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Conserved domains on  [gi|564381070|ref|XP_006250059|]
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N-acetylneuraminate lyase isoform X1 [Rattus norvegicus]

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

 Zoom to residue level

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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 ...
 8-275 1.41e-110

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: 321.57  E-value: 1.41e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   8 LQGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVGA 87
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  88 LNLKESQELAQHAAEIGADGIAVIAPFFFK------------------------------SQNKVRAEELLDGIQdkIPS 137
Cdd:cd00954   80 LNLKESQELAKHAEELGYDAISAITPFYYKfsfeeikdyyreiiaaaaslpmiiyhipalTGVNLTLEQFLELFE--IPN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 138 FQGLKFSDTDLLDFGQCVDQnHQRQFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFR 217
Cdd:cd00954  158 VIGVKFTATDLYDLERIRAA-SPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHV 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564381070 218 IQRFINYVIKLGFgVSQTKAIMTLVsGIPMGPPRLPLQKATQEftanAEAKLKSLNFL 275
Cdd:cd00954  237 INDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPLRKVTEK----ALAKAKELAAK 288
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 8-275 1.41e-110

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: 321.57  E-value: 1.41e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   8 LQGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVGA 87
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  88 LNLKESQELAQHAAEIGADGIAVIAPFFFK------------------------------SQNKVRAEELLDGIQdkIPS 137
Cdd:cd00954   80 LNLKESQELAKHAEELGYDAISAITPFYYKfsfeeikdyyreiiaaaaslpmiiyhipalTGVNLTLEQFLELFE--IPN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 138 FQGLKFSDTDLLDFGQCVDQnHQRQFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFR 217
Cdd:cd00954  158 VIGVKFTATDLYDLERIRAA-SPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHV 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564381070 218 IQRFINYVIKLGFgVSQTKAIMTLVsGIPMGPPRLPLQKATQEftanAEAKLKSLNFL 275
Cdd:cd00954  237 INDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPLRKVTEK----ALAKAKELAAK 288
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 7-275 4.30e-66

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 208.08  E-value: 4.30e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   7 KLQGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVG 86
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  87 ALNLKESQELAQHAAEIGADGIAVIAPFFFK-SQnkvraEELLD-------------GIQD------------------K 134
Cdd:COG0329   79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKpTQ-----EGLYAhfkaiaeavdlpiILYNipgrtgvdlspetlarlaE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 135 IPSFQGLKFSDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSY 214
Cdd:COG0329  154 IPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARAL 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564381070 215 QFRIQRFINYVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTANAEAKLKSLNFL 275
Cdd:COG0329  233 QDRLLPLIRALFAEG-NPAPVKAALALL-GLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 6-267 7.61e-49

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 164.01  E-value: 7.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   6 KKLQGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLDqVVIHV 85
Cdd:PRK04147   2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVK-LIAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  86 GALNLKESQELAQHAAEIGADGIAVIAPFFFK---SQNKVRAEELLDGIQDK------------------------IPSF 138
Cdd:PRK04147  81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPfsfEEICDYYREIIDSADNPmivynipaltgvnlsldqfnelftLPKV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 139 QGLKFSDTDLLDFGQcVDQNHQRQFaLLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRI 218
Cdd:PRK04147 161 IGVKQTAGDLYQLER-IRKAFPDKL-IYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHEC 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564381070 219 QRFINYVIKLgfGVSQT-KAIMTLVsGIPMGPPRLPLQKATQEFTANAEA 267
Cdd:PRK04147 239 NDVIDLLIKN--GVYPGlKEILHYM-GVDAGLCRKPFKPVDEKYLPALKA 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 7-272 1.06e-41

