|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
4-290 |
1.77e-148 |
|
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: 417.66 E-value: 1.77e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 4 IEGVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDC--SKVPVIAGTGSNN 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAvnGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 82 TKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITNIKGV 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLA-EHPNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 162 KEASGDLKQVGAIIrsvAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRLF 241
Cdd:cd00950 160 KEATGDLDRVSELI---ALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1899281696 242 SLFEAMFLETNPIPVKKAAEMMGLvETGDVRLPLGALSEGNEEKLRAVL 290
Cdd:cd00950 237 PLIKALFAEPNPIPVKAALALLGL-ISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-294 |
1.41e-135 |
|
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: 385.28 E-value: 1.41e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 3 KIEGVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCS--KVPVIAGTGSN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAagRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 81 NTKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITNIKG 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 161 VKEASGDLKQVGAIIRSVAEqglDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRL 240
Cdd:COG0329 160 IKEASGDLDRIAELIRATGD---DFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1899281696 241 FSLFEAMFLETNPIPVKKAAEMMGLvETGDVRLPLGALSEGNEEKLRAVLKGLG 294
Cdd:COG0329 237 LPLIRALFAEGNPAPVKAALALLGL-PSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
6-293 |
1.56e-130 |
|
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: 372.05 E-value: 1.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 6 GVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCSK--VPVIAGTGSNNTK 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNgrVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 84 EAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELASEItNIKGVKE 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 164 ASGDLKQVGAIIrsvAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRLFSL 243
Cdd:TIGR00674 160 ATGNLERISEIK---AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1899281696 244 FEAMFLETNPIPVKKAAEMMGLVEtGDVRLPLGALSEGNEEKLRAVLKGL 293
Cdd:TIGR00674 237 HKALFIETNPIPVKTALALLGLIE-GELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
6-291 |
2.70e-106 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 310.84 E-value: 2.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 6 GVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCSK--VPVIAGTGSNNTK 83
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKgrIPVIAGVGSNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 84 EAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITNIKGVKE 163
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLA-TNPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 164 ASGDLKQvgaIIRSVAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRLFSL 243
Cdd:pfam00701 163 ASGDLDR---MINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1899281696 244 FEAMFLETNPIPVKKAAEMMGLVETGDVRLPLGALSEGNEEKLRAVLK 291
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILK 287
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
6-295 |
2.51e-75 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 231.84 E-value: 2.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 6 GVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDC--SKVPVIAGTGSNNTK 83
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCfgGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 84 EAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDsvEIPLILYNIPSRTAQNVNAGTMVELASEiTNIKGVKE 163
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAGVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 164 ASGDLKqvgaiIRSVAEQGldFTVVAGDDFLTLP-IMSLGGKGVISVAANIAPREMTEMvdaMLKGkveKAKEINIRLFS 242
Cdd:PLN02417 161 CTGNDR-----VKQYTEKG--ILLWSGNDDECHDaRWDYGADGVISVTSNLVPGLMHKL---MFAG---KNKELNDKLLP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1899281696 243 LFEAMFLETNPIPVKKAAEMMGLVETGdVRLPLGALSEGNEEKLRAVLKGLGM 295
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRPV-FRLPYVPLDLAKRAEFVALVKAIGR 279
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
4-290 |
1.77e-148 |
|
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: 417.66 E-value: 1.77e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 4 IEGVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDC--SKVPVIAGTGSNN 81
