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Conserved domains on  [gi|510817338|ref|WP_016190875|]
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deoxyribose-phosphate aldolase [Erwinia tracheiphila]

Protein Classification

2-deoxyribose-5-phosphate aldolase( domain architecture ID 10000957)

2-deoxyribose-5-phosphate aldolase (DERA) catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate.

EC:  4.1.2.4
Gene Symbol:  deoC
PubMed:  12206759|30284013
SCOP:  4003216

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
29-245 7.01e-74

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


:

Pssm-ID: 440043  Cd Length: 219  Bit Score: 224.17  E-value: 7.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  29 VIALCRQACTPagNTAAVCIYPRFIPVACKTLREQgtpDIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPWR 108
Cdd:COG0274   21 IEKLCEEAKEY--GFAAVCVNPCYVPLAAELLKGS---GVKVATVIGFPLGATTTEVKVAEAKEAVADGADEIDMVINIG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338 109 ALIAGNHGVGFQLVSACKKACasAGVLLKVIIESGELKTAElIRQASEQAIAAGADFIKTSTGKVAINATPDAAEIMLRV 188
Cdd:COG0274   96 ALKSGDYDAVEEEIAAVVEAA--GGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTSTGFGPGGATVEDVRLMRET 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510817338 189 IadkglGQQVGFKPAGGVKTAEEAARYLALADDilgrgwvdvrhfRFGASGLLGNLL 245
Cdd:COG0274  173 V-----GGRVGVKASGGIRTLEDALAMIEAGAT------------RIGTSSGVAILE 212
 
Name Accession Description Interval E-value
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
29-245 7.01e-74

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 224.17  E-value: 7.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  29 VIALCRQACTPagNTAAVCIYPRFIPVACKTLREQgtpDIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPWR 108
Cdd:COG0274   21 IEKLCEEAKEY--GFAAVCVNPCYVPLAAELLKGS---GVKVATVIGFPLGATTTEVKVAEAKEAVADGADEIDMVINIG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338 109 ALIAGNHGVGFQLVSACKKACasAGVLLKVIIESGELKTAElIRQASEQAIAAGADFIKTSTGKVAINATPDAAEIMLRV 188
Cdd:COG0274   96 ALKSGDYDAVEEEIAAVVEAA--GGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTSTGFGPGGATVEDVRLMRET 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510817338 189 IadkglGQQVGFKPAGGVKTAEEAARYLALADDilgrgwvdvrhfRFGASGLLGNLL 245
Cdd:COG0274  173 V-----GGRVGVKASGGIRTLEDALAMIEAGAT------------RIGTSSGVAILE 212
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
10-232 6.95e-66

deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism of nucleotides and deoxyriibonucleotides. The catalytic process is as follows: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. It is found in both gram-postive and gram-negative bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]


Pssm-ID: 272921  Cd Length: 211  Bit Score: 203.85  E-value: 6.95e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338   10 RALQLMDLTTLNDDDTDDNVIALCRQACTPagNTAAVCIYPRFIPVACKTLReqGTpDIRIATVTNFPHGNDDIDIALAE 89
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELLK--GT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338   90 TRAAIAYGADEVDVVFPWRALIAGNHGVGFQLVsaCKKACASAGVLLKVIIESGELKTAElIRQASEQAIAAGADFIKTS 169
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510817338  170 TGKVAINATPDAAEIMLRVIADkglgqQVGFKPAGGVKTAEEAARYLALADDILGRGWVDVRH 232
Cdd:TIGR00126 153 TGFGAGGATVEDVRLMRNTVGD-----TIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAII 210
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
29-224 5.53e-62

2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.


Pssm-ID: 188646  Cd Length: 203  Bit Score: 193.52  E-value: 5.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  29 VIALCRQACTPagNTAAVCIYPRFIPVACKTLREqgtPDIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPWR 108
Cdd:cd00959   19 IRKLCDEAKEY--GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGFPLGATTTEVKVