|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-292 |
4.58e-73 |
|
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: 226.19 E-value: 4.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 1 MFTGLSAFPLTPLV-NGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAV-QAAGDIPVITSIGAL 78
Cdd:COG0329 1 KFRGVIPALVTPFDaDGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVeAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 79 RLEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNVGSV 158
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 159 KrsPSGTTLAQMREEIAALRRDIpatvTIGASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALSGDEARTAALNA 238
Cdd:COG0329 161 K--EASGDLDRIAELIRATGDDF----AVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1358831916 239 AFEPLWALFRHHGGLRVIAAAAELTGRVAAPCLPePLQSLQGDARAQLQRVLAA 292
Cdd:COG0329 235 RLLPLIRALFAEGNPAPVKAALALLGLPSGPVRL-PLLPLSEEERAELRAALKE 287
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
5-290 |
3.21e-60 |
|
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: 193.15 E-value: 3.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 5 LSAFPLTPL-VNGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQAA-GDIPVITSIGALRLEE 82
Cdd:cd00408 1 VIPALVTPFtADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVaGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 83 MLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNVGSVKRsp 162
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKD-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 163 SGTTLAQMREEIAALRRDIpatvTIGASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALSGDEARTAALNAAFEP 242
Cdd:cd00408 159 SSGDLDRLTRLIALLGPDF----AVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1358831916 243 LWALFRHHGGLRVIAAAAELTGRVAAPCLPePLQSLQGDARAQLQRVL 290
Cdd:cd00408 235 LIEALFKEGNPAPVKAALALLGLDAGPVRL-PLVPLSEEERAKLEALL 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-292 |
3.91e-41 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 144.05 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 1 MFTGLSAFPLTPLVN-GQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQAAGD-IPVITSIGAL 78
Cdd:pfam00701 1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGrIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 79 RLEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNVGSV 158
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 159 KRSpSGTTlaqmrEEIAALRRDIPATVTIGASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALSGDEARTAALNA 238
Cdd:pfam00701 161 KEA-SGDL-----DRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINH 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1358831916 239 AFEPLWALFRHHGGLRVIAAAAELTGRVAAPCLPEPLQSLQGDARAQLQRVLAA 292
Cdd:pfam00701 235 KLLPLIKILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKA 288
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
1-292 |
2.67e-18 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 82.94 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 1 MFTGLSAFPLTPL-VNGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQA-AGDIPVITSIGAl 78
Cdd:PRK03620 7 LGSGLLSFPVTPFdADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETtAGRVPVIAGAGG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 79 RLEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYdNPATTgfTFTPELLQAVA-RLPNVGS 157
Cdd:PRK03620 86 GTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVY-NRDNA--VLTADTLARLAeRCPNLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 158 VKrspSGT-TLAQMREEIAALRRDI-------PATVTIGASadpKAIsallaGADTWYSVVAGLWPHDSRALAQAALSGD 229
Cdd:PRK03620 163 FK---DGVgDIELMQRIVRALGDRLlylgglpTAEVFAAAY---LAL-----GVPTYSSAVFNFVPEIALAFYRALRAGD 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358831916 230 EARTAA-LNAAFEPLWALFRHHGGLRV--IAAAAELTGRVAAPCLPePLQSLQGDARAQLQRVLAA 292
Cdd:PRK03620 232 HATVDRlLDDFFLPYVALRNRKKGYAVsiVKAGARLVGLDAGPVRA-PLTDLTPEELAELAALIAK 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
1-292 |
4.58e-73 |
|
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: 226.19 E-value: 4.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 1 MFTGLSAFPLTPLV-NGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAV-QAAGDIPVITSIGAL 78
Cdd:COG0329 1 KFRGVIPALVTPFDaDGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVeAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 79 RLEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNVGSV 158
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 159 KrsPSGTTLAQMREEIAALRRDIpatvTIGASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALSGDEARTAALNA 238