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAvnGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 82 TKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITNIKGV 161
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLA-EHPNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 162 KEASGDLKQVGAIIrsvAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRLF 241
Cdd:cd00950 160 KEATGDLDRVSELI---ALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1899281696 242 SLFEAMFLETNPIPVKKAAEMMGLvETGDVRLPLGALSEGNEEKLRAVL 290
Cdd:cd00950 237 PLIKALFAEPNPIPVKAALALLGL-ISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-294 |
1.41e-135 |
|
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: 385.28 E-value: 1.41e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 3 KIEGVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCS--KVPVIAGTGSN 80
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAagRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 81 NTKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITNIKG 160
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 161 VKEASGDLKQVGAIIRSVAEqglDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRL 240
Cdd:COG0329 160 IKEASGDLDRIAELIRATGD---DFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1899281696 241 FSLFEAMFLETNPIPVKKAAEMMGLvETGDVRLPLGALSEGNEEKLRAVLKGLG 294
Cdd:COG0329 237 LPLIRALFAEGNPAPVKAALALLGL-PSGPVRLPLLPLSEEERAELRAALKELG 289
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
6-293 |
1.56e-130 |
|
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: 372.05 E-value: 1.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 6 GVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCSK--VPVIAGTGSNNTK 83
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNgrVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 84 EAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELASEItNIKGVKE 163
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 164 ASGDLKQVGAIIrsvAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRLFSL 243
Cdd:TIGR00674 160 ATGNLERISEIK---AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1899281696 244 FEAMFLETNPIPVKKAAEMMGLVEtGDVRLPLGALSEGNEEKLRAVLKGL 293
Cdd:TIGR00674 237 HKALFIETNPIPVKTALALLGLIE-GELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
7-290 |
4.02e-119 |
|
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: 342.99 E-value: 4.02e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 7 VYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCS--KVPVIAGTGSNNTKE 84
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVagRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 85 AVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITNIKGVKEA 164
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLA-EHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 165 SGDLKQVGAIIRSVAEqglDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRLFSLF 244
Cdd:cd00408 160 SGDLDRLTRLIALLGP---DFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1899281696 245 EAMFLETNPIPVKKAAEMMGLvETGDVRLPLGALSEGNEEKLRAVL 290
Cdd:cd00408 237 EALFKEGNPAPVKAALALLGL-DAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
6-291 |
2.70e-106 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 310.84 E-value: 2.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 6 GVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCSK--VPVIAGTGSNNTK 83
Cdd:pfam00701 4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKgrIPVIAGVGSNSTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 84 EAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITNIKGVKE 163
Cdd:pfam00701 84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLA-TNPNIVGIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 164 ASGDLKQvgaIIRSVAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRLFSL 243
Cdd:pfam00701 163 ASGDLDR---MINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1899281696 244 FEAMFLETNPIPVKKAAEMMGLVETGDVRLPLGALSEGNEEKLRAVLK 291
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILK 287
|
|
| HpaI-NOT-DapA |
TIGR02313 |
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents a subset of the DapA ... |
4-296 |
1.12e-84 |
|
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents a subset of the DapA (dihydrodipicolinate synthase) family which has apparently evolved a separate function. The product of DapA, dihydrodipicolinate, results from the non-enzymatic cyclization and dehydration of 6-amino-2,4-dihydroxyhept-2-ene-1,7-dioic acid, which is different from the substrate of this reaction only in the presence of the amino group. In the absence of this amino group, and running the reaction in the opposite direction, the reaction corresponds to the HpaI aldolase component of the 4-hydroxyphenylacetic acid catabolism pathway (see TIGR02311). At present, this variant of DapA is found only in Oceanobacillus iheyensis HTE831 and Thermus thermophilus HB27. In both of these cases, one or more other DapA genes can be found and the one identified by this model is part of an operon for 4-hydroxyphenylacetic acid catabolism.
