|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
5-292 |
4.83e-110 |
|
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: 320.18 E-value: 4.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 5 IHGIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLT 84
Cdd:COG0329 2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 85 TAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMV 164
Cdd:COG0329 82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 165 KESTGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLL 244
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489192550 245 DFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-289 |
2.11e-99 |
|
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: 292.91 E-value: 2.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 8 IIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTAK 87
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 88 TVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKES 167
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLA-EHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 168 TGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDFI 247
Cdd:cd00408 160 SGDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489192550 248 LRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLL 289
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-292 |
1.41e-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: 199.09 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVREVdNVTMVKE 166
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489192550 247 ILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-292 |
6.45e-60 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 192.58 E-value: 6.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKE 166
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLA-TNPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:pfam00701 163 ASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489192550 247 ILRRGLPTTIKAGLGLSGLEVGA-PRLPVQALDTEGCRYLQGLLEEL 292
Cdd:pfam00701 243 LFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
7-293 |
2.97e-34 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 126.08 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSdLTTA 86
Cdd:PRK03620 10 GLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 87 KTVRRAQFAESLGAEAVMVLPiSYwkLNEAE---VFQHYRAVGEAIGVPVMLYNNpGTSgiDMSVELILRIVREVDNVTM 163
Cdd:PRK03620 89 QAIEYAQAAERAGADGILLLP-PY--LTEAPqegLAAHVEAVCKSTDLGVIVYNR-DNA--VLTADTLARLAERCPNLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 164 VKESTGDIQRMHKLRLLGEGRVPFYNGCnPLAlEAFVAGAKG-----WCSAAPNLIPTLNGQLYQAVLDGDLEKARAL-- 236
Cdd:PRK03620 163 FKDGVGDIELMQRIVRALGDRLLYLGGL-PTA-EVFAAAYLAlgvptYSSAVFNFVPEIALAFYRALRAGDHATVDRLld 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489192550 237 -FYrqLPLLDfiLRRGLP----TTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEELR 293
Cdd:PRK03620 241 dFF--LPYVA--LRNRKKgyavSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGG 298
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
5-292 |
4.83e-110 |
|
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: 320.18 E-value: 4.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 5 IHGIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLT 84
Cdd:COG0329 2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 85 TAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMV 164
Cdd:COG0329 82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 165 KESTGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLL 244
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489192550 245 DFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-289 |
2.11e-99 |
|
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: 292.91 E-value: 2.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 8 IIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTAK 87
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 88 TVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKES 167
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLA-EHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 168 TGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDFI 247
Cdd:cd00408 160 SGDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489192550 248 LRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLL 289
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
13-286 |
2.75e-78 |
|
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: 239.32 E-value: 2.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 13 ITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTAKTVRRA 92
Cdd:cd00950 9 VTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTAEAIELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 93 QFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKESTGDIQ 172
Cdd:cd00950 89 KRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLA-EHPNIVGIKEATGDLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 173 RMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDFILRRGL 252
Cdd:cd00950 168 RVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIKALFAEPN 247
|
250 260 270
....*....|....*....|....*....|....
gi 489192550 253 PTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQ 286
Cdd:cd00950 248 PIPVKAALALLGLISGELRLPLVPLSEELRAKLR 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-292 |
1.41e-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: 199.09 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVREVdNVTMVKE 166
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489192550 247 ILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-292 |
6.45e-60 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 192.58 E-value: 6.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKE 166
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLA-TNPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:pfam00701 163 ASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489192550 247 ILRRGLPTTIKAGLGLSGLEVGA-PRLPVQALDTEGCRYLQGLLEEL 292
Cdd:pfam00701 243 LFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
7-280 |
2.91e-43 |
|
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: 149.38 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLID-GGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTT 85
Cdd:cd00954 3 GLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 86 AKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGE-AIGVPVMLYNNPGTSGIDMSVELILrIVREVDNVTMV 164
