|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
8-306 |
1.54e-131 |
|
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: 375.88 E-value: 1.54e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 8 LRGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGrNKLDQVVIHVGA 87
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAA-KGKVTLIAHVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 88 LNVKESQELAQHAAEIGADGIAVIAPFFFKSqNKDALISFLREVAAAAPTLPFYYYHMPSMTGVKIRAEELLDGIQdkIP 167
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKF-SFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFE--IP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 168 TFQGLKFTDTDLLDFGQCVDQnHQRQFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQF 247
Cdd:cd00954 157 NVIGVKFTATDLYDLERIRAA-SPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21311855 248 RIQRFINYVIKLGFgVSQTKAIMTLVsGIPMGPPRLPLQKATQeftaKAEAKLKSLDFL 306
Cdd:cd00954 236 VINDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPLRKVTE----KALAKAKELAAK 288
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
7-306 |
1.96e-80 |
|
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: 245.83 E-value: 1.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 7 KLRGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVG 86
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 87 ALNVKESQELAQHAAEIGADGIAVIAPFFFK-SQnkDALISFLREVAAAAPtLPFYYYHMPSMTGVKIRAEELLDGIqdK 165
Cdd:COG0329 79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKpTQ--EGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLA--E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 166 IPTFQGLKFTDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSY 245
Cdd:COG0329 154 IPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21311855 246 QFRIQRFINYVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKLKSLDFL 306
Cdd:COG0329 233 QDRLLPLIRALFAEG-NPAPVKAALALL-GLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
6-298 |
3.34e-57 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 186.35 E-value: 3.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 6 KKLRGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQ----VAEEwvNQGRNKLdqv 81
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 82 VIHVGALNVKESQELAQHAAEIGADGIAVIAPFFFK---SQNKDalisFLREVAAAApTLPFYYYHMPSMTGVKIRAE-- 156
Cdd:PRK04147 77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYYPfsfEEICD----YYREIIDSA-DNPMIVYNIPALTGVNLSLDqf 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 157 -ELLdgiqdKIPTFQGLKFTDTDLLDFGQcVDQNHQRQFaLLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFE 235
Cdd:PRK04147 152 nELF-----TLPKVIGVKQTAGDLYQLER-IRKAFPDKL-IYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21311855 236 QKDLASALSYQFRIQRFINYVIKLgfGVSQT-KAIMTLVsGIPMGPPRLPLQKATQEFTAKAEA 298
Cdd:PRK04147 225 AGDIQEAQELQHECNDVIDLLIKN--GVYPGlKEILHYM-GVDAGLCRKPFKPVDEKYLPALKA 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-303 |
6.87e-51 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 170.24 E-value: 6.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 7 KLRGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVG 86
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 87 ALNVKESQELAQHAAEIGADGIAVIAPFFFK-SQnkDALISFLREVAAAaPTLPFYYYHMPSMTGVKIRAEELldGIQDK 165
Cdd:pfam00701 79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKpSQ--EGLYQHFKAIAEA-TDLPMILYNVPSRTGVDLTPETV--GRLAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 166 IPTFQGLKFTDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSY 245
Cdd:pfam00701 154 NPNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21311855 246 QFRIQRFINYVIKLGFgVSQTKAIMTLVsGIPMGP-PRLPLQKATQEFTAKAEAKLKSL 303
Cdd:pfam00701 233 NHKLLPLIKILFAEPN-PIPIKTALELL-GLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-303 |
2.53e-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: 110.50 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 10 GLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVGALN 89
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 90 VKESQELAQHAAEIGADGIAVIAPFFFK-SQNkdALISFLREVAAAApTLPFYYYHMPSMTGVKIRAEELLDGIqdKIPT 168
Cdd:TIGR00674 79 TEEAISLTKFAEDVGADGFLVVTPYYNKpTQE--GLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKRLA--EEPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 169 FQGLKFTDTDLLDFGQCVdQNHQRQFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFR 248