Pssm-ID: 131366 Cd Length: 294 Bit Score: 256.05 E-value: 1.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 4 IEGVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVD--CSKVPVIAGTGSNN 81
Cdd:TIGR02313 1 FRGSIAPLITPFKRNGDIDEEALRELIEFQIEGGSHAISVGGTSGEPGSLTLEERKQAIENAIDqiAGRIPFAPGTGALN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 82 TKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSV-EIPLILYNIPSRTAQNVNAGTMVELASEITNIKG 160
Cdd:TIGR02313 81 HDETLELTKFAEEAGADAAMVIVPYYNKPNQEALYDHFAEVADAVpDFPIIIYNIPGRAAQEIAPKTMARLRKDCPNIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 161 VKEASGDLKQVGaiiRSVAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRL 240
Cdd:TIGR02313 161 AKESNKDFEHLN---HLFLEAGRDFLLFCGIELLCLPMLAIGAAGSIAATANVEPKEVAELCEAAEAGDIKGAQDLHFEL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899281696 241 FSLFEAMFLETNPIPVKKAAEMMGLVETgDVRLPLGALSEGNEEKLRAVLKGLGMV 296
Cdd:TIGR02313 238 LEANDAIFKDTNPAPLKAALGMMGLIEK-ELRPPLGLPSDALEEEIRDMAEKYGKI 292
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
6-295 |
2.51e-75 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 231.84 E-value: 2.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 6 GVYPALITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDC--SKVPVIAGTGSNNTK 83
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCfgGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 84 EAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDsvEIPLILYNIPSRTAQNVNAGTMVELASEiTNIKGVKE 163
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAGVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 164 ASGDLKqvgaiIRSVAEQGldFTVVAGDDFLTLP-IMSLGGKGVISVAANIAPREMTEMvdaMLKGkveKAKEINIRLFS 242
Cdd:PLN02417 161 CTGNDR-----VKQYTEKG--ILLWSGNDDECHDaRWDYGADGVISVTSNLVPGLMHKL---MFAG---KNKELNDKLLP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1899281696 243 LFEAMFLETNPIPVKKAAEMMGLVETGdVRLPLGALSEGNEEKLRAVLKGLGM 295
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRPV-FRLPYVPLDLAKRAEFVALVKAIGR 279
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-291 |
2.21e-58 |
|
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: 188.67 E-value: 2.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 5 EGVYPALITPFTKDDEVDKEGLRRLVEYMIE-GGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCSK--VPVIAGTGSNN 81
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKgkVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 82 TKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSV-EIPLILYNIPSRTAQNVNAGTMVELAsEITNIKG 160
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAaSLPMIIYHIPALTGVNLTLEQFLELF-EIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 161 VKEASGDLKQVGaiiRSVAEQGLDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEINIRL 240
Cdd:cd00954 161 VKFTATDLYDLE---RIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1899281696 241 FSLFEAMfLETNPIPVKKAA-EMMGLvETGDVRLPLGALSEGNEEKLRAVLK 291
Cdd:cd00954 238 NDVITVL-IKNGLYPTLKAIlRLMGL-DAGPCRLPLRKVTEKALAKAKELAA 287
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-291 |
1.08e-46 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 158.62 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 1 MLKIEGVYPALITPFTKDDEVDKEGLRRLVEYMIEG-GVAGIVPCGTTGESATLSHKEHEEVIDVVVDCS--KVPVIAGT 77
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAkgKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 78 GSNNTKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNIPSRTAQNVNAGTMVELAsEITN 157
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELF-TLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 158 IKGVKEASGDLKQVGAIIRSVAeqglDFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEIN 237
Cdd:PRK04147 160 VIGVKQTAGDLYQLERIRKAFP----DKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1899281696 238 IRLFSLFEAMfLETNPIPVKKAA-EMMGlVETGDVRLPLGALSEGNEEKLRAVLK 291
Cdd:PRK04147 236 HECNDVIDLL-IKNGVYPGLKEIlHYMG-VDAGLCRKPFKPVDEKYLPALKALAA 288
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
12-292 |
2.83e-37 |
|
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: 133.99 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 12 ITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCS--KVPVIAGTGSNnTKEAVEFT 89
