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Conserved domains on  [gi|446576749|ref|WP_000654095|]
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MULTISPECIES: dihydrodipicolinate synthase family protein [Streptococcus]

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 ...
 7-295 4.34e-113

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: 328.50  E-value: 4.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   7 YQGIIPAFYACYDDKGDICPERVKALTNYFIDK-GVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAAPQTDFIIYNIPQLAGVALTSDLYRKMLQNPQVIG 165
Cdd:cd00954   81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 166 VKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTINDI 245
Cdd:cd00954  161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446576749 246 ITKLCSghGNMYAVIKAVLEINEqLTIGSVRLPLASVTEEDKPIIKEAAE 295
Cdd:cd00954  241 ITVLIK--NGLYPTLKAILRLMG-LDAGPCRLPLRKVTEKALAKAKELAA 287
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 7-295 4.34e-113

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: 328.50  E-value: 4.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   7 YQGIIPAFYACYDDKGDICPERVKALTNYFIDK-GVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAAPQTDFIIYNIPQLAGVALTSDLYRKMLQNPQVIG 165
Cdd:cd00954   81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 166 VKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTINDI 245
Cdd:cd00954  161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446576749 246 ITKLCSghGNMYAVIKAVLEINEqLTIGSVRLPLASVTEEDKPIIKEAAE 295
Cdd:cd00954  241 ITVLIK--NGLYPTLKAILRLMG-LDAGPCRLPLRKVTEKALAKAKELAA 287
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 6-295 8.83e-83

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: 251.23  E-value: 8.83e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   6 KYQGIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAAPqTDFIIYNIPQLAGVALTSDLYRKMLQNPQVIG 165
Cdd:COG0329   81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 166 VKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTINDI 245
Cdd:COG0329  160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446576749 246 ItKLCSGHGNMyAVIKAVLEINEqLTIGSVRLPLASVTEEDKPIIKEAAE 295
Cdd:COG0329  240 I-RALFAEGNP-APVKAALALLG-LPSGPVRLPLLPLSEEERAELRAALK 286
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 1-295 7.68e-69

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 216.01  E-value: 7.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   1 MKDLQkyqGIIPAFYACYDDKGDICPERVKALTNYFIDK-GVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVI 79
Cdd:PRK04147   1 AKNLK---GVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  80 AHVACNNTKDSVELAMHAEAMGVDAIAAIPPIY--FRLPEyaIADYWNTISQAApQTDFIIYNIPQLAGVALTSDLYRKM 157
Cdd:PRK04147  78 AQVGSVNTAEAQELAKYATELGYDAISAVTPFYypFSFEE--ICDYYREIIDSA-DNPMIVYNIPALTGVNLSLDQFNEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 158 LQNPQVIGVKNSSmpvQDIQNFVAIGGE--NHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKA 235
Cdd:PRK04147 155 FTLPKVIGVKQTA---GDLYQLERIRKAfpDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEA 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 236 RELQFTINDIITKLCSghGNMYAVIKAVLEInEQLTIGSVRLPLASVTEEDKPIIKEAAE 295
Cdd:PRK04147 232 QELQHECNDVIDLLIK--NGVYPGLKEILHY-MGVDAGLCRKPFKPVDEKYLPALKALAA 288
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 6-293 7.03e-56

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 182.57  E-value: 7.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749    6 KYQGIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTIsqaAPQTDF--IIYNIPQLAGVALTSDLYRKMLQNPQV 163
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAI---AEATDLpmILYNVPSRTGVDLTPETVGRLATNPNI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  164 IGVKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTIN 243
Cdd:pfam00701 158 VGIKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLL 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446576749  244 DIITKLCSgHGNmYAVIKAVLEInEQLTIGS-VRLPLASVTEEDKP----IIKEA 293
Cdd:pfam00701 238 PLIKILFA-EPN-PIPIKTALEL-LGLVVGPtCRLPLTPLSEEERPeleaILKAA 289
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 9-293 6.60e-34

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: 125.13  E-value: 6.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749    9 GIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACNNTK 88
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   89 DSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAA--PQtdfIIYNIPQLAGVALTSDLYRKMLQNPQVIGV 166
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVdlPI---ILYNVPSRTGVSLYPETVKRLAEEPNIVAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  167 KNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARElqftINDII 246
Cdd:TIGR00674 158 KEATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEARE----IHQKL 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446576749  247 TKLCSGhgnMY-----AVIKAVLEInEQLTIGSVRLPLASVTEEDKPIIKEA 293
Cdd:TIGR00674 234 MPLHKA---LFietnpIPVKTALAL-LGLIEGELRLPLTELSEEHRNKLRDV 281
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 7-295 4.34e-113

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: 328.50  E-value: 4.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   7 YQGIIPAFYACYDDKGDICPERVKALTNYFIDK-GVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAAPQTDFIIYNIPQLAGVALTSDLYRKMLQNPQVIG 165
Cdd:cd00954   81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 166 VKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTINDI 245
Cdd:cd00954  161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446576749 246 ITKLCSghGNMYAVIKAVLEINEqLTIGSVRLPLASVTEEDKPIIKEAAE 295
Cdd:cd00954  241 ITVLIK--NGLYPTLKAILRLMG-LDAGPCRLPLRKVTEKALAKAKELAA 287
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 6-295 8.83e-83