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 145.20  E-value: 1.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070    7 KLQGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVG 86
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   87 ALNLKESQELAQHAAEIGADGIAVIAPFFfksqNKVRAEELLDGIQD-------------------------------KI 135
Cdd:pfam00701  79 SNSTSEAIHLAQLAEEYGADGALAVTPYY----NKPSQEGLYQHFKAiaeatdlpmilynvpsrtgvdltpetvgrlaTN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  136 PSFQGLKFSDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQ 215
Cdd:pfam00701 155 PNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALIN 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564381070  216 FRIQRFINYVIKLGFgVSQTKAIMTLVsGIPMGP-PRLPLQKATQEFTANAEAKLKSL 272
Cdd:pfam00701 234 HKLLPLIKILFAEPN-PIPIKTALELL-GLVVGPtCRLPLTPLSEEERPELEAILKAA 289
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-272 2.19e-23

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: 96.63  E-value: 2.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   10 GLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVGALN 89
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   90 LKESQELAQHAAEIGADGIAVIAPFFFK-SQN------KVRAEE-----LLDGIQD---------------KIPSFQGLK 142
Cdd:TIGR00674  79 TEEAISLTKFAEDVGADGFLVVTPYYNKpTQEglyqhfKAIAEEvdlpiILYNVPSrtgvslypetvkrlaEEPNIVAIK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  143 FSDTDLLDFGQCVdQNHQRQFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRIQRFI 222
Cdd:TIGR00674 159 EATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLH 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564381070  223 N--YVIKLGFGVsqtKAIMTLVsGIPMGPPRLPLQKATQEFTANAEAKLKSL 272
Cdd:TIGR00674 238 KalFIETNPIPV---KTALALL-GLIEGELRLPLTELSEEHRNKLRDVLKDL 285
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 8-275 1.41e-110

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: 321.57  E-value: 1.41e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   8 LQGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVGA 87
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  88 LNLKESQELAQHAAEIGADGIAVIAPFFFK------------------------------SQNKVRAEELLDGIQdkIPS 137
Cdd:cd00954   80 LNLKESQELAKHAEELGYDAISAITPFYYKfsfeeikdyyreiiaaaaslpmiiyhipalTGVNLTLEQFLELFE--IPN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 138 FQGLKFSDTDLLDFGQCVDQnHQRQFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFR 217
Cdd:cd00954  158 VIGVKFTATDLYDLERIRAA-SPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHV 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564381070 218 IQRFINYVIKLGFgVSQTKAIMTLVsGIPMGPPRLPLQKATQEftanAEAKLKSLNFL 275
Cdd:cd00954  237 INDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPLRKVTEK----ALAKAKELAAK 288
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 7-275 4.30e-66

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 208.08  E-value: 4.30e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   7 KLQGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVG 86
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  87 ALNLKESQELAQHAAEIGADGIAVIAPFFFK-SQnkvraEELLD-------------GIQD------------------K 134
Cdd:COG0329   79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKpTQ-----EGLYAhfkaiaeavdlpiILYNipgrtgvdlspetlarlaE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 135 IPSFQGLKFSDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSY 214
Cdd:COG0329  154 IPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARAL 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564381070 215 QFRIQRFINYVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTANAEAKLKSLNFL 275
Cdd:COG0329  233 QDRLLPLIRALFAEG-NPAPVKAALALL-GLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 11-269 4.50e-64

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: 202.78  E-value: 4.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  11 LVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVGALNL 90
Cdd:cd00408    1 VIPALVTPFTADGEVDLDALRRLVEFLI-EAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRV-PVIAGVGANST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  91 KESQELAQHAAEIGADGIAVIAPFFFK-SQNKVRA--EELLD------GIQD------------------KIPSFQGLKF 143
Cdd:cd00408   79 REAIELARHAEEAGADGVLVVPPYYNKpSQEGIVAhfKAVADasdlpvILYNipgrtgvdlspetiarlaEHPNIVGIKD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 144 SDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRIQRFIN 223
Cdd:cd00408  159 SSGDLDRLTRLIALLGPD-FAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIE 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564381070 224 YVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTANAEAKL 269
Cdd:cd00408  238 ALFKEG-NPAPVKAALALL-GLDAGPVRLPLVPLSEEERAKLEALL 281
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 6-267 7.61e-49