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETagRVPVLAGAGYG-TATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 90 KHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNipsRTAQNVNAGTMVELASEITNIKGVKEASGDlk 169
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAERCPNLVGFKDGVGD-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 170 qVGAIIRSVAEQGLDFTVVAGDDFLTLPIMSLGGKGVI---SVAANIAPREMTEMVDAMLKGKVEKAKEInIRLFslfea 246
Cdd:cd00951 163 -IELMRRIVAKLGDRLLYLGGLPTAEVFALAYLAMGVPtysSAVFNFVPEIALAFYAAVRAGDHATVKRL-LRDF----- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899281696 247 mFLETNPIP----------VKKAAEMMGLVeTGDVRLPLGALSEGNEEKLRAVLKG 292
Cdd:cd00951 236 -FLPYVDIRnrrkgyavsiVKAGARLVGRD-AGPVRPPLTDLTEEELAQLTALIKT 289
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
12-294 |
1.20e-31 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 119.15 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 12 ITPFTKDDEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCS--KVPVIAGTGSnNTKEAVEFT 89
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTagRVPVIAGAGG-GTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 90 KHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSVEIPLILYNipsRTAQNVNAGTMVELASEITNIKGVKEASGDLK 169
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAERCPNLVGFKDGVGDIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 170 QVGAIIRSVaeqgldftvvaGDDFLTL-----------PIMSLGGKGVISVAANIAPREMTEMVDAMLKGKVEKAKEInI 238
Cdd:PRK03620 172 LMQRIVRAL-----------GDRLLYLgglptaevfaaAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRL-L 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899281696 239 RLFslfeamFLETNPIP----------VKKAAEMMGLvETGDVRLPLGALSEGNEEKLRAVLKGLG 294
Cdd:PRK03620 240 DDF------FLPYVALRnrkkgyavsiVKAGARLVGL-DAGPVRAPLTDLTPEELAELAALIAKGG 298
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
1-292 |
3.67e-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: 101.30 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 1 MLKIEGVypalITPFTKDdEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDCSKvPVIAGTGSN 80
Cdd:cd00953 2 PDKITPV----ITPFTGN-KIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD-KVIFQVGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 81 NTKEAVEFTKHAADAGADACLLITPYYnkpnVKGLKE-----HFKRIgdSVEIPLILYNIPSRTAQNVNAGTMVELASEI 155
Cdd:cd00953 76 NLEESIELARAAKSFGIYAIASLPPYY----FPGIPEewlikYFTDI--SSPYPTFIYNYPKATGYDINARMAKEIKKAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 156 TNIKGVKEASGDlkqvgaIIRSVAEQGL--DFTVVAGDDFLTLPIMSLGGKGVISVAANIAPREMTEMVDAMlkgKVEKA 233
Cdd:cd00953 150 GDIIGVKDTNED------ISHMLEYKRLvpDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV---AIEDA 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899281696 234 KEINIRLFSLFEAM----FLETNPIPVKkaaEMMGlVETGDVRLPLGALSEGNEEKLRAVLKG 292
Cdd:cd00953 221 FKLQFLINEVLDASrkygSWSANYSLVK---IFQG-YDAGEPRPPFYPLDEEEEEKLRKEVNE 279
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
4-280 |
6.14e-20 |
|
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: 87.89 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 4 IEGVYPALITPFTKD-------DEVDKEGLRRLVEYMIEGGVAGIVPCGTTGESATLSHKEHEEVIDVVVDC--SKVPVI 74
Cdd:cd00952 2 IKGVWAIVPTPSKPDasdwratDTVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETvaGRVPVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 75 AGTGSNNTKEAVEFTKHAADAGADACLLITPYYNKPNVKGLKEHFKRIGDSV-EIPLILYNIPSRTAQNVNAGTMVELAs 153
Cdd:cd00952 82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDFPRAAWAELA- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 154 EITNIKGVKEASGdlkqVGAIIrsvaeqgLDFTVVAGD------DFLTLPIMSLGGKGVI---SVAANIAPREMTEMVDA 224
Cdd:cd00952 161 QIPQVVAAKYLGD----IGALL-------SDLAAVKGRmrllplEDDYYAAARLFPEEVTafwSSGAACGPAPVTALRDA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899281696 225 MLKGKVEKAKEINIRLFSLFEAMFLETN-------PIPVKKAA-EMMGLVETGDVRLPLGALSE 280
Cdd:cd00952 230 VATGDWTDARALTDRMRWAAEPLFPRGDfsefskyNIALEKARfDAAGYMRAGPARPPYNTAPE 293
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
22-214 |
1.42e-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: 38.85 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 22 DKEGLRRLVEYMIEGGVAGIVpcgTTGESATLSHKEheevidvvVDCSKVPVIA----GTGSNNTKEAVEFTKHAADAGA 97
Cdd:cd00945 11 TLEDIAKLCDEAIEYGFAAVC---VNPGYVRLAADA--------LAGSDVPVIVvvgfPTGLTTTEVKVAEVEEAIDLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899281696 98 DAcLLITPYYNKPNVKGLKEHFKRIGDSVE-----IPLILYNIPS--RTAQNVNAGTMVELASEITNIK---GVKEASGD 167
Cdd:cd00945 80 DE-IDVVINIGSLKEGDWEEVLEEIAAVVEaadggLPLKVILETRglKTADEIAKAARIAAEAGADFIKtstGFGGGGAT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1899281696 168 LKQVGAIIRSVAEQgldftvvagddfltLPIMSLGG-KGVISVAANIA 214
Cdd:cd00945 159 VEDVKLMKEAVGGR--------------VGVKAAGGiKTLEDALAAIE 192
|
|
| |