Cdd:cd00954 83 KESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAaAASLPMIIYHIPALTGVNLTLEQFL-ELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 165 KESTGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLL 244
Cdd:cd00954 162 KFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVI 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 489192550 245 DFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTE 280
Cdd:cd00954 242 TVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEK 277
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
7-290 |
2.61e-36 |
|
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: 131.29 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSdLTTA 86
Cdd:cd00951 3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAG-YGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 87 KTVRRAQFAESLGAEAVMVLPiSYWKLNEAE-VFQHYRAVGEAIGVPVMLYNNpGTSGIdmSVELILRIVREVDNVTMVK 165
Cdd:cd00951 82 TAIAYAQAAEKAGADGILLLP-PYLTEAPQEgLYAHVEAVCKSTDLGVIVYNR-ANAVL--TADSLARLAERCPNLVGFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 166 ESTGDIQRMHKLRLLGEGRVPFYNGCnPLAlEAFVAGAKG-----WCSAAPNLIPTLNGQLYQAVLDGDLEKARAL---F 237
Cdd:cd00951 158 DGVGDIELMRRIVAKLGDRLLYLGGL-PTA-EVFALAYLAmgvptYSSAVFNFVPEIALAFYAAVRAGDHATVKRLlrdF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489192550 238 YrqLPLLDFILRR-GLPTTI-KAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLE 290
Cdd:cd00951 236 F--LPYVDIRNRRkGYAVSIvKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIK 288
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
7-293 |
2.97e-34 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 126.08 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSdLTTA 86
Cdd:PRK03620 10 GLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 87 KTVRRAQFAESLGAEAVMVLPiSYwkLNEAE---VFQHYRAVGEAIGVPVMLYNNpGTSgiDMSVELILRIVREVDNVTM 163
Cdd:PRK03620 89 QAIEYAQAAERAGADGILLLP-PY--LTEAPqegLAAHVEAVCKSTDLGVIVYNR-DNA--VLTADTLARLAERCPNLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 164 VKESTGDIQRMHKLRLLGEGRVPFYNGCnPLAlEAFVAGAKG-----WCSAAPNLIPTLNGQLYQAVLDGDLEKARAL-- 236
Cdd:PRK03620 163 FKDGVGDIELMQRIVRALGDRLLYLGGL-PTA-EVFAAAYLAlgvptYSSAVFNFVPEIALAFYRALRAGDHATVDRLld 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489192550 237 -FYrqLPLLDfiLRRGLP----TTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEELR 293
Cdd:PRK03620 241 dFF--LPYVA--LRNRKKgyavSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGG 298
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
7-273 |
4.38e-32 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 120.10 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDG-GVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTT 85
Cdd:PRK04147 6 GVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSVNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 86 AKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVK 165
Cdd:PRK04147 86 AEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELF-TLPKVIGVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 166 ESTGDIQRMHKLRllgeGRVP---FYNGCNPLALEAFVAGAKGWCSAAPNliptLNGQLYQAVLD----GDLEKARALFY 238
Cdd:PRK04147 165 QTAGDLYQLERIR----KAFPdklIYNGFDEMFASGLLAGADGAIGSTYN----VNGWRARQIFEaakaGDIQEAQELQH 236
|
250 260 270
....*....|....*....|....*....|....*
gi 489192550 239 RQLPLLDFILRRGLPTTIKAGLGLSGLEVGAPRLP 273
Cdd:PRK04147 237 ECNDVIDLLIKNGVYPGLKEILHYMGVDAGLCRKP 271
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
7-280 |
5.72e-23 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 95.48 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSdpeWDE---VVDFTLKTVAHRVPTIVSVSDL 83
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMS---WDEhimLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 84 TTAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEaIGvPVMLYNNPGTSGIDMSVELILrIVREVDNVTM 163
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD-MG-PTIIYNVPGRTGQDIPPEVIF-KIAQHPNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 164 VKESTGDiQRMHKLRllgEGRVPFYNGCNPLALEA-FVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKaralfyRQLP 242
Cdd:PLN02417 158 VKECTGN-DRVKQYT---EKGILLWSGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFAGKNKELND------KLLP 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 489192550 243 LLDFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTE 280
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLA 265
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
8-280 |
1.91e-22 |
|
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: 93.99 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 8 IIGYTITPFAaDGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDfTLKTVAHRVptIVSVSDLTTAK 87
Cdd:cd00953 4 KITPVITPFT-GNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLK-AYSDITDKV--IFQVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 88 TVRRAQFAESLGAEAVMVLPISYW-KLNEAEVFQHYRAVGEAIgvPVMLYNNPGTSGIDMSVELILRIVREVDNVTMVKE 166
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYFpGIPEEWLIKYFTDISSPY--PTFIYNYPKATGYDINARMAKEIKKAGGDIIGVKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 167 STGDIqrMHKL---RLLGEGRVpfYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVldgDLEKARALFYRQLPL 243
Cdd:cd00953 158 TNEDI--SHMLeykRLVPDFKV--YSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV---AIEDAFKLQFLINEV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489192550 244 LDFILRRGlptTIKAGLGL----SGLEVGAPRLPVQALDTE 280
Cdd:cd00953 231 LDASRKYG---SWSANYSLvkifQGYDAGEPRPPFYPLDEE 268
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
5-236 |
1.53e-21 |
|
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: 92.12 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 5 IHGIIGYTITPFAADGG-------LDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTI 77
Cdd:cd00952 2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 78 VSVSDLTTAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAigVP---VMLYNNPGTSGIDMSvELILRI 154
Cdd:cd00952 82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEA--VPemaIAIYANPEAFKFDFP-RAAWAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 155 VREVDNVTMVKEsTGDIQRMHKLRLLGEGRVPFYngcnPL------ALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDG 228
Cdd:cd00952 159 LAQIPQVVAAKY-LGDIGALLSDLAAVKGRMRLL----PLeddyyaAARLFPEEVTAFWSSGAACGPAPVTALRDAVATG 233
|
....*...
gi 489192550 229 DLEKARAL 236
Cdd:cd00952 234 DWTDARAL 241
|
|
|