|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
4-292 |
2.95e-118 |
|
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: 341.36 E-value: 2.95e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 4 KLKGIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLV 83
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 84 GTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGV 163
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 164 KDSSGNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDSIRS 243
Cdd:COG0329 161 KEASGDLDRIAELIRAT--GDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1496366546 244 -FRDCFKFANPnTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVLNE 292
Cdd:COG0329 239 lIRALFAEGNP-APVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKE 287
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-290 |
9.82e-108 |
|
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: 314.10 E-value: 9.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 8 IITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLVGTQD 87
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 88 TIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGVKDSS 167
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 168 GNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDSIRS-FRD 246
Cdd:cd00408 161 GDLDRLTRLIALL--GPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPlIEA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1496366546 247 CFKFANPnTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVL 290
Cdd:cd00408 239 LFKEGNP-APVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-290 |
1.45e-80 |
|
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: 245.32 E-value: 1.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 7 GIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLVGTQ 86
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 87 DTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGVKDS 166
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 167 SGNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARN-YQDSIRSFR 245
Cdd:TIGR00674 161 TGNLERISEIKAIA--PDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREiHQKLMPLHK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1496366546 246 DCFKFANPnTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVL 290
Cdd:TIGR00674 239 ALFIETNP-IPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVL 282
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
4-290 |
8.33e-78 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 238.42 E-value: 8.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 4 KLKGIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLV 83
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 84 GTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGV 163
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 164 KDSSGNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDSIRS 243
Cdd:pfam00701 161 KEASGDLDRMINIKKEA--GPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1496366546 244 FRDCFkFANPNTV-VKTAVELLGYPVG-KCRAPFNQVSAEGIAALKSVL 290
Cdd:pfam00701 239 LIKIL-FAEPNPIpIKTALELLGLVVGpTCRLPLTPLSEEERPELEAIL 286
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-287 |
4.34e-46 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 157.08 E-value: 4.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 2 QNKLKGIITPIVTPMFDNEEVNYEELVNQVNRVIE-NGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYAST 80
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 81 GLVGTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNI 160
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 161 VGVKDSSGNFdnilqY-IERTRNR-EDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQ 238
Cdd:PRK04147 161 IGVKQTAGDL-----YqLERIRKAfPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1496366546 239 DSIRSFRDCFKFANPNTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALK 287
Cdd:PRK04147 236 HECNDVIDLLIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYLPALK 284
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
4-292 |
2.95e-118 |
|
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: 341.36 E-value: 2.95e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 4 KLKGIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLV 83
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 84 GTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGV 163
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 164 KDSSGNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDSIRS 243
Cdd:COG0329 161 KEASGDLDRIAELIRAT--GDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1496366546 244 -FRDCFKFANPnTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVLNE 292
Cdd:COG0329 239 lIRALFAEGNP-APVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKE 287
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-290 |
9.82e-108 |
|
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: 314.10 E-value: 9.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 8 IITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLVGTQD 87
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 88 TIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGVKDSS 167
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 168 GNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDSIRS-FRD 246
Cdd:cd00408 161 GDLDRLTRLIALL--GPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPlIEA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1496366546 247 CFKFANPnTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVL 290
Cdd:cd00408 239 LFKEGNP-APVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
5-290 |
8.04e-101 |
|
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: 296.71 E-value: 8.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 5 LKGIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLVG 84
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 85 TQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGVK 164
