|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
8-249 |
6.18e-117 |
|
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: 336.59 E-value: 6.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGrNKLDQIVIHVGA 87
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAA-KGKVTLIAHVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 88 LSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIQekIP 167
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELFE--IP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 168 TFQGLKFSDTDLLDFGQCVDQNrQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQK 247
Cdd:cd00954 157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235
|
..
gi 1811022937 248 KS 249
Cdd:cd00954 236 VI 237
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
7-248 |
3.86e-66 |
|
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: 207.70 E-value: 3.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 7 RLQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWV--TRGRNKldqIVIH 84
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLID-AGVDGLVVLGTTGESATLTDEERKRVLEAVVeaAAGRVP---VIAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 85 VGALSLKESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAAPaLPFYYYHIPALTGVKIRAE---ELLDg 161
Cdd:COG0329 77 VGSNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPEtlaRLAE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 162 iqekIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSS 241
Cdd:COG0329 154 ----IPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAE 228
|
....*..
gi 1811022937 242 ALNYQKK 248
Cdd:COG0329 229 ARALQDR 235
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
8-247 |
5.75e-48 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 160.93 E-value: 5.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCR----VAEEwvTRGRNKLdqiVI 83
Cdd:PRK04147 4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL---IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 84 HVGALSLKESQELAQHAAKIGADGIAVIAPFFLkPWNKDILVNFLKEVAAAApALPFYYYHIPALTGVKIRaeelLDGIQ 163
Cdd:PRK04147 79 QVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLS----LDQFN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 164 E--KIPTFQGLKFSDTDLLDFGQCvdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSS 241
Cdd:PRK04147 153 ElfTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQE 230
|
....*.
gi 1811022937 242 ALNYQK 247
Cdd:PRK04147 231 AQELQH 236
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
8-248 |
1.32e-43 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 149.44 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVT--RGRNKLdqiVIHV 85
Cdd:pfam00701 2 FSGIITALVTPFDTDGTLDFAALRQLIDFLIN-KGVDGLVVGGTTGESFTLSTEEREQLVEITVNeaKGRIPV---IAGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 86 GALSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAaPALPFYYYHIPALTGVKIRAEElldgIQE- 164
Cdd:pfam00701 78 GSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHF-KAIAEA-TDLPMILYNVPSRTGVDLTPET----VGRl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 165 -KIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSAL 243
Cdd:pfam00701 152 aTNPNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAA 230
|
....*
gi 1811022937 244 NYQKK 248
Cdd:pfam00701 231 LINHK 235
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-248 |
1.34e-28 |
|
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: 110.11 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 10 GLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGALS 89
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIE-NGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 90 LKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiQEKIPTF 169
Cdd:TIGR00674 79 TEEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHF-KAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811022937 170 QGLKFSDTDLLDFGQCVdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQKK 248
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
8-249 |
6.18e-117 |
|
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: 336.59 E-value: 6.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGrNKLDQIVIHVGA 87
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAA-KGKVTLIAHVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 88 LSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIQekIP 167
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELFE--IP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 168 TFQGLKFSDTDLLDFGQCVDQNrQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQK 247
Cdd:cd00954 157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235
|
..
gi 1811022937 248 KS 249
Cdd:cd00954 236 VI 237
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
7-248 |
3.86e-66 |
|
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: 207.70 E-value: 3.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 7 RLQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWV--TRGRNKldqIVIH 84
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLID-AGVDGLVVLGTTGESATLTDEERKRVLEAVVeaAAGRVP---VIAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 85 VGALSLKESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAAPaLPFYYYHIPALTGVKIRAE---ELLDg 161
Cdd:COG0329 77 VGSNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPEtlaRLAE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 162 iqekIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSS 241
Cdd:COG0329 154 ----IPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAE 228
|
....*..
gi 1811022937 242 ALNYQKK 248
Cdd:COG0329 229 ARALQDR 235
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
11-248 |
7.17e-65 |
|
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: 203.93 E-value: 7.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 11 LVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGALSL 90
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIE-AGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRV-PVIAGVGANST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 91 KESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAaPALPFYYYHIPALTGVKIRAEELLDGIQekIPTFQ 170
Cdd:cd00408 79 REAIELARHAEEAGADGVLVVPPYYNKP-SQEGIVAHFKAVADA-SDLPVILYNIPGRTGVDLSPETIARLAE--HPNIV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811022937 171 GLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQKK 248
Cdd:cd00408 155 GIKDSSGDLDRLTRLIALLGPD-FAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDR 231
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
8-247 |
5.75e-48 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 160.93 E-value: 5.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCR----VAEEwvTRGRNKLdqiVI 83
Cdd:PRK04147 4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL---IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 84 HVGALSLKESQELAQHAAKIGADGIAVIAPFFLkPWNKDILVNFLKEVAAAApALPFYYYHIPALTGVKIRaeelLDGIQ 163
Cdd:PRK04147 79 QVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLS----LDQFN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 164 E--KIPTFQGLKFSDTDLLDFGQCvdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSS 241
Cdd:PRK04147 153 ElfTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQE 230
|
....*.
