|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
8-218 |
1.68e-104 |
|
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: 303.46 E-value: 1.68e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 8 LQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGA 87
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 88 LSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIldKIP 167
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELF--EIP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 318037616 168 TFQGLKFSDTDLLDFGQCVDQNrQQQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:cd00954 157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGS 206
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
7-219 |
1.74e-60 |
|
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: 191.52 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLDgiLDKI 166
Cdd:COG0329 79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLAR--LAEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318037616 167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGSF 219
Cdd:COG0329 155 PNIVGIKEASGDLDRIAELIRATG-DDFAVLSGDDALALPALALGADGVISVT 206
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
6-218 |
1.39e-43 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 148.22 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 6 KKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQ----VAEEwvTKGKDKLdqv 81
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 82 IIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLkPWTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELldG 161
Cdd:PRK04147 77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLSLDQF--N 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 318037616 162 ILDKIPTFQGLKFSDTDLLDFGQCvdQNRQQQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:PRK04147 153 ELFTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGS 207
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-218 |
5.54e-40 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 138.65 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDiLINFLKEVaAAAPALPFYYYHIPALTGVKIRAEELldGILDKI 166
Cdd:pfam00701 79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEG-LYQHFKAI-AEATDLPMILYNVPSRTGVDLTPETV--GRLATN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 318037616 167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:pfam00701 155 PNIVGIKEASGDLDRMINIKKEAG-PDFVILSGDDETMLPALSLGADGVISV 205
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-216 |
5.52e-26 |
|
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: 102.02 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 10 GLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGALS 89
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 90 LKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiLDKIPTF 169
Cdd:TIGR00674 79 TEEAISLTKFAEDVGADGFLVVTPYYNKP-TQEGLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 318037616 170 QGLKFSDTDLLDFGQCVdQNRQQQFAFLFGVDEQLLSALVMGATGAV 216
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVI 200
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
8-218 |
1.68e-104 |
|
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: 303.46 E-value: 1.68e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 8 LQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGA 87
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 88 LSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIldKIP 167
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELF--EIP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 318037616 168 TFQGLKFSDTDLLDFGQCVDQNrQQQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:cd00954 157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGS 206
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
7-219 |
1.74e-60 |
|
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: 191.52 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLDgiLDKI 166
Cdd:COG0329 79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLAR--LAEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 318037616 167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGSF 219
Cdd:COG0329 155 PNIVGIKEASGDLDRIAELIRATG-DDFAVLSGDDALALPALALGADGVISVT 206
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
11-218 |
6.09e-58 |
|
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: 184.67 E-value: 6.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 11 LVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGALSL 90
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLI-EAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRV-PVIAGVGANST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 91 KESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVaAAAPALPFYYYHIPALTGVKIRAEELLDgiLDKIPTFQ 170
Cdd:cd00408 79 REAIELARHAEEAGADGVLVVPPYYNKP-SQEGIVAHFKAV-ADASDLPVILYNIPGRTGVDLSPETIAR--LAEHPNIV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 318037616 171 GLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:cd00408 155 GIKDSSGDLDRLTRLIALLG-PDFAVLSGDDDLLLPALALGADGAISG 201
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
6-218 |
1.39e-43 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 148.22 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 6 KKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQ----VAEEwvTKGKDKLdqv 81
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 82 IIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLkPWTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELldG 161
Cdd:PRK04147 77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLSLDQF--N 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 318037616 162 ILDKIPTFQGLKFSDTDLLDFGQCvdQNRQQQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:PRK04147 153 ELFTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGS 207