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 165 DSSGNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDSIRS- 243
Cdd:cd00950 161 EATGDLDRVSELIALC--PDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPl 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1496366546 244 FRDCFKFANPnTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVL 290
Cdd:cd00950 239 IKALFAEPNP-IPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-290 |
1.45e-80 |
|
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: 245.32 E-value: 1.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 7 GIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLVGTQ 86
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 87 DTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGVKDS 166
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 167 SGNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARN-YQDSIRSFR 245
Cdd:TIGR00674 161 TGNLERISEIKAIA--PDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREiHQKLMPLHK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1496366546 246 DCFKFANPnTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVL 290
Cdd:TIGR00674 239 ALFIETNP-IPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVL 282
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
4-290 |
8.33e-78 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 238.42 E-value: 8.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 4 KLKGIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLV 83
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 84 GTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNIVGV 163
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 164 KDSSGNFDNILQYIERTrnREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDSIRS 243
Cdd:pfam00701 161 KEASGDLDRMINIKKEA--GPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1496366546 244 FRDCFkFANPNTV-VKTAVELLGYPVG-KCRAPFNQVSAEGIAALKSVL 290
Cdd:pfam00701 239 LIKIL-FAEPNPIpIKTALELLGLVVGpTCRLPLTPLSEEERPELEAIL 286
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-291 |
3.88e-56 |
|
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: 182.89 E-value: 3.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 5 LKGIITPIVTPMFDNEEVNYEELVNQVNRVIE-NGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLV 83
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 84 GTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAV-DMPIVLYNIPARTGNTIQPATVEKLSHIDNIVG 162
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 163 VKDSSGNFdnilQYIERTR--NREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQDS 240
Cdd:cd00954 161 VKFTATDL----YDLERIRaaSPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1496366546 241 IRSFRdCFKFANP-NTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVLN 291
Cdd:cd00954 237 INDVI-TVLIKNGlYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAKELAA 287
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-287 |
4.34e-46 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 157.08 E-value: 4.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 2 QNKLKGIITPIVTPMFDNEEVNYEELVNQVNRVIE-NGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYAST 80
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 81 GLVGTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNIPARTGNTIQPATVEKLSHIDNI 160
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 161 VGVKDSSGNFdnilqY-IERTRNR-EDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFVKGNIEEARNYQ 238
Cdd:PRK04147 161 IGVKQTAGDL-----YqLERIRKAfPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1496366546 239 DSIRSFRDCFKFANPNTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALK 287
Cdd:PRK04147 236 HECNDVIDLLIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYLPALK 284
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
4-289 |
8.89e-42 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 145.56 E-value: 8.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 4 KLKGIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLV 83
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 84 GTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAeavDM-PIVLYNIPARTGNTIQPATVEKLSHIDNIVG 162
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVL---DMgPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 163 VKDSSGNfDNILQYIERtrnreDFSVLSGNDSLIL-WTLLAGGTGGIAGCSNVYPFTMAQIyeqfvkgnIEEARNyqDSI 241
Cdd:PLN02417 158 VKECTGN-DRVKQYTEK-----GILLWSGNDDECHdARWDYGADGVISVTSNLVPGLMHKL--------MFAGKN--KEL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1496366546 242 RS-FRDCFK--FANPNTV-VKTAVELLGY--PVgkCRAPFNQVS----AEGIAALKSV 289
Cdd:PLN02417 222 NDkLLPLMDwlFCEPNPIgLNTALAQLGLirPV--FRLPYVPLDlakrAEFVALVKAI 277
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
8-292 |
1.01e-34 |
|
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188640 Cd Length: 279 Bit Score: 127.11 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 8 IITPIVTPmFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDtVADRVPVyaSTGLVGTQD 87
Cdd:cd00953 4 KITPVITP-FTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSD-ITDKVIF--QVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 88 TIRLSLEAKRVGVDYLSIITP-YFAAATQEEIYTHFKTVAEAvdMPIVLYNIPARTGNTIQPATVEKL-SHIDNIVGVKD 165
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPyYFPGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIkKAGGDIIGVKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 166 SSGNFDNILQYierTRNREDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFTMAQIYEQFvkgNIEEARNYQDSIRSFR 245
Cdd:cd00953 158 TNEDISHMLEY---KRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV---AIEDAFKLQFLINEVL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1496366546 246 DCF-KFANPNTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVLNE 292
Cdd:cd00953 232 DASrKYGSWSANYSLVKIFQGYDAGEPRPPFYPLDEEEEEKLRKEVNE 279
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
7-290 |
2.15e-29 |
|
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH); 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate.
