdlAEARaLQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 242093822 310 MKWLFCQPNPIAVNTALAQLGVARPVFRLPYVPLPLEKRIEFVRIVEAIG 359
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
86-348 |
1.12e-71 |
|
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: 225.67 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 86 LITAVKTPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTRE 165
Cdd:TIGR00674 2 VITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 166 AVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAVLPMG--PTIIYNVPSRSAQDISPEVIVAISGYTNMAGVKECV 243
Cdd:TIGR00674 82 AISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVdlPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 244 GH-ERIQQY---ADKGITIWSGNDDECHDSRwKYGATGVISVTSNLVPGLMHSLM---YKG---ENAMLNEKLLPLMKWL 313
Cdd:TIGR00674 162 GNlERISEIkaiAPDDFVVLSGDDALTLPMM-ALGGKGVISVTANVAPKLMKEMVnnaLEGdfaEAREIHQKLMPLHKAL 240
|
250 260 270
....*....|....*....|....*....|....*
gi 242093822 314 FCQPNPIAVNTALAQLGVARPVFRLPYVPLPLEKR 348
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHR 275
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
86-285 |
2.72e-18 |
|
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: 84.28 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 86 LITAVKTPYLPDGRFDLEAYDSLINMQIE-GGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNSTR 164
Cdd:cd00954 4 LIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLNLK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 165 EAV----HATEQGFavgmHAALHINPYYGKTSTEGMISHFEAV------LPMgptIIYNVPSRSAQDISPEVIVAISGYT 234
Cdd:cd00954 84 ESQelakHAEELGY----DAISAITPFYYKFSFEEIKDYYREIiaaaasLPM---IIYHIPALTGVNLTLEQFLELFEIP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 242093822 235 NMAGVKECVGH----ERIQQYADKGITIWSGNDDECHDSRwKYGATGVISVTSNL 285
Cdd:cd00954 157 NVIGVKFTATDlydlERIRAASPEDKLVLNGFDEMLLSAL-ALGADGAIGSTYNV 210
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
86-285 |
4.66e-18 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 83.50 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 86 LITAVKTPYLPDGRFDLEAYDSLINMQIEG-GAEGVIVGGTTGEGHLMSWDE--HIMLIGHTVNcfGSRIKVIGNTGSNS 162
Cdd:PRK04147 7 VYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEkkQVLEIVAEEA--KGKVKLIAQVGSVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 163 TREAV----HATEQGFavgmHAALHINPYYGKTSTEGMISHFEAVLPM--GPTIIYNVPSRSAQDISPEVIVAISGYTNM 236
Cdd:PRK04147 85 TAEAQelakYATELGY----DAISAVTPFYYPFSFEEICDYYREIIDSadNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 242093822 237 AGVKECVGH----ERIQQ-YADKgiTIWSGNDDECHdSRWKYGATGVISVTSNL 285
Cdd:PRK04147 161 IGVKQTAGDlyqlERIRKaFPDK--LIYNGFDEMFA-SGLLAGADGAIGSTYNV 211
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
92-244 |
2.18e-11 |
|
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: 63.88 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 92 TPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNsTREAVHATE 171
Cdd:cd00951 10 THFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYAQ 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242093822 172 QGFAVGMHAALHINPYYGKTSTEGMISHFEAVLPMG--PTIIYNvpsRSAQDISPEVIVAIS-GYTNMAGVKECVG 244
Cdd:cd00951 89 AAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTdlGVIVYN---RANAVLTADSLARLAeRCPNLVGFKDGVG 161
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
92-244 |
3.67e-09 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 57.52 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 92 TPYLPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRIKVIGNTGSNsTREAVHATE 171
Cdd:PRK03620 17 TPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG-TAQAIEYAQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242093822 172 QGFAVGMHAALHINPYYGKTSTEGMISHFEAV-----LpmgPTIIYNvpsRSAQDISPEVIVAISG-YTNMAGVKECVG 244
Cdd:PRK03620 96 AAERAGADGILLLPPYLTEAPQEGLAAHVEAVckstdL---GVIVYN---RDNAVLTADTLARLAErCPNLVGFKDGVG 168
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
83-243 |
2.26e-08 |
|
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: 54.70 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 83 SLRLITAVKTPYlPDGRFDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIgHTVNCFGSriKVIGNTGSNS 162
Cdd:cd00953 1 MPDKITPVITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELL-KAYSDITD--KVIFQVGSLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 163 TREAVHATEQGFAVGMHAALHINPYY-GKTSTEGMISHFEAVLPMGPTIIYNVPSRSAQDISPEVIVAI-SGYTNMAGVK 240
Cdd:cd00953 77 LEESIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISSPYPTFIYNYPKATGYDINARMAKEIkKAGGDIIGVK 156
|
...
gi 242093822 241 ECV 243
Cdd:cd00953 157 DTN 159
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
80-240 |
5.51e-08 |
|
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: 53.99 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 80 DITSLRLItaVKTPYLPDGR-------FDLEAYDSLINMQIEGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGSRI 152
Cdd:cd00952 1 DIKGVWAI--VPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242093822 153 KVIGNTGSNSTREAVHATEQGFAVGMHAALHINPYYGKTSTEGMISHFEAV---LPMGPTIIYNVPSRSAQDISPEVIVA 229
Cdd:cd00952 79 PVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVaeaVPEMAIAIYANPEAFKFDFPRAAWAE 158
|
170
....*....|.
gi 242093822 230 ISGYTNMAGVK 240
Cdd:cd00952 159 LAQIPQVVAAK 169
|
|
| |
