|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
3-286 |
4.53e-146 |
|
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: 411.12 E-value: 4.53e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 3 FKGSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNN 82
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 83 TMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVK 162
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 163 EASGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIA 242
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489534069 243 ALFIEVNPVPVKTAMNILGFNVGDLRLPLAEMEETNLNVLKQEL 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-291 |
3.39e-137 |
|
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: 389.13 E-value: 3.39e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 3 FKGSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNN 82
Cdd:COG0329 2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 83 TMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVK 162
Cdd:COG0329 82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 163 EASGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIA 242
Cdd:COG0329 162 EASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489534069 243 ALFIEVNPVPVKTAMNILGFNVGDLRLPLAEMEETNLNVLKQELTNFGF 291
Cdd:COG0329 242 ALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-287 |
2.24e-120 |
|
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: 346.24 E-value: 2.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 5 GSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNNTM 84
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 85 LSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVKEA 164
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 165 SGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIAAL 244
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489534069 245 FIEVNPVPVKTAMNILGFNVGDLRLPLAEMEETNLNVLKQELT 287
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLK 283
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-287 |
1.22e-106 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 311.61 E-value: 1.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 3 FKGSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNN 82
Cdd:pfam00701 2 FSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 83 TMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVK 162
Cdd:pfam00701 82 TSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 163 EASGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIA 242
Cdd:pfam00701 162 EASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489534069 243 ALFIEVNPVPVKTAMNILGFNVGD-LRLPLAEMEETNLNVLKQELT 287
Cdd:pfam00701 242 ILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILK 287
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
5-274 |
8.09e-82 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 248.02 E-value: 8.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 5 GSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNNTM 84
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 85 LSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVklPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVKEA 164
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 165 SGDlaqvAEIAKLVPKDFAIYSGNDDTILP-LLSLGGSGVISVLANICPKETHDLVtkfFEGDiegSKKLQLDMDALIAA 243
Cdd:PLN02417 162 TGN----DRVKQYTEKGILLWSGNDDECHDaRWDYGADGVISVTSNLVPGLMHKLM---FAGK---NKELNDKLLPLMDW 231
|
250 260 270
....*....|....*....|....*....|.
gi 489534069 244 LFIEVNPVPVKTAMNILGFNVGDLRLPLAEM 274
Cdd:PLN02417 232 LFCEPNPIGLNTALAQLGLIRPVFRLPYVPL 262
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
3-286 |
4.53e-146 |
|
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: 411.12 E-value: 4.53e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 3 FKGSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNN 82
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 83 TMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVK 162
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 163 EASGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIA 242
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489534069 243 ALFIEVNPVPVKTAMNILGFNVGDLRLPLAEMEETNLNVLKQEL 286
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-291 |
3.39e-137 |
|
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: 389.13 E-value: 3.39e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 3 FKGSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNN 82
Cdd:COG0329 2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 83 TMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVK 162
Cdd:COG0329 82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 163 EASGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIA 242
Cdd:COG0329 162 EASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489534069 243 ALFIEVNPVPVKTAMNILGFNVGDLRLPLAEMEETNLNVLKQELTNFGF 291
Cdd:COG0329 242 ALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
5-287 |
2.24e-120 |
|
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: 346.24 E-value: 2.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 5 GSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNNTM 84
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 85 LSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVKEA 164
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 165 SGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIAAL 244
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489534069 245 FIEVNPVPVKTAMNILGFNVGDLRLPLAEMEETNLNVLKQELT 287
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLK 283
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-286 |
7.78e-120 |
|
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: 344.92 E-value: 7.78e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 8 VALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNNTMLSV 87
Cdd:cd00408 3 PALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 88 HMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVKEASGD 167
Cdd:cd00408 83 ELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 168 LAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIAALFIE 247
Cdd:cd00408 163 LDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKE 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 489534069 248 VNPVPVKTAMNILGFNVGDLRLPLAEMEETNLNVLKQEL 286
Cdd:cd00408 243 GNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-287 |
1.22e-106 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 311.61 E-value: 1.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 3 FKGSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNN 82
Cdd:pfam00701 2 FSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 83 TMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVK 162
Cdd:pfam00701 82 TSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 163 EASGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIA 242
Cdd:pfam00701 162 EASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489534069 243 ALFIEVNPVPVKTAMNILGFNVGD-LRLPLAEMEETNLNVLKQELT 287
Cdd:pfam00701 242 ILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILK 287
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
5-274 |
8.09e-82 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 248.02 E-value: 8.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 5 GSAVALVTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNNTM 84
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 85 LSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVklPIILYNVPGRTKVNIKPSVVAELAKIDNIVAVKEA 164
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG--PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 165 SGDlaqvAEIAKLVPKDFAIYSGNDDTILP-LLSLGGSGVISVLANICPKETHDLVtkfFEGDiegSKKLQLDMDALIAA 243
Cdd:PLN02417 162 TGN----DRVKQYTEKGILLWSGNDDECHDaRWDYGADGVISVTSNLVPGLMHKLM---FAGK---NKELNDKLLPLMDW 231
|
250 260 270
....*....|....*....|....*....|.