Pssm-ID: 188638 Cd Length: 289 Bit Score: 113.19 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 7 GIITPIVTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGlVGTQ 86
Cdd:cd00951 3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAG-YGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 87 DTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNipaRTGNTIQPATVEKLS-HIDNIVGVKD 165
Cdd:cd00951 82 TAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAeRCPNLVGFKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 166 SSGNFDnILQYIERTRNrEDFSVLSGNDSLILWTLLAGGTGGIAGCSNVYPFT--MAQIYEQFVKGNIEEA--RNYQDSI 241
Cdd:cd00951 159 GVGDIE-LMRRIVAKLG-DRLLYLGGLPTAEVFALAYLAMGVPTYSSAVFNFVpeIALAFYAAVRAGDHATvkRLLRDFF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1496366546 242 RSFRDCFKFAN--PNTVVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVL 290
Cdd:cd00951 237 LPYVDIRNRRKgyAVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLTALI 287
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
13-290 |
3.00e-27 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 107.59 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 13 VTPMFDNEEVNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVYASTGLvGTQDTIRLS 92
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 93 LEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAVDMPIVLYNipaRTGNTIQPATVEKLSH-IDNIVGVKDSSGNFD 171
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAErCPNLVGFKDGVGDIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 172 NiLQYIeRTRNREDFSVLSGndsliLWT--LLAGGTGGIaGC----SNVYPF------------------TMAQIYEQFV 227
Cdd:PRK03620 172 L-MQRI-VRALGDRLLYLGG-----LPTaeVFAAAYLAL-GVptysSAVFNFvpeialafyralragdhaTVDRLLDDFF 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1496366546 228 KgNIEEARN----YQDSIrsfrdcfkfanpntvVKTAVELLGYPVGKCRAPFNQVSAEGIAALKSVL 290
Cdd:PRK03620 244 L-PYVALRNrkkgYAVSI---------------VKAGARLVGLDAGPVRAPLTDLTPEELAELAALI 294
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
5-281 |
2.58e-25 |
|
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: 102.52 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 5 LKGIITPIVTPMFDNEE-------VNYEELVNQVNRVIENGVHGIFTFGTNGEGYILSEEEKVHVMETVVDTVADRVPVY 77
Cdd:cd00952 2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 78 ASTGLVGTQDTIRLSLEAKRVGVDYLSIITPYFAAATQEEIYTHFKTVAEAV-DMPIVLYNIPARTGNTIQPATVEKLSH 156
Cdd:cd00952 82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 157 IDNIVGVKdSSGNFDNILQYIERTRNREDFSVLsgnDSLILWTLLAG---GTGGIAGCSNVYPFTMAQIYEQFVKGNIEE 233
Cdd:cd00952 162 IPQVVAAK-YLGDIGALLSDLAAVKGRMRLLPL---EDDYYAAARLFpeeVTAFWSSGAACGPAPVTALRDAVATGDWTD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1496366546 234 ARNYQDSIRSFRDCF-------KFANPN-TVVKTAVELLGYPV-GKCRAPFNQVSAE 281
Cdd:cd00952 238 ARALTDRMRWAAEPLfprgdfsEFSKYNiALEKARFDAAGYMRaGPARPPYNTAPEA 294
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
8-157 |
1.30e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 39.23 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496366546 8 IITPIVTPMFDneevnYEELVNQVNRVIENGVHGIFTFGTngegyilseeekvhVMETVVDTVADRVPVYA-----STGL 82
Cdd:cd00945 1 IDLTLLHPDAT-----LEDIAKLCDEAIEYGFAAVCVNPG--------------YVRLAADALAGSDVPVIvvvgfPTGL 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1496366546 83 VGTQDTIRLSLEAKRVGVDYLSIITPYFAAAT--QEEIYTHFKTVAEAVD--MPIVLYNIPARTGNtiqPATVEKLSHI 157
Cdd:cd00945 62 TTTEVKVAEVEEAIDLGADEIDVVINIGSLKEgdWEEVLEEIAAVVEAADggLPLKVILETRGLKT---ADEIAKAARI 137
|
|
| |
