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Conserved domains on  [gi|21311855|ref|NP_083025|]
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N-acetylneuraminate lyase [Mus musculus]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 8-306 1.54e-131

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd00954:

Pssm-ID: 473867 [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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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