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 164.01  E-value: 7.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   6 KKLQGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLDqVVIHV 85
Cdd:PRK04147   2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVK-LIAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  86 GALNLKESQELAQHAAEIGADGIAVIAPFFFK---SQNKVRAEELLDGIQDK------------------------IPSF 138
Cdd:PRK04147  81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPfsfEEICDYYREIIDSADNPmivynipaltgvnlsldqfnelftLPKV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 139 QGLKFSDTDLLDFGQcVDQNHQRQFaLLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRI 218
Cdd:PRK04147 161 IGVKQTAGDLYQLER-IRKAFPDKL-IYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHEC 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564381070 219 QRFINYVIKLgfGVSQT-KAIMTLVsGIPMGPPRLPLQKATQEFTANAEA 267
Cdd:PRK04147 239 NDVIDLLIKN--GVYPGlKEILHYM-GVDAGLCRKPFKPVDEKYLPALKA 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 7-272 1.06e-41

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 145.20  E-value: 1.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070    7 KLQGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVG 86
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   87 ALNLKESQELAQHAAEIGADGIAVIAPFFfksqNKVRAEELLDGIQD-------------------------------KI 135
Cdd:pfam00701  79 SNSTSEAIHLAQLAEEYGADGALAVTPYY----NKPSQEGLYQHFKAiaeatdlpmilynvpsrtgvdltpetvgrlaTN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  136 PSFQGLKFSDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQ 215
Cdd:pfam00701 155 PNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALIN 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564381070  216 FRIQRFINYVIKLGFgVSQTKAIMTLVsGIPMGP-PRLPLQKATQEFTANAEAKLKSL 272
Cdd:pfam00701 234 HKLLPLIKILFAEPN-PIPIKTALELL-GLVVGPtCRLPLTPLSEEERPELEAILKAA 289
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 8-269 4.73e-34

Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.


Pssm-ID: 188637 [Multi-domain]  Cd Length: 284  Bit Score: 124.91  E-value: 4.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   8 LQGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVGA 87
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQI-ENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRV-PVIAGTGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  88 LNLKESQELAQHAAEIGADGIAVIAPFFFK-SQNKVRA--EELLDGI--------------QD----------KIPSFQG 140
Cdd:cd00950   79 NNTAEAIELTKRAEKAGADAALVVTPYYNKpSQEGLYAhfKAIAEATdlpvilynvpgrtgVNiepetvlrlaEHPNIVG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 141 LKFSDTDLLDFGQCVDQNHQRqFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRIQR 220
Cdd:cd00950  159 IKEATGDLDRVSELIALCPDD-FAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLP 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564381070 221 FINYVIKLGfGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTANAEAKL 269
Cdd:cd00950  238 LIKALFAEP-NPIPVKAALALL-GLISGELRLPLVPLSEELRAKLRAAL 284
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-272 2.19e-23

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: 96.63  E-value: 2.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   10 GLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVGALN 89
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   90 LKESQELAQHAAEIGADGIAVIAPFFFK-SQN------KVRAEE-----LLDGIQD---------------KIPSFQGLK 142
Cdd:TIGR00674  79 TEEAISLTKFAEDVGADGFLVVTPYYNKpTQEglyqhfKAIAEEvdlpiILYNVPSrtgvslypetvkrlaEEPNIVAIK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  143 FSDTDLLDFGQCVdQNHQRQFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRIQRFI 222
Cdd:TIGR00674 159 EATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLH 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564381070  223 N--YVIKLGFGVsqtKAIMTLVsGIPMGPPRLPLQKATQEFTANAEAKLKSL 272
Cdd:TIGR00674 238 KalFIETNPIPV---KTALALL-GLIEGELRLPLTELSEEHRNKLRDVLKDL 285
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 12-271 3.74e-23