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: 251.23  E-value: 8.83e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   6 KYQGIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAAPqTDFIIYNIPQLAGVALTSDLYRKMLQNPQVIG 165
Cdd:COG0329   81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 166 VKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTINDI 245
Cdd:COG0329  160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446576749 246 ItKLCSGHGNMyAVIKAVLEINEqLTIGSVRLPLASVTEEDKPIIKEAAE 295
Cdd:COG0329  240 I-RALFAEGNP-APVKAALALLG-LPSGPVRLPLLPLSEEERAELRAALK 286
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 10-293 7.92e-72

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: 223.19  E-value: 7.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  10 IIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACNNTKD 89
Cdd:cd00408    1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  90 SVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISqAAPQTDFIIYNIPQLAGVALTSDLYRKMLQNPQVIGVKNS 169
Cdd:cd00408   81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVA-DASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 170 SMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTINDIITKL 249
Cdd:cd00408  160 SGDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446576749 250 csGHGNMYAVIKAVLEINEqLTIGSVRLPLASVTEEDKPIIKEA 293
Cdd:cd00408  240 --FKEGNPAPVKAALALLG-LDAGPVRLPLVPLSEEERAKLEAL 280
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 1-295 7.68e-69

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 216.01  E-value: 7.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   1 MKDLQkyqGIIPAFYACYDDKGDICPERVKALTNYFIDK-GVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVI 79
Cdd:PRK04147   1 AKNLK---GVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  80 AHVACNNTKDSVELAMHAEAMGVDAIAAIPPIY--FRLPEyaIADYWNTISQAApQTDFIIYNIPQLAGVALTSDLYRKM 157
Cdd:PRK04147  78 AQVGSVNTAEAQELAKYATELGYDAISAVTPFYypFSFEE--ICDYYREIIDSA-DNPMIVYNIPALTGVNLSLDQFNEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 158 LQNPQVIGVKNSSmpvQDIQNFVAIGGE--NHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKA 235
Cdd:PRK04147 155 FTLPKVIGVKQTA---GDLYQLERIRKAfpDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEA 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 236 RELQFTINDIITKLCSghGNMYAVIKAVLEInEQLTIGSVRLPLASVTEEDKPIIKEAAE 295
Cdd:PRK04147 232 QELQHECNDVIDLLIK--NGVYPGLKEILHY-MGVDAGLCRKPFKPVDEKYLPALKALAA 288
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 6-293 7.03e-56

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 182.57  E-value: 7.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749    6 KYQGIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTIsqaAPQTDF--IIYNIPQLAGVALTSDLYRKMLQNPQV 163
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAI---AEATDLpmILYNVPSRTGVDLTPETVGRLATNPNI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  164 IGVKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTIN 243
Cdd:pfam00701 158 VGIKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLL 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446576749  244 DIITKLCSgHGNmYAVIKAVLEInEQLTIGS-VRLPLASVTEEDKP----IIKEA 293
Cdd:pfam00701 238 PLIKILFA-EPN-PIPIKTALEL-LGLVVGPtCRLPLTPLSEEERPeleaILKAA 289
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 8-293 5.74e-38

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: 135.70  E-value: 5.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   8 QGIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACNNT 87
Cdd:cd00950    2 GGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  88 KDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAA--PQtdfIIYNIPQLAGVALTSDLYRKMLQNPQVIG 165
Cdd:cd00950   82 AEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATdlPV---ILYNVPGRTGVNIEPETVLRLAEHPNIVG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 166 VKNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELQFTINDI 245
Cdd:cd00950  159 IKEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPL 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446576749 246 ItKLCSGHGNMyAVIKAVLeiNEQ-LTIGSVRLPLASVTEEDKPIIKEA 293
Cdd:cd00950  239 I-KALFAEPNP-IPVKAAL--ALLgLISGELRLPLVPLSEELRAKLRAA 283
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 9-293 6.60e-34

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: 125.13  E-value: 6.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749    9 GIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACNNTK 88
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   89 DSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAA--PQtdfIIYNIPQLAGVALTSDLYRKMLQNPQVIGV 166
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVdlPI---ILYNVPSRTGVSLYPETVKRLAEEPNIVAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  167 KNSSMPVQDIQNFVAIGGENHIVFNGPDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARElqftINDII 246
Cdd:TIGR00674 158 KEATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEARE----IHQKL 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446576749  247 TKLCSGhgnMY-----AVIKAVLEInEQLTIGSVRLPLASVTEEDKPIIKEA 293
Cdd:TIGR00674 234 MPLHKA---LFietnpIPVKTALAL-LGLIEGELRLPLTELSEEHRNKLRDV 281
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 21-287 9.79e-28