gi 489534069 244 LFIEVNPVPVKTAMNILGFNVGDLRLPLAEM 274
Cdd:PLN02417 232 LFCEPNPIGLNTALAQLGLIRPVFRLPYVPL 262
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
4-284 |
1.91e-61 |
|
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: 196.38 E-value: 1.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 4 KGSAVALVTPFTEDNNVNFEKLGELIEYHIE-NGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNN 82
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 83 TMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVK-LPIILYNVPGRTKVNIKPSVVAELAKIDNIVAV 161
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAAsLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 162 KEASGDLAQVAEIAKLVPKDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALI 241
Cdd:cd00954 162 KFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489534069 242 AALfIEVNPVPV-KTAMNILGFNVGDLRLPLAEMEETNLNVLKQ 284
Cdd:cd00954 242 TVL-IKNGLYPTlKAILRLMGLDAGPCRLPLRKVTEKALAKAKE 284
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-284 |
2.50e-49 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 165.17 E-value: 2.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 1 MLFKGSAVALVTPFTEDNNVNFEKLGELIEYHIE-NGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTG 79
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 80 SNNTMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNVPGRTKVNIKPSVVAELAKIDNIV 159
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 160 AVKEASGDLAQVAEIAKLVPkDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDA 239
Cdd:PRK04147 162 GVKQTAGDLYQLERIRKAFP-DKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECND 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489534069 240 LIAALfIEVNPVP-VKTAMNILGFNVGDLRLPLAEMEETNLNVLKQ 284
Cdd:PRK04147 241 VIDLL-IKNGVYPgLKEILHYMGVDAGLCRKPFKPVDEKYLPALKA 285
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
11-284 |
4.54e-35 |
|
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: 127.82 E-value: 4.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 11 VTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSNnTMLSVHMS 90
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 91 QEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNvpgRTKVNIKPSVVAELA-KIDNIVAVKEASGDLA 169
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAeRCPNLVGFKDGVGDIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 170 QVAEIAKLVPKDFAIYSG---NDDTILPLLSLGGSGVISVLANICPKETHDLVTKFFEGDIEGSKKLQLDMDALIAALfi 246
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFFLPYVDI-- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489534069 247 eVNPVP------VKTAMNILGFNVGDLRLPLAEMEETNLNVLKQ 284
Cdd:cd00951 243 -RNRRKgyavsiVKAGARLVGRDAGPVRPPLTDLTEEELAQLTA 285
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
11-276 |
6.45e-33 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 122.62 E-value: 6.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 11 VTPFTEDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIAGTGSnNTMLSVHMS 90
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 91 QEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSVKLPIILYNvpgRTKVNIKPSVVAELA-KIDNIVAVKEASGDLA 169
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAeRCPNLVGFKDGVGDIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 170 QVAEIAKLVPKDFAIYSG---NDDTILPLLSLGGSGVISVLANICPKethdLVTKFFEGDIEGSKKLqldMDALIAALFI 246
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGGlptAEVFAAAYLALGVPTYSSAVFNFVPE----IALAFYRALRAGDHAT---VDRLLDDFFL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489534069 247 EV----NPVP------VKTAMNILGFNVGDLRLPL-----AEMEE 276
Cdd:PRK03620 245 PYvalrNRKKgyavsiVKAGARLVGLDAGPVRAPLtdltpEELAE 289
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
8-279 |
9.93e-25 |
|
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188640 Cd Length: 279 Bit Score: 100.15 E-value: 9.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 8 VALVTPFTeDNNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKripVIAGTGSNNTMLSV 87
Cdd:cd00953 6 TPVITPFT-GNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITDK---VIFQVGSLNLEESI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 88 HMSQEAEKLGVDGLLIITPYY-NKTNEKGLKLHFETIANSVklPIILYNVPGRTKVNIKPSVVAELAKI-DNIVAVKEAS 165
Cdd:cd00953 82 ELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISSPY--PTFIYNYPKATGYDINARMAKEIKKAgGDIIGVKDTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 166 GDLAQVAEIAKLVPkDFAIYSGNDDTILPLLSLGGSGVISVLANICPKETHDLVTKFfegDIEGSKKLQLDMDALIAAL- 244
Cdd:cd00953 160 EDISHMLEYKRLVP-DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV---AIEDAFKLQFLINEVLDASr 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489534069 245 ---FIEVNPVPVKTamnILGFNVGDLR---LPLAEMEETNL 279
Cdd:cd00953 236 kygSWSANYSLVKI---FQGYDAGEPRppfYPLDEEEEEKL 273
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
4-245 |
2.75e-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: 91.35 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 4 KGSAVALVTPFTED-------NNVNFEKLGELIEYHIENGTDALVVCGTTGEATTMSESEIFAVIKYTVEKVNKRIPVIA 76
Cdd:cd00952 3 KGVWAIVPTPSKPDasdwratDTVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 77 GTGSNNTMLSVHMSQEAEKLGVDGLLIITPYYNKTNEKGLKLHFETIANSV-KLPIILYNVPGRTKVNIKPSVVAELAKI 155
Cdd:cd00952 83 GATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534069 156 DNIVAVKEAS------GDLAQVAEIAKLVPKDFAIYSGNddTILPLLSLGG--SGVisvlanIC-PKETHDLVTKFFEGD 226
Cdd:cd00952 163 PQVVAAKYLGdigallSDLAAVKGRMRLLPLEDDYYAAA--RLFPEEVTAFwsSGA------ACgPAPVTALRDAVATGD 234
|
250
....*....|....*....
gi 489534069 227 IEGSKKLQLDMDALIAALF 245
Cdd:cd00952 235 WTDARALTDRMRWAAEPLF 253
|
|
| |