Cdd:TIGR00674 154 IVAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 21311855 249 IQRFIN--YVIKLGFGVsqtKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKLKSL 303
Cdd:TIGR00674 233 LMPLHKalFIETNPIPV---KTALALL-GLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
8-306 |
1.54e-131 |
|
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: 375.88 E-value: 1.54e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 8 LRGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGrNKLDQVVIHVGA 87
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAA-KGKVTLIAHVGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 88 LNVKESQELAQHAAEIGADGIAVIAPFFFKSqNKDALISFLREVAAAAPTLPFYYYHMPSMTGVKIRAEELLDGIQdkIP 167
Cdd:cd00954 80 LNLKESQELAKHAEELGYDAISAITPFYYKF-SFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFE--IP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 168 TFQGLKFTDTDLLDFGQCVDQnHQRQFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQF 247
Cdd:cd00954 157 NVIGVKFTATDLYDLERIRAA-SPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21311855 248 RIQRFINYVIKLGFgVSQTKAIMTLVsGIPMGPPRLPLQKATQeftaKAEAKLKSLDFL 306
Cdd:cd00954 236 VINDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPLRKVTE----KALAKAKELAAK 288
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
7-306 |
1.96e-80 |
|
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: 245.83 E-value: 1.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 7 KLRGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVG 86
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 87 ALNVKESQELAQHAAEIGADGIAVIAPFFFK-SQnkDALISFLREVAAAAPtLPFYYYHMPSMTGVKIRAEELLDGIqdK 165
Cdd:COG0329 79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKpTQ--EGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLA--E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 166 IPTFQGLKFTDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSY 245
Cdd:COG0329 154 IPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21311855 246 QFRIQRFINYVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKLKSLDFL 306
Cdd:COG0329 233 QDRLLPLIRALFAEG-NPAPVKAALALL-GLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
11-300 |
6.19e-78 |
|
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: 239.37 E-value: 6.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 11 LVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVGALNV 90
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLI-EAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRV-PVIAGVGANST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 91 KESQELAQHAAEIGADGIAVIAPFFFKsQNKDALISFLREVAAAAPtLPFYYYHMPSMTGVKIRAEELLDGIQdkIPTFQ 170
Cdd:cd00408 79 REAIELARHAEEAGADGVLVVPPYYNK-PSQEGIVAHFKAVADASD-LPVILYNIPGRTGVDLSPETIARLAE--HPNIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 171 GLKFTDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRIQ 250
Cdd:cd00408 155 GIKDSSGDLDRLTRLIALLGPD-FAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 21311855 251 RFINYVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKL 300
Cdd:cd00408 234 PLIEALFKEG-NPAPVKAALALL-GLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
6-298 |
3.34e-57 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 186.35 E-value: 3.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 6 KKLRGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQ----VAEEwvNQGRNKLdqv 81
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 82 VIHVGALNVKESQELAQHAAEIGADGIAVIAPFFFK---SQNKDalisFLREVAAAApTLPFYYYHMPSMTGVKIRAE-- 156
Cdd:PRK04147 77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYYPfsfEEICD----YYREIIDSA-DNPMIVYNIPALTGVNLSLDqf 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 157 -ELLdgiqdKIPTFQGLKFTDTDLLDFGQcVDQNHQRQFaLLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFE 235
Cdd:PRK04147 152 nELF-----TLPKVIGVKQTAGDLYQLER-IRKAFPDKL-IYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21311855 236 QKDLASALSYQFRIQRFINYVIKLgfGVSQT-KAIMTLVsGIPMGPPRLPLQKATQEFTAKAEA 298
Cdd:PRK04147 225 AGDIQEAQELQHECNDVIDLLIKN--GVYPGlKEILHYM-GVDAGLCRKPFKPVDEKYLPALKA 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
7-303 |
6.87e-51 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 170.24 E-value: 6.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 7 KLRGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVG 86
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 87 ALNVKESQELAQHAAEIGADGIAVIAPFFFK-SQnkDALISFLREVAAAaPTLPFYYYHMPSMTGVKIRAEELldGIQDK 165
