|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
7-289 |
2.46e-139 |
|
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: 394.55 E-value: 2.46e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 7 FRGSFTALVTPFKN-GALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNS 85
Cdd:cd00950 1 FGGSITALVTPFKDdGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 86 TREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGVK 165
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 166 DATANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLHD 245
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1347342330 246 AVFKEPGVAGAKHGLTLLGRIQEDVRLPLMTVTEPTGKAIRAAM 289
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
6-295 |
9.46e-133 |
|
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: 377.96 E-value: 9.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 6 KFRGSFTALVTPF-KNGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSN 84
Cdd:COG0329 1 KFRGVIPALVTPFdADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 85 STREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGV 164
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 165 KDATANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLH 244
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1347342330 245 DAVFKEPGVAGAKHGLTLLGRIQEDVRLPLMTVTEPTGKAIRAAMVHAGVI 295
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
9-292 |
7.67e-111 |
|
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: 322.36 E-value: 7.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 9 GSFTALVTPFK-NGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNSTR 87
Cdd:TIGR00674 1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 88 EAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGVKDA 167
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 168 TANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLHDAV 247
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1347342330 248 FKEPGVAGAKHGLTLLGRIQEDVRLPLMTVTEPTGKAIRAAMVHA 292
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
6-279 |
8.49e-103 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 301.98 E-value: 8.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 6 KFRGSFTALVTPFKN-GALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSN 84
Cdd:pfam00701 1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 85 STREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGV 164
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 165 KDATANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLH 244
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1347342330 245 DAVFKEPGVAGAKHGLTLLGRIQED-VRLPLMTVTE 279
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSE 276
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
9-292 |
6.33e-65 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 205.26 E-value: 6.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 9 GSFTALVTPF-KNGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNSTR 87
Cdd:PLN02417 4 RLITAIKTPYlPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 88 EAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVndAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGVKDA 167
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETV--LDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 168 TANlGRVSQqrhAMGPDFIQLSGEDMTAL-AYMAAGGHGCISVVSNIAPKLCSDLMgavFAGDYPgalKIQDRLVPLHDA 246
Cdd:PLN02417 162 TGN-DRVKQ---YTEKGILLWSGNDDECHdARWDYGADGVISVTSNLVPGLMHKLM---FAGKNK---ELNDKLLPLMDW 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1347342330 247 VFKEPGVAGAKHGLTLLGRIQEDVRLPLMtvtePTGKAIRAAMVHA 292
Cdd:PLN02417 232 LFCEPNPIGLNTALAQLGLIRPVFRLPYV----PLDLAKRAEFVAL 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
7-289 |
2.46e-139 |
|
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: 394.55 E-value: 2.46e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 7 FRGSFTALVTPFKN-GALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNS 85
Cdd:cd00950 1 FGGSITALVTPFKDdGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 86 TREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGVK 165
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 166 DATANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLHD 245
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1347342330 246 AVFKEPGVAGAKHGLTLLGRIQEDVRLPLMTVTEPTGKAIRAAM 289
Cdd:cd00950 241 ALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
6-295 |
9.46e-133 |
|
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: 377.96 E-value: 9.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 6 KFRGSFTALVTPF-KNGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSN 84
Cdd:COG0329 1 KFRGVIPALVTPFdADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 85 STREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGV 164
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 165 KDATANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLH 244
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1347342330 245 DAVFKEPGVAGAKHGLTLLGRIQEDVRLPLMTVTEPTGKAIRAAMVHAGVI 295
Cdd:COG0329 241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
11-289 |
6.67e-115 |
|
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: 332.21 E-value: 6.67e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 11 FTALVTPFK-NGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNSTREA 89
Cdd:cd00408 2 IPALVTPFTaDGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 90 VELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGVKDATA 169
Cdd:cd00408 82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 170 NLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLHDAVFK 249
Cdd:cd00408 162 DLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1347342330 250 EPGVAGAKHGLTLLGRIQEDVRLPLMTVTEPTGKAIRAAM 289
Cdd:cd00408 242 EGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
9-292 |
7.67e-111 |
|
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: 322.36 E-value: 7.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 9 GSFTALVTPFK-NGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNSTR 87
Cdd:TIGR00674 1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 88 EAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGVKDA 167
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 168 TANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLHDAV 247
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1347342330 248 FKEPGVAGAKHGLTLLGRIQEDVRLPLMTVTEPTGKAIRAAMVHA 292
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
6-279 |
8.49e-103 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 301.98 E-value: 8.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 6 KFRGSFTALVTPFKN-GALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSN 84
Cdd:pfam00701 1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 85 STREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGV 164
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 165 KDATANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLH 244
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1347342330 245 DAVFKEPGVAGAKHGLTLLGRIQED-VRLPLMTVTE 279
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSE 276
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
9-292 |
6.33e-65 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 205.26 E-value: 6.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 9 GSFTALVTPF-KNGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNSTR 87
Cdd:PLN02417 4 RLITAIKTPYlPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 88 EAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVndAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGVKDA 167
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETV--LDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKEC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 168 TANlGRVSQqrhAMGPDFIQLSGEDMTAL-AYMAAGGHGCISVVSNIAPKLCSDLMgavFAGDYPgalKIQDRLVPLHDA 246
Cdd:PLN02417 162 TGN-DRVKQ---YTEKGILLWSGNDDECHdARWDYGADGVISVTSNLVPGLMHKLM---FAGKNK---ELNDKLLPLMDW 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1347342330 247 VFKEPGVAGAKHGLTLLGRIQEDVRLPLMtvtePTGKAIRAAMVHA 292
Cdd:PLN02417 232 LFCEPNPIGLNTALAQLGLIRPVFRLPYV----PLDLAKRAEFVAL 273
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
8-279 |
2.31e-49 |
|
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: 165.18 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 8 RGSFTALVTPF-KNGALDEQAFRSLVNWQIE-QGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNS 85
Cdd:cd00954 2 KGLIAALLTPFdENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 86 TREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAV-NDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIVGV 164
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIiAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 165 KDATANLGRVSQQRHAMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQDRLVPLH 244
Cdd:cd00954 162 KFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVI 241
|
250 260 270
....*....|....*....|....*....|....*
gi 1347342330 245 DAVFKEPGVAGAKHGLTLLGRIQEDVRLPLMTVTE 279
Cdd:cd00954 242 TVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTE 276
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
15-279 |
5.06e-47 |
|
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: 159.41 E-value: 5.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 15 VTPFK-NGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNsTREAVELA 93
Cdd:cd00951 9 VTHFDaDGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYG-TATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 94 RHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAigiPIIIYNIPPRSVVDMSVDTMSRLYEL-DNIVGVKDATANLG 172
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKS---TDLGVIVYNRANAVLTADSLARLAERcPNLVGFKDGVGDIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 173 RVSQQRHAMGPDFIQLSG---EDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALK-IQDRLVPLHDAVF 248
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRlLRDFFLPYVDIRN 244
|
250 260 270
....*....|....*....|....*....|...
