|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-293 |
0e+00 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 522.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 1 MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQV 80
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 81 GSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKV 160
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 161 LGVKFTAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTND 240
Cdd:PRK04147 161 IGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECND 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
1F6P_C 241 LIEGILANGLYLTIKELLKLEGVDAGYCREPMtSKATAEQVAKAKDLKAKFLS 293
Cdd:PRK04147 241 VIDLLIKNGVYPGLKEILHYMGVDAGLCRKPF-KPVDEKYLPALKALAAKYLK 292
|
|
| nanA |
TIGR00683 |
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid ... |
4-292 |
3.41e-178 |
|
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid aldolase, sialic acid aldolase, or sialate lyase. It is an intracellular enzyme. The structure of this homotetrameric enzyme related to dihydrodipicolinate synthase is known. In Clostridium tertium, the enzyme appears to be in an operon with a secreted sialidase that releases sialic acid from host sialoglycoconjugates. In several E. coli strains, however, this enzyme is responsible for N-acetyl-D-neuraminic acid synthesis for capsule production by condensing N-acetyl-D-mannosamine and pyruvate. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273217 Cd Length: 293 Bit Score: 492.93 E-value: 3.41e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 4 LKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMkVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSV 83
Cdd:TIGR00683 1 LRGVMAALLTPFDQQQALDKASLRRLVQFNIQQG-IDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 84 NLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGS-NMIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:TIGR00683 80 NTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGlPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLI 242
Cdd:TIGR00683 160 LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
1F6P_C 243 EGILANGLYLTIKELLK-LEGVDAGYCREPMT---SKATAEQVAKAKDLKAKFL 292
Cdd:TIGR00683 240 DLLIKTGVFRGLKTVLHyMDVVSVPLCRKPFGpvdEKYLPELKALAQQLMQERG 293
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
4-290 |
1.19e-158 |
|
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: 443.29 E-value: 1.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 4 LKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSV 83
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 84 NLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSN-MIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLpMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKKAYP-NHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDL 241
Cdd:cd00954 161 VKFTATDLYDLERIRAASPeDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
1F6P_C 242 IEGILANGLYLTIKELLKLEGVDAGYCREPMTsKATAEQVAKAKDLKAK 290
Cdd:cd00954 241 ITVLIKNGLYPTLKAILRLMGLDAGPCRLPLR-KVTEKALAKAKELAAK 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-290 |
2.60e-141 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 399.43 E-value: 2.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 3 DLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMkVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGS 82
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKG-VDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 83 VNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:pfam00701 80 NSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKK-AYPNHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDL 241
Cdd:pfam00701 160 IKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
1F6P_C 242 IEGILANGLYLTIKELLKLEGVDAG-YCREPMTSKATAEQVAKAKDLKAK 290
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGpTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-284 |
7.81e-88 |
|
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: 263.94 E-value: 7.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 3 DLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGS 82
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDA-GVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 83 VNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:COG0329 80 NSTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKKAYPNHL-IWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDL 241
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFaVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
1F6P_C 242 IEGILANGLYLTIKELLKLEGVDAGYCREPMT--SKATAEQVAKA 284
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLplSEEERAELRAA 284
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
1-293 |
0e+00 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 522.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 1 MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQV 80
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 81 GSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKV 160
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 161 LGVKFTAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTND 240
Cdd:PRK04147 161 IGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECND 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