Cdd:pfam00701 79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKpSQ--EGLYQHFKAIAEA-TDLPMILYNVPSRTGVDLTPETV--GRLAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 166 IPTFQGLKFTDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSY 245
Cdd:pfam00701 154 NPNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21311855 246 QFRIQRFINYVIKLGFgVSQTKAIMTLVsGIPMGP-PRLPLQKATQEFTAKAEAKLKSL 303
Cdd:pfam00701 233 NHKLLPLIKILFAEPN-PIPIKTALELL-GLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
8-300 |
1.19e-41 |
|
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: 145.71 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 8 LRGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVGA 87
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQI-ENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRV-PVIAGTGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 88 LNVKESQELAQHAAEIGADGIAVIAPFFFK-SQnkDALISFLREVAAAAPtLPFYYYHMPSMTGVKIRAEELLdgIQDKI 166
Cdd:cd00950 79 NNTAEAIELTKRAEKAGADAALVVTPYYNKpSQ--EGLYAHFKAIAEATD-LPVILYNVPGRTGVNIEPETVL--RLAEH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 167 PTFQGLKFTDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQ 246
Cdd:cd00950 154 PNIVGIKEATGDLDRVSELIALCPDD-FAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELH 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 21311855 247 FRIQRFINYVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKL 300
Cdd:cd00950 233 RKLLPLIKALFAEP-NPIPVKAALALL-GLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
12-302 |
3.24e-33 |
|
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: 123.65 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 12 VAATITPMTENgEINFPVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGrnklDQVVIHVGALNVK 91
Cdd:cd00953 5 ITPVITPFTGN-KIDKEKFKKHCENLISK-GIDYVFVAGTTGLGPSLSFQEKLELLKAYSDIT----DKVIFQVGSLNLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 92 ESQELAQHAAEIGADGIAVIAPFFFKSQNKDALISFLREVAAAAPTlpfYYYHMPSMTGVKIRAeELLDGIQDKIPTFQG 171
Cdd:cd00953 79 ESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISSPYPT---FIYNYPKATGYDINA-RMAKEIKKAGGDIIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 172 LKFTDTDL---LDFGQCVDqnhqrQFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDlasALSYQFr 248
Cdd:cd00953 155 VKDTNEDIshmLEYKRLVP-----DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIED---AFKLQF- 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 21311855 249 iqrFINYVIKLGFGVSQTKAIMTLV---SGIPMGPPRLPLQKATQEFTAKAEAKLKS 302
Cdd:cd00953 226 ---LINEVLDASRKYGSWSANYSLVkifQGYDAGEPRPPFYPLDEEEEEKLRKEVNE 279
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-303 |
2.53e-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: 110.50 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 10 GLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHVGALN 89
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 90 VKESQELAQHAAEIGADGIAVIAPFFFK-SQNkdALISFLREVAAAApTLPFYYYHMPSMTGVKIRAEELLDGIqdKIPT 168
Cdd:TIGR00674 79 TEEAISLTKFAEDVGADGFLVVTPYYNKpTQE--GLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKRLA--EEPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 169 FQGLKFTDTDLLDFGQCVdQNHQRQFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFR 248
Cdd:TIGR00674 154 IVAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 21311855 249 IQRFIN--YVIKLGFGVsqtKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKLKSL 303
Cdd:TIGR00674 233 LMPLHKalFIETNPIPV---KTALALL-GLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
6-243 |
2.61e-17 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 80.46 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 6 KKLRgLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLdQVVIHV 85
Cdd:PLN02417 1 KKLR-LITAIKTPYLPDGRFDLEAYDSLVNMQI-ENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKI-KVIGNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 86 GALNVKESQELAQHAAEIGADGIAVIAPFFFKSqNKDALISFLREVAAAAPTLpfyYYHMPSMTGVKIRAEELLDGIQDk 165
Cdd:PLN02417 78 GSNSTREAIHATEQGFAVGMHAALHINPYYGKT-SQEGLIKHFETVLDMGPTI---IYNVPGRTGQDIPPEVIFKIAQH- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 166 iPTFQGLKftdtdlldfgQCVDQNHQRQFA----LLF-GVDEQLLSA-LVMGATGAVGSTYNYLGKKTNQMLEAFEQKDL 239
Cdd:PLN02417 153 -PNFAGVK----------ECTGNDRVKQYTekgiLLWsGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFAGKNKEL 221
|
....