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-218 |
5.54e-40 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 138.65 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDiLINFLKEVaAAAPALPFYYYHIPALTGVKIRAEELldGILDKI 166
Cdd:pfam00701 79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEG-LYQHFKAI-AEATDLPMILYNVPSRTGVDLTPETV--GRLATN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 318037616 167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:pfam00701 155 PNIVGIKEASGDLDRMINIKKEAG-PDFVILSGDDETMLPALSLGADGVISV 205
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
8-216 |
1.42e-32 |
|
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: 119.14 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 8 LQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGA 87
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQI-ENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRV-PVIAGTGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 88 LSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLdgILDKIP 167
Cdd:cd00950 79 NNTAEAIELTKRAEKAGADAALVVTPYYNKP-SQEGLYAHFKAIAEATD-LPVILYNVPGRTGVNIEPETVL--RLAEHP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 318037616 168 TFQGLKFSDTDlLDFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAV 216
Cdd:cd00950 155 NIVGIKEATGD-LDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVI 202
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-216 |
5.52e-26 |
|
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: 102.02 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 10 GLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGALS 89
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 90 LKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiLDKIPTF 169
Cdd:TIGR00674 79 TEEAISLTKFAEDVGADGFLVVTPYYNKP-TQEGLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 318037616 170 QGLKFSDTDLLDFGQCVdQNRQQQFAFLFGVDEQLLSALVMGATGAV 216
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVI 200
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
12-218 |
7.38e-20 |
|
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: 85.51 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 12 VAATITPMTENgEINFSVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERRQVAEEWvtkgKDKLDQVIIHVGALSLK 91
Cdd:cd00953 5 ITPVITPFTGN-KIDKEKFKKHCENLISK-GIDYVFVAGTTGLGPSLSFQEKLELLKAY----SDITDKVIFQVGSLNLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 92 ESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFLKEVAAaapALPFYYYHIPALTGVKIRAeELLDGILDKIPTFQG 171
Cdd:cd00953 79 ESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISS---PYPTFIYNYPKATGYDINA-RMAKEIKKAGGDIIG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 318037616 172 LK---FSDTDLLDFGQCVDqnrqqQFAFLFGVDEQLLSALVMGATGAVGS 218
Cdd:cd00953 155 VKdtnEDISHMLEYKRLVP-----DFKVYSGPDSLIFSALRSGLDGSVAA 199
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
7-195 |
3.45e-18 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 80.84 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQI-ENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKI-KVIGNTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPALpfyYYHIPALTGVKIRAEELldGILDKI 166
Cdd:PLN02417 79 SNSTREAIHATEQGFAVGMHAALHINPYYGKT-SQEGLIKHFETVLDMGPTI---IYNVPGRTGQDIPPEVI--FKIAQH 152
|
170 180
....*....|....*....|....*....
gi 318037616 167 PTFQGLKfsdtdlldfgQCVDQNRQQQFA 195
Cdd:PLN02417 153 PNFAGVK----------ECTGNDRVKQYT 171
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
10-180 |
4.68e-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: 52.32 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 10 GLVAATITPMTENGEINFSVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERRQVAEEWV--TKGKdkldqVIIHVGA 87
Cdd:cd00951 3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSY-GAAALFAAGGTGEFFSLTPDEYAQVVRAAVeeTAGR-----VPVLAGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 88 -LSLKESQELAQHAAEIGADGIaVIAPFFLKPWTKDILINFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGILDKI 166
Cdd:cd00951 77 gYGTATAIAYAQAAEKAGADGI-LLLPPYLTEAPQEGLYAHVEAVCKSTD-LGVIVYN----RANAVLTADSLARLAERC 150
|
170
....*....|....*.
gi 318037616 167 PTFQGLK--FSDTDLL 180
Cdd:cd00951 151 PNLVGFKdgVGDIELM 166
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
10-173 |
1.44e-07 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 50.97 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 10 GLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQV---AEEwVTKGKdkldqVIIHVG 86
Cdd:PRK03620 10 GLLSFPVTPFDADGSFDEAAYREHLEWLA-PYGAAALFAAGGTGEFFSLTPDEYSQVvraAVE-TTAGR-----VPVIAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 87 A-LSLKESQELAQHAAEIGADGIAVIAPfFLKPWTKDILINFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGILDK 165
Cdd:PRK03620 83 AgGGTAQAIEYAQAAERAGADGILLLPP-YLTEAPQEGLAAHVEAVCKSTD-LGVIVYN----RDNAVLTADTLARLAER 156
|
....*...
gi 318037616 166 IPTFQGLK 173
Cdd:PRK03620 157 CPNLVGFK 164
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
8-146 |
1.39e-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: 48.21 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037616 8 LQGLVAATITPMTENGE-------INFSVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERR----QVAEewVTKGKd 76
Cdd:cd00952 2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAA-GVDGILTMGTFGECATLTWEEKQafvaTVVE--TVAGR- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318037616 77 kldqVIIHVGALSL--KESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPALPFYYYHIP 146
Cdd:cd00952 78 ----VPVFVGATTLntRDTIARTRALLDLGADGTMLGRPMWLPL-DVDTAVQFYRDVAEAVPEMAIAIYANP 144
|
|
|