1F6P_C 241 LIEGILANGLYLTIKELLKLEGVDAGYCREPMtSKATAEQVAKAKDLKAKFLS 293
Cdd:PRK04147 241 VIDLLIKNGVYPGLKEILHYMGVDAGLCRKPF-KPVDEKYLPALKALAAKYLK 292
|
|
| nanA |
TIGR00683 |
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid ... |
4-292 |
3.41e-178 |
|
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid aldolase, sialic acid aldolase, or sialate lyase. It is an intracellular enzyme. The structure of this homotetrameric enzyme related to dihydrodipicolinate synthase is known. In Clostridium tertium, the enzyme appears to be in an operon with a secreted sialidase that releases sialic acid from host sialoglycoconjugates. In several E. coli strains, however, this enzyme is responsible for N-acetyl-D-neuraminic acid synthesis for capsule production by condensing N-acetyl-D-mannosamine and pyruvate. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273217 Cd Length: 293 Bit Score: 492.93 E-value: 3.41e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 4 LKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMkVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSV 83
Cdd:TIGR00683 1 LRGVMAALLTPFDQQQALDKASLRRLVQFNIQQG-IDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 84 NLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGS-NMIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:TIGR00683 80 NTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGlPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLI 242
Cdd:TIGR00683 160 LKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
1F6P_C 243 EGILANGLYLTIKELLK-LEGVDAGYCREPMT---SKATAEQVAKAKDLKAKFL 292
Cdd:TIGR00683 240 DLLIKTGVFRGLKTVLHyMDVVSVPLCRKPFGpvdEKYLPELKALAQQLMQERG 293
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
4-290 |
1.19e-158 |
|
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: 443.29 E-value: 1.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 4 LKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSV 83
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 84 NLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSN-MIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLpMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKKAYP-NHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDL 241
Cdd:cd00954 161 VKFTATDLYDLERIRAASPeDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
1F6P_C 242 IEGILANGLYLTIKELLKLEGVDAGYCREPMTsKATAEQVAKAKDLKAK 290
Cdd:cd00954 241 ITVLIKNGLYPTLKAILRLMGLDAGPCRLPLR-KVTEKALAKAKELAAK 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
3-290 |
2.60e-141 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 399.43 E-value: 2.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 3 DLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMkVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGS 82
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKG-VDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 83 VNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:pfam00701 80 NSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKK-AYPNHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDL 241
Cdd:pfam00701 160 IKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
1F6P_C 242 IEGILANGLYLTIKELLKLEGVDAG-YCREPMTSKATAEQVAKAKDLKAK 290
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGpTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
7-287 |
6.65e-89 |
|
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: 266.34 E-value: 6.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 7 IFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSVNLK 86
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEA-GVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 87 EAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLGVKFT 166
Cdd:cd00408 80 EAIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 167 AGDFYLLERLKKAYPNHL-IWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLIEGI 245
Cdd:cd00408 160 SGDLDRLTRLIALLGPDFaVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
1F6P_C 246 LANGLYLTIKELLKLEGVDAGYCREPMTsKATAEQVAKAKDL 287
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLV-PLSEEERAKLEAL 280
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
3-284 |
7.81e-88 |
|
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: 263.94 E-value: 7.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 3 DLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGS 82
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDA-GVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 83 VNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLG 162
Cdd:COG0329 80 NSTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 163 VKFTAGDFYLLERLKKAYPNHL-IWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDL 241
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFaVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
1F6P_C 242 IEGILANGLYLTIKELLKLEGVDAGYCREPMT--SKATAEQVAKA 284
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLplSEEERAELRAA 284
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
4-287 |
1.55e-57 |
|
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: 186.16 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 4 LKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSV 83
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIEN-GTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 84 NLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLGV 163