Cdd:COG0329 161 K--EASGDLDRIAELIRATGDDF----AVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1358831916 239 AFEPLWALFRHHGGLRVIAAAAELTGRVAAPCLPePLQSLQGDARAQLQRVLAA 292
Cdd:COG0329 235 RLLPLIRALFAEGNPAPVKAALALLGLPSGPVRL-PLLPLSEEERAELRAALKE 287
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
5-290 |
3.21e-60 |
|
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: 193.15 E-value: 3.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 5 LSAFPLTPL-VNGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQAA-GDIPVITSIGALRLEE 82
Cdd:cd00408 1 VIPALVTPFtADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVaGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 83 MLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNVGSVKRsp 162
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKD-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 163 SGTTLAQMREEIAALRRDIpatvTIGASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALSGDEARTAALNAAFEP 242
Cdd:cd00408 159 SSGDLDRLTRLIALLGPDF----AVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1358831916 243 LWALFRHHGGLRVIAAAAELTGRVAAPCLPePLQSLQGDARAQLQRVL 290
Cdd:cd00408 235 LIEALFKEGNPAPVKAALALLGLDAGPVRL-PLVPLSEEERAKLEALL 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
1-292 |
3.91e-41 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 144.05 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 1 MFTGLSAFPLTPLVN-GQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQAAGD-IPVITSIGAL 78
Cdd:pfam00701 1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGrIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 79 RLEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNVGSV 158
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 159 KRSpSGTTlaqmrEEIAALRRDIPATVTIGASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALSGDEARTAALNA 238
Cdd:pfam00701 161 KEA-SGDL-----DRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINH 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1358831916 239 AFEPLWALFRHHGGLRVIAAAAELTGRVAAPCLPEPLQSLQGDARAQLQRVLAA 292
Cdd:pfam00701 235 KLLPLIKILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKA 288
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
2-290 |
1.15e-33 |
|
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: 124.14 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 2 FTGLsafpLTPLV-----NGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQAAGD-IPVITSI 75
Cdd:cd00950 1 FGGS----ITALVtpfkdDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGrVPVIAGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 76 GALRLEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNV 155
Cdd:cd00950 77 GSNNTAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 156 GSVKRSpSGTtlaqmREEIAALRRDIPATVTIGASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALSGDEARTAA 235
Cdd:cd00950 157 VGIKEA-TGD-----LDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1358831916 236 LNAAFEPLW-ALFRHHGGLRVIAAAAELtGRVAAPCLPePLQSLQGDARAQLQRVL 290
Cdd:cd00950 231 LHRKLLPLIkALFAEPNPIPVKAALALL-GLISGELRL-PLVPLSEELRAKLRAAL 284
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
2-292 |
1.27e-19 |
|
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: 86.61 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 2 FTGLSAFPLTPL-VNGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQ-AAGDIPVITSIGAlR 79
Cdd:cd00951 1 GSGLLSFPVTHFdADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEeTAGRVPVLAGAGY-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 80 LEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIY--DNPAttgftFTPELLQAVA-RLPNVG 156
Cdd:cd00951 80 TATAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYnrANAV-----LTADSLARLAeRCPNLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 157 SVKrspSGTTlaqmreEIAALRRdipATVTIG---------ASADPKAISALLAGADTWYSVVAGLWPHDSRALAQAALS 227
Cdd:cd00951 155 GFK---DGVG------DIELMRR---IVAKLGdrllylgglPTAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358831916 228 GDEARTAA-LNAAFEPLWALFRHHGGLRV--IAAAAELTGRVAAPCLPePLQSLQGDARAQLQRVLAA 292
Cdd:cd00951 223 GDHATVKRlLRDFFLPYVDIRNRRKGYAVsiVKAGARLVGRDAGPVRP-PLTDLTEEELAQLTALIKT 289
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
1-292 |
2.67e-18 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 82.94 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 1 MFTGLSAFPLTPL-VNGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQA-AGDIPVITSIGAl 78
Cdd:PRK03620 7 LGSGLLSFPVTPFdADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETtAGRVPVIAGAGG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 79 RLEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVSVPLCIYdNPATTgfTFTPELLQAVA-RLPNVGS 157