gi 1347342330 249 KEPG--VAGAKHGLTLLGRIQEDVRLPLMTVTE 279
Cdd:cd00951 245 RRKGyaVSIVKAGARLVGRDAGPVRPPLTDLTE 277
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
15-279 |
5.74e-44 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 151.51 E-value: 5.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 15 VTPFK-NGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAGSNsTREAVELA 93
Cdd:PRK03620 16 VTPFDaDGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGGG-TAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 94 RHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAigiPIIIYNIPPRSVVDMSVDTMSRL-YELDNIVGVKDATANLG 172
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKS---TDLGVIVYNRDNAVLTADTLARLaERCPNLVGFKDGVGDIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 173 RVSQQRHAMGPDFIQLSG---EDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKI-QDRLVPLHDAVF 248
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGGlptAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLlDDFFLPYVALRN 251
|
250 260 270
....*....|....*....|....*....|...
gi 1347342330 249 KEPG--VAGAKHGLTLLGRIQEDVRLPLMTVTE 279
Cdd:PRK03620 252 RKKGyaVSIVKAGARLVGLDAGPVRAPLTDLTP 284
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
5-237 |
3.25e-43 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 149.37 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 5 TKFRGSFTALVTPF-KNGALDEQAFRSLVNWQIE-QGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPVIAGAG 82
Cdd:PRK04147 2 KNLKGVYAALLTPFdEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 83 SNSTREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDAIGIPIIIYNIPPRSVVDMSVDTMSRLYELDNIV 162
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347342330 163 GVKDATANLGRVSQQRHAMgPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDYPGALKIQ 237
Cdd:PRK04147 162 GVKQTAGDLYQLERIRKAF-PDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQ 235
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
8-129 |
1.74e-16 |
|
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: 77.87 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 8 RGSFTALVTPFKNGA----------LDEQAfrSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWCIAEAKGRVPV 77
Cdd:cd00952 3 KGVWAIVPTPSKPDAsdwratdtvdLDETA--RLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1347342330 78 IAGAGSNSTREAVELARHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAVNDA 129
Cdd:cd00952 81 FVGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEA 132
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
12-289 |
9.41e-15 |
|
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: 72.80 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 12 TALVTPFKNGALDEQAFRSLVNWQIEQGTHGLVPVGTTGESPTLSHEEHHKVVEWC--IAEAkgrvpVIAGAGSNSTREA 89
Cdd:cd00953 6 TPVITPFTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYsdITDK-----VIFQVGSLNLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 90 VELARHAEKAGADAVLVVTPYY----------------NKPTQEGMYQHFKAVNdaigipiiiynipprsvVDMSVDTMS 153
Cdd:cd00953 81 IELARAAKSFGIYAIASLPPYYfpgipeewlikyftdiSSPYPTFIYNYPKATG-----------------YDINARMAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347342330 154 RL-YELDNIVGVKDATANLGRVSQQRHaMGPDFIQLSGEDMTALAYMAAGGHGCISVVSNIAPKLCSDLMGAVFAGDypg 232
Cdd:cd00953 144 EIkKAGGDIIGVKDTNEDISHMLEYKR-LVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIED--- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347342330 233 ALKIQDrlvpLHDAVF---KEPGVAGAKHGLT--LLGRIQEDVRLPLMTVTEPTGKAIRAAM 289
Cdd:cd00953 220 AFKLQF----LINEVLdasRKYGSWSANYSLVkiFQGYDAGEPRPPFYPLDEEEEEKLRKEV 277
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
71-129 |
7.93e-04 |
|
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: 39.62 E-value: 7.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347342330 71 AKGRVPVIAGAGSN----STREAVELARHAEKAGADAVLVVTPYYNKPT--QEGMYQHFKAVNDA 129
Cdd:cd00945 45 AGSDVPVIVVVGFPtgltTTEVKVAEVEEAIDLGADEIDVVINIGSLKEgdWEEVLEEIAAVVEA 109
|
|
| |