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: 95.91  E-value: 3.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  12 VAATITPMTENgEINFPVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSISERRQVAEEWvrqgKNKLDQVVIHVGALNLK 91
Cdd:cd00953    5 ITPVITPFTGN-KIDKEKFKKHCENLISK-GIDYVFVAGTTGLGPSLSFQEKLELLKAY----SDITDKVIFQVGSLNLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  92 ESQELAQHAAEIGADGIAVIAPFFF---------------------------KSQNKVRAEELLDGIQDKIPSFQGLKfs 144
Cdd:cd00953   79 ESIELARAAKSFGIYAIASLPPYYFpgipeewlikyftdisspyptfiynypKATGYDINARMAKEIKKAGGDIIGVK-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 145 DT-----DLLDFGQCVDqnhqrQFALLFGVDEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDlasALSYQFriq 219
Cdd:cd00953  157 DTnedisHMLEYKRLVP-----DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIED---AFKLQF--- 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564381070 220 rFINYVIKLGFGVSQTKAIMTLV---SGIPMGPPRLPLQKATQEftanAEAKLKS 271
Cdd:cd00953  226 -LINEVLDASRKYGSWSANYSLVkifQGYDAGEPRPPFYPLDEE----EEEKLRK 275
PLN02417 PLN02417
dihydrodipicolinate synthase
 7-121 3.97e-11

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 61.97  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   7 KLQGLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKLdQVVIHVG 86
Cdd:PLN02417   1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQI-ENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKI-KVIGNTG 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564381070  87 ALNLKESQELAQHAAEIGADGIAVIAPFFFKSQNK 121
Cdd:PLN02417  79 SNSTREAIHATEQGFAVGMHAALHINPYYGKTSQE 113
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 10-270 6.53e-08

5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH); 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate.


Pssm-ID: 188638  Cd Length: 289  Bit Score: 52.71  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  10 GLVAATITPMTENGEINFPVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKldqVVIHVGA-L 88
Cdd:cd00951    3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSY-GAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGR---VPVLAGAgY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  89 NLKESQELAQHAAEIGADGIAVIAPFF-------------------------FKSQNKVRAEELLDGIQDKIPSFQGLK- 142
Cdd:cd00951   79 GTATAIAYAQAAEKAGADGILLLPPYLteapqeglyahveavckstdlgvivYNRANAVLTADSLARLAERCPNLVGFKd 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070 143 -FSDTDLLDfgQCVDQNHQRqFALLFGV---DEQLLSALVLGATGAVGSTYNYLGKKTNQMLEAFEQKDlaSALSYQFRI 218
Cdd:cd00951  159 gVGDIELMR--RIVAKLGDR-LLYLGGLptaEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGD--HATVKRLLR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564381070 219 QRFINYVI----KLGFGVSQTKAIMTLVsGIPMGPPRLPLQKATQEFTANAEAKLK 270
Cdd:cd00951  234 DFFLPYVDirnrRKGYAVSIVKAGARLV-GRDAGPVRPPLTDLTEEELAQLTALIK 288
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 10-114 2.06e-06

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 48.27  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070  10 GLVAATITPMTENGEINFPVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKldqVVIHVGA-L 88
Cdd:PRK03620  10 GLLSFPVTPFDADGSFDEAAYREHLEWLA-PYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGR---VPVIAGAgG 85

                         90       100
                 ....*....|....*....|....*.
gi 564381070  89 NLKESQELAQHAAEIGADGIAVIAPF 114
Cdd:PRK03620  86 GTAQAIEYAQAAERAGADGILLLPPY 111
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 8-113 1.14e-03

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: 39.74  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381070   8 LQGLVAATITPMTENGE-------INFPVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSISERRQVAEEWVRQGKNKldq 80
Cdd:cd00952    2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAA-GVDGILTMGTFGECATLTWEEKQAFVATVVETVAGR--- 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564381070  81 VVIHVGA--LNLKESQELAQHAAEIGADGIAVIAP 113
Cdd:cd00952   78 VPVFVGAttLNTRDTIARTRALLDLGADGTMLGRP 112
 
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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