Cdd:PRK03620 86 GTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVY-NRDNA--VLTADTLARLAeRCPNLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 158 VKrspSGT-TLAQMREEIAALRRDI-------PATVTIGASadpKAIsallaGADTWYSVVAGLWPHDSRALAQAALSGD 229
Cdd:PRK03620 163 FK---DGVgDIELMQRIVRALGDRLlylgglpTAEVFAAAY---LAL-----GVPTYSSAVFNFVPEIALAFYRALRAGD 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358831916 230 EARTAA-LNAAFEPLWALFRHHGGLRV--IAAAAELTGRVAAPCLPePLQSLQGDARAQLQRVLAA 292
Cdd:PRK03620 232 HATVDRlLDDFFLPYVALRNRKKGYAVsiVKAGARLVGLDAGPVRA-PLTDLTPEELAELAALIAK 296
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
3-292 |
6.12e-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: 81.97 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 3 TGLSAFPLTPL-VNGQVDETTFVSLIETLA-AARVDSVAALGSTGSHAYLSREQRARVTTLAVQAAGD-IPVITSIGALR 79
Cdd:cd00954 2 KGLIAALLTPFdENGEINEDVLRAIVDYLIeKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGkVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 80 LEEMLDIADDAQRAGVSGLLLAPLSYQPLSQEEAYRLY-ERVARAVSVPLCIYDNPATTGFTFTPELLQAVARLPNVGSV 158
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYrEIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 159 KRspSGTTLAQMREEIAALRRD--IPATVtigasaDPKAISALLAGAD----TWYSVVAGLWphdsRALAQAALSGDEAR 232
Cdd:cd00954 162 KF--TATDLYDLERIRAASPEDklVLNGF------DEMLLSALALGADgaigSTYNVNGKRY----RKIFEAFNAGDIDT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 233 TAALNAAFEPLWALFRHHGGLRVIAAAAELTGRVAAPClPEPLQSLQGDARAQLQRVLAA 292
Cdd:cd00954 230 ARELQHVINDVITVLIKNGLYPTLKAILRLMGLDAGPC-RLPLRKVTEKALAKAKELAAK 288
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
19-245 |
4.79e-11 |
|
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: 62.46 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 19 DETtfVSLIETLAAARVDSVAALGSTGSHAYLS-REQRARVTTLAVQAAGDIPVITSIGALRLEEMLDIADDAQRAGVSG 97
Cdd:cd00952 29 DET--ARLVERLIAAGVDGILTMGTFGECATLTwEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGADG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 98 LLLAPLSYQPLSQEEAYRLYERVARAV-SVPLCIYDNPATTGFTFTPELLQAVARLPNVGSVKRSPSGTTLAQmreEIAA 176
Cdd:cd00952 107 TMLGRPMWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKYLGDIGALLS---DLAA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358831916 177 LRRDIPATVT-----IGASADPKAISALLAGadtwySVVAGLWPhdSRALAQAALSGD--EAR--TAALNAAFEPLWA 245
Cdd:cd00952 184 VKGRMRLLPLeddyyAAARLFPEEVTAFWSS-----GAACGPAP--VTALRDAVATGDwtDARalTDRMRWAAEPLFP 254
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
11-292 |
2.07e-09 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 57.34 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 11 TP-LVNGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTTLAVQAAGD-IPVITSIGALRLEEMLDIAD 88
Cdd:PLN02417 11 TPyLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGkIKVIGNTGSNSTREAIHATE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 89 DAQRAGVSGLLLAPLSYQPLSQEEAYRLYERVARAVsvPLCIYDNPATTGFTFTPELLQAVARLPNVGSVKRSPSGTTLA 168
Cdd:PLN02417 91 QGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKECTGNDRVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 169 QMREEiaalrrdipaTVTIGASADPKAISALL-AGADTWYSVVAGLWPHDSRALAQaalsgdEARTAALNAAFEPL--Wa 245
Cdd:PLN02417 169 QYTEK----------GILLWSGNDDECHDARWdYGADGVISVTSNLVPGLMHKLMF------AGKNKELNDKLLPLmdW- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1358831916 246 LFRHHGGLRVIAAAAELTgrVAAPCLPEPLQSLQGDARAQLQRVLAA 292
Cdd:PLN02417 232 LFCEPNPIGLNTALAQLG--LIRPVFRLPYVPLDLAKRAEFVALVKA 276
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
10-139 |
1.67e-07 |
|
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: 51.61 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 10 LTPLVNGQVDETTFVSLIETLAAARVDSVAALGSTGSHAYLSREQRARVTtlavQAAGDIP--VITSIGALRLEEMLDIA 87
Cdd:cd00953 9 ITPFTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELL----KAYSDITdkVIFQVGSLNLEESIELA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1358831916 88 DDAQRAGVSGLL-LAPLSYQPLSQEEAYRLYERVARavSVPLCIYDNPATTGF 139
Cdd:cd00953 85 RAAKSFGIYAIAsLPPYYFPGIPEEWLIKYFTDISS--PYPTFIYNYPKATGY 135
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
51-149 |
7.01e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 37.55 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358831916 51 SREQRARVTTLAVQAA-----GDIPVITSIGA-------LRLEEMLDIADDAQRAGVSGL-------LLAPLSYQPLSQE 111
Cdd:cd02803 186 SLENRARFLLEIVAAVreavgPDFPVGVRLSAddfvpggLTLEEAIEIAKALEEAGVDALhvsggsyESPPPIIPPPYVP 265
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1358831916 112 EAYRLY--ERVARAVSVPLciydnpATTGFTFTPELLQAV 149
Cdd:cd02803 266 EGYFLElaEKIKKAVKIPV------IAVGGIRDPEVAEEI 299
|
|
| |