gi 21311855 240 ASAL 243
Cdd:PLN02417 222 NDKL 225
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
10-301 |
2.60e-11 |
|
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: 63.11 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 10 GLVAATITPMTENGEINFPVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKldqVVIHVGA-L 88
Cdd:cd00951 3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSY-GAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGR---VPVLAGAgY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 89 NVKESQELAQHAAEIGADGIAVIAPFFFKSQnKDALISFLREVAAAAPtLPFYYYHmpsmTGVKIRAEELLDGIQDKIPT 168
Cdd:cd00951 79 GTATAIAYAQAAEKAGADGILLLPPYLTEAP-QEGLYAHVEAVCKSTD-LGVIVYN----RANAVLTADSLARLAERCPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 169 FQGLK--FTDTDLLDfgQCVDQNHQRqFALLFGV---DEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDlaSAL 243
Cdd:cd00951 153 LVGFKdgVGDIELMR--RIVAKLGDR-LLYLGGLptaEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGD--HAT 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21311855 244 SYQFRIQRFINYVI----KLGFGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKLK 301
Cdd:cd00951 228 VKRLLRDFFLPYVDirnrRKGYAVSIVKAGARLV-GRDAGPVRPPLTDLTEEELAQLTALIK 288
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
1-303 |
1.66e-09 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 57.90 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 1 MAFPKKKLRGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKldq 80
Cdd:PRK03620 1 QELKQILGSGLLSFPVTPFDADGSFDEAAYREHLEWLA-PYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 81 VVIHVGA-LNVKESQELAQHAAEIGADGIAVIAPFF-FKSQnkDALISFLREVAAAAPtLPFYYYHmpsmTGVKIRAEEL 158
Cdd:PRK03620 77 VPVIAGAgGGTAQAIEYAQAAERAGADGILLLPPYLtEAPQ--EGLAAHVEAVCKSTD-LGVIVYN----RDNAVLTADT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 159 LDGIQDKIPTFQGLK--FTDTDLLdfgQCVDQNHQRQFALLFGvdeqLLSA-LVMGATGAVGST------YNYLGKKTNQ 229
Cdd:PRK03620 150 LARLAERCPNLVGFKdgVGDIELM---QRIVRALGDRLLYLGG----LPTAeVFAAAYLALGVPtyssavFNFVPEIALA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21311855 230 MLEAFEQKDLASAlsyQFRIQRFINYVIKL-----GFGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTAKAEAKLKSL 303
Cdd:PRK03620 223 FYRALRAGDHATV---DRLLDDFFLPYVALrnrkkGYAVSIVKAGARLV-GLDAGPVRAPLTDLTPEELAELAALIAKG 297
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
8-146 |
5.93e-08 |
|
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: 53.22 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311855 8 LRGLVAATITPMTENGE-------INFPVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKldq 80
Cdd:cd00952 2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAA-GVDGILTMGTFGECATLTWEEKQAFVATVVETVAGR--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21311855 81 VVIHVGA--LNVKESQELAQHAAEIGADGIAVIAPFFFKsQNKDALISFLREVAAAAPTLPFYYYHMP 146
Cdd:cd00952 78 VPVFVGAttLNTRDTIARTRALLDLGADGTMLGRPMWLP-LDVDTAVQFYRDVAEAVPEMAIAIYANP 144
|
|
| |