gi 1811022937 242 ALNYQK 247
Cdd:PRK04147 231 AQELQH 236
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
8-248 |
1.32e-43 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 149.44 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVT--RGRNKLdqiVIHV 85
Cdd:pfam00701 2 FSGIITALVTPFDTDGTLDFAALRQLIDFLIN-KGVDGLVVGGTTGESFTLSTEEREQLVEITVNeaKGRIPV---IAGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 86 GALSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAaPALPFYYYHIPALTGVKIRAEElldgIQE- 164
Cdd:pfam00701 78 GSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHF-KAIAEA-TDLPMILYNVPSRTGVDLTPET----VGRl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 165 -KIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSAL 243
Cdd:pfam00701 152 aTNPNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAA 230
|
....*
gi 1811022937 244 NYQKK 248
Cdd:pfam00701 231 LINHK 235
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
8-248 |
2.20e-34 |
|
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: 125.30 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAE---EWVtRGRNKldqIVIH 84
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIE-NGTDGLVVCGTTGESPTLSDEEHEAVIEavvEAV-NGRVP---VIAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 85 VGALSLKESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLdgIQE 164
Cdd:cd00950 76 TGSNNTAEAIELTKRAEKAGADAALVVTPYYNKP-SQEGLYAHFKAIAEATD-LPVILYNVPGRTGVNIEPETVL--RLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 165 KIPTFQGLKFSDTDlLDFGQCVDQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALN 244
Cdd:cd00950 152 EHPNIVGIKEATGD-LDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARE 230
|
....
gi 1811022937 245 YQKK 248
Cdd:cd00950 231 LHRK 234
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-248 |
1.34e-28 |
|
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: 110.11 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 10 GLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGALS 89
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIE-NGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 90 LKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiQEKIPTF 169
Cdd:TIGR00674 79 TEEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHF-KAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811022937 170 QGLKFSDTDLLDFGQCVdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQKK 248
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
12-247 |
1.38e-22 |
|
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188640 Cd Length: 279 Bit Score: 93.99 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 12 VAATITPMTEhGEINFSVIGQYVDYLVEEqGVKNIFVNGTTGEGLSLSISERCRVAEEWVtrgrNKLDQIVIHVGALSLK 91
Cdd:cd00953 5 ITPVITPFTG-NKIDKEKFKKHCENLISK-GIDYVFVAGTTGLGPSLSFQEKLELLKAYS----DITDKVIFQVGSLNLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 92 ESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFLKEVAAaapALPFYYYHIPALTGVKIRAeELLDGIQEKIPTFQG 171
Cdd:cd00953 79 ESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISS---PYPTFIYNYPKATGYDINA-RMAKEIKKAGGDIIG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811022937 172 LK---FSDTDLLDFGQCVDqnrqrQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDfssALNYQK 247
Cdd:cd00953 155 VKdtnEDISHMLEYKRLVP-----DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIED---AFKLQF 225
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
9-243 |
5.40e-14 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 70.06 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 9 QGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGAL 88
Cdd:PLN02417 3 LRLITAIKTPYLPDGRFDLEAYDSLVNMQIE-NGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKI-KVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 89 SLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlkevAAAAPALPFYYYHIPALTGVKIraeelLDGIQEKI-- 166
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHF----ETVLDMGPTIIYNVPGRTGQDI-----PPEVIFKIaq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 167 -PTFQGLKfsdtdlldfgQCVDQNRQRQFA---FLF--GVDEQLLSA-LVMGATGAVGSTYNYLGKKTNQMLEAFERKDF 239
Cdd:PLN02417 152 hPNFAGVK----------ECTGNDRVKQYTekgILLwsGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFAGKNKEL 221
|
....
gi 1811022937 240 SSAL 243
Cdd:PLN02417 222 NDKL 225
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
10-180 |
2.36e-08 |
|
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: 53.86 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 10 GLVAATITPMTEHGEINFSVIGQYVDYLVEEqGVKNIFVNGTTGEGLSLSISE--RC-RVAEEwVTRGRnkldqIVIHVG 86
Cdd:cd00951 3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSY-GAAALFAAGGTGEFFSLTPDEyaQVvRAAVE-ETAGR-----VPVLAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 87 A-LSLKESQELAQHAAKIGADGIaVIAPFFLKPWNKDILVNFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGIQEK 165
Cdd:cd00951 76 AgYGTATAIAYAQAAEKAGADGI-LLLPPYLTEAPQEGLYAHVEAVCKSTD-LGVIVYN----RANAVLTADSLARLAER 149
|
170
....*....|....*..
gi 1811022937 166 IPTFQGLK--FSDTDLL 180
Cdd:cd00951 150 CPNLVGFKdgVGDIELM 166
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
34-146 |
1.17e-06 |
|
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: 48.98 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 34 VDYLVEEqGVKNIFVNGTTGEGLSLSISER----CRVAEewVTRGRnkldqIVIHVGALSL--KESQELAQHAAKIGADG 107
Cdd:cd00952 35 VERLIAA-GVDGILTMGTFGECATLTWEEKqafvATVVE--TVAGR-----VPVFVGATTLntRDTIARTRALLDLGADG 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 1811022937 108 IAVIAPFFLKPwNKDILVNFLKEVAAAAPALPFYYYHIP 146
Cdd:cd00952 107 TMLGRPMWLPL-DVDTAVQFYRDVAEAVPEMAIAIYANP 144
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
10-173 |
2.19e-06 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 47.89 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 10 GLVAATITPMTEHGEINFSVIGQYVDYLVEEqGVKNIFVNGTTGEGLSLSISE--RC-RVAEEwVTRGRnkldqIVIHVG 86
Cdd:PRK03620 10 GLLSFPVTPFDADGSFDEAAYREHLEWLAPY-GAAALFAAGGTGEFFSLTPDEysQVvRAAVE-TTAGR-----VPVIAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022937 87 A-LSLKESQELAQHAAKIGADGIAVIAPfFLKPWNKDILVNFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGIQEK 165
Cdd:PRK03620 83 AgGGTAQAIEYAQAAERAGADGILLLPP-YLTEAPQEGLAAHVEAVCKSTD-LGVIVYN----RDNAVLTADTLARLAER 156
|
....*...
gi 1811022937 166 IPTFQGLK 173
Cdd:PRK03620 157 CPNLVGFK 164
|
|
|