Cdd:cd00950 80 NTAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 164 KFTAGDFYLLERLKKAYPNHL-IWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLI 242
Cdd:cd00950 160 KEATGDLDRVSELIALCPDDFaVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
1F6P_C 243 EGILANGLYLTIKELLKLEGVDAGYCREPMTSkATAEQVAKAKDL 287
Cdd:cd00950 240 KALFAEPNPIPVKAALALLGLISGELRLPLVP-LSEELRAKLRAA 283
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
6-284 |
5.46e-46 |
|
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: 156.33 E-value: 5.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 6 GIFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSVNL 85
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIEN-GTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 86 KEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLGVKF 165
Cdd:TIGR00674 80 EEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 166 TAGDFYLLERLKKAYPNHL-IWAGFDEMMLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHvtnDLIEg 244
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFvVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQ---KLMP- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
1F6P_C 245 iLANGLYLT-----IKELLKLEGVDAGYCREPMT--SKATAEQVAKA 284
Cdd:TIGR00674 236 -LHKALFIEtnpipVKTALALLGLIEGELRLPLTelSEEHRNKLRDV 281
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
39-271 |
1.28e-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: 94.37 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 39 VDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDqiaLIAQVGSVNLKEAVELGKYATELGYDCLSAVTPFYYKfSFPE- 117
Cdd:cd00953 34 IDYVFVAGTTGLGPSLSFQEKLELLKAYSDITDK---VIFQVGSLNLEESIELARAAKSFGIYAIASLPPYYFP-GIPEe 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 118 -IKHYYDTIIAETgsNMIVYSIPFLTGVNMGIEQFGELYKNPK-VLGVKFTAGDFYLLERLKKAYPNHLIWAGFDEMMLP 195
Cdd:cd00953 110 wLIKYFTDISSPY--PTFIYNYPKATGYDINARMAKEIKKAGGdIIGVKDTNEDISHMLEYKRLVPDFKVYSGPDSLIFS 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1F6P_C 196 AASLGVDGAIGSTFNVNGVRARQIFELTKAgklKEALEIQHVTNDLIEGILANGLYLTIKELLK-LEGVDAGYCREP 271
Cdd:cd00953 188 ALRSGLDGSVAAASNYLPEVFVKIKDHVAI---EDAFKLQFLINEVLDASRKYGSWSANYSLVKiFQGYDAGEPRPP 261
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
6-230 |
2.75e-22 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 93.55 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 6 GIFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSVNL 85
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIEN-GAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 86 KEAVELGKYATELGYDCLSAVTPFYYKFSFPE-IKHYYDTiiAETGSnMIVYSIPFLTGVNMGIEQFGELYKNPKVLGVK 164
Cdd:PLN02417 83 REAIHATEQGFAVGMHAALHINPYYGKTSQEGlIKHFETV--LDMGP-TIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1F6P_C 165 FTAGDfyllERLKKAYPNH-LIWAGFDEMMLPAA-SLGVDGAIGSTFNvngVRARQIFELTKAGKLKE 230
Cdd:PLN02417 160 ECTGN----DRVKQYTEKGiLLWSGNDDECHDARwDYGADGVISVTSN---LVPGLMHKLMFAGKNKE 220
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
6-188 |
3.33e-12 |
|
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: 65.42 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 6 GIFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSvNL 85
Cdd:cd00951 3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSY-GAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 86 KEAVELGKYATELGYDCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSipfLTGVNMGIEQFGELYKN-PKVLGVK 164
Cdd:cd00951 81 ATAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAERcPNLVGFK 157
|
170 180
....*....|....*....|....
1F6P_C 165 FTAGDFYLLERLKKAYPNHLIWAG 188
Cdd:cd00951 158 DGVGDIELMRRIVAKLGDRLLYLG 181
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
6-290 |
6.61e-10 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 58.67 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 6 GIFSALLVSFNEDGTINEKGLRQIIRHNIDKmKVDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSvNL 85
Cdd:PRK03620 10 GLLSFPVTPFDADGSFDEAAYREHLEWLAPY-GAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 86 KEAVELGKYATELGYDCLsAVTPFYYKFSFPE-IKHYYDTIIAETGSNMIVYsipfltgvNMGIEQFGE------LYKNP 158
Cdd:PRK03620 88 AQAIEYAQAAERAGADGI-LLLPPYLTEAPQEgLAAHVEAVCKSTDLGVIVY--------NRDNAVLTAdtlarlAERCP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 159 KVLGVKFTAGDFYLLERLKKAYPNHLIWAG---FDEM-MLPAASLGVDGAIGSTFNVNGVRARQIFELTKAGKlkealei 234
Cdd:PRK03620 159 NLVGFKDGVGDIELMQRIVRALGDRLLYLGglpTAEVfAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGD------- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1F6P_C 235 qhvtNDLIEGILaNGLYLTIKEL---------------LKLEGVDAGYCREPMTSkATAEQVAKAKDLKAK 290
Cdd:PRK03620 232 ----HATVDRLL-DDFFLPYVALrnrkkgyavsivkagARLVGLDAGPVRAPLTD-LTPEELAELAALIAK 296
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
39-206 |
1.92e-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: 48.60 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 39 VDGLYVGGSTGENFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSVNLKEAVELGKYATELGYDCLSAVTPFYYKFSFPEI 118
Cdd:cd00952 43 VDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F6P_C 119 KHYYDTiIAET--GSNMIVYSIPFLTGVNMGIEQFGELYKNPKVLGVKFTAGDFYLLERLKKAYPNHLIWAgFDEMMLPA 196
Cdd:cd00952 123 VQFYRD-VAEAvpEMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKYLGDIGALLSDLAAVKGRMRLLP-LEDDYYAA 200
|
170
....*....|
1F6P_C 197 ASLGVDGAIG 206
Cdd:cd00952 201 ARLFPEEVTA 210
|
|
| |