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: 108.62  E-value: 9.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  21 KGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKgklTVIAHVACNNTKDSVELAMHAEAM 100
Cdd:cd00953   14 GNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEESIELARAAKSF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 101 GVDAIAAIPPIYF-RLPEYAIADYWNTISQAAPQtdfIIYNIPQLAGVALTSDLYRKMLQNPQ-VIGVKNSsmpVQDIQN 178
Cdd:cd00953   91 GIYAIASLPPYYFpGIPEEWLIKYFTDISSPYPT---FIYNYPKATGYDINARMAKEIKKAGGdIIGVKDT---NEDISH 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 179 FVA--IGGENHIVFNGPDEQFLGG---RLMGAAAGiGGTYgvMPElylTLNQLIVDKDLEKARELQFTINDIITklCSGH 253
Cdd:cd00953  165 MLEykRLVPDFKVYSGPDSLIFSAlrsGLDGSVAA-ASNY--LPE---VFVKIKDHVAIEDAFKLQFLINEVLD--ASRK 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 446576749 254 GNMYAVIKAVLEINEQLTIGSVRLPLASVTEEDK 287
Cdd:cd00953  237 YGSWSANYSLVKIFQGYDAGEPRPPFYPLDEEEE 270
PLN02417 PLN02417
dihydrodipicolinate synthase
 6-219 5.27e-16

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 76.60  E-value: 5.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749   6 KYQGIIPAFYACYDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACN 85
Cdd:PLN02417   1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  86 NTKDSVELAMHAEAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAAPQtdfIIYNIPQLAGVALTSDLYRKMLQNPQVIG 165
Cdd:PLN02417  81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPT---IIYNVPGRTGQDIPPEVIFKIAQHPNFAG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446576749 166 VKNSsmpVQD--IQNFVaigGENHIVFNGPDEQFLGGRLMGAAAG-IGGTYGVMPEL 219
Cdd:PLN02417 158 VKEC---TGNdrVKQYT---EKGILLWSGNDDECHDARWDYGADGvISVTSNLVPGL 208
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 32-239 2.96e-15

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: 74.79  E-value: 2.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  32 LTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVACNNTKDSVELAMHAEAMGVDAIAAIPPI 111
Cdd:cd00952   34 LVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRPM 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 112 YFRLPEYAIADYWNTISQAAPQTDFIIYNIPQLAGVALTSDLYRKMLQNPQVIGVK---NSSMPVQDIQnfvAIGGEnhI 188
Cdd:cd00952  114 WLPLDVDTAVQFYRDVAEAVPEMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKylgDIGALLSDLA---AVKGR--M 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446576749 189 VFNGPDEQFLGGRLMGAAAGIGG-TYGVM--PELYLTLNQLIVDKDLEKARELQ 239
Cdd:cd00952  189 RLLPLEDDYYAAARLFPEEVTAFwSSGAAcgPAPVTALRDAVATGDWTDARALT 242
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 18-304 1.35e-09

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 57.90  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  18 YDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHVAcNNTKDSVELAMHA 97
Cdd:PRK03620  19 FDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTAQAIEYAQAA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  98 EAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAapqTDF--IIYNipqLAGVALTSD-LYRKMLQNPQVIGVKNSSMPVQ 174
Cdd:PRK03620  98 ERAGADGILLLPPYLTEAPQEGLAAHVEAVCKS---TDLgvIVYN---RDNAVLTADtLARLAERCPNLVGFKDGVGDIE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 175 DIQNFVAIGGENHIVFNG-PD-EQFlggrlMGAAAGIGGT------YGVMPELYLTLNQLIVDKDLEKARELqftINDII 246
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGGlPTaEVF-----AAAYLALGVPtyssavFNFVPEIALAFYRALRAGDHATVDRL---LDDFF 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446576749 247 TKLCS----GHGnmYAV--IKAVLEInEQLTIGSVRLPLASVTEEDkpiIKEAAEMIRHAKKQF 304
Cdd:PRK03620 244 LPYVAlrnrKKG--YAVsiVKAGARL-VGLDAGPVRAPLTDLTPEE---LAELAALIAKGGAQL 301
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 18-286 2.28e-09

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: 57.33  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  18 YDDKGDICPERVKALTNYFIDKGVQGLYVNGSSGECIYQSVADRKLVLENVMSVAKGKLTVIAHvACNNTKDSVELAMHA 97
Cdd:cd00951   12 FDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAG-AGYGTATAIAYAQAA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749  98 EAMGVDAIAAIPPIYFRLPEYAIADYWNTISQAapqTDF--IIYNipqLAGVALTSDLYRKMLQN-PQVIGVKNSSMPVQ 174
Cdd:cd00951   91 EKAGADGILLLPPYLTEAPQEGLYAHVEAVCKS---TDLgvIVYN---RANAVLTADSLARLAERcPNLVGFKDGVGDIE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446576749 175 DIQNFVAIGGENHIVFNG---PDEQFLGGRLMGAAAGIGGTYGVMPELYLTLNQLIVDKDLEKARELqftINDI------ 245
Cdd:cd00951  165 LMRRIVAKLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRL---LRDFflpyvd 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446576749 246 ITKLCSGhgnmYAV--IKAVLEInEQLTIGSVRLPLASVTEED 286
Cdd:cd00951  242 IRNRRKG----YAVsiVKAGARL-VGRDAGPVRPPLTDLTEEE 279
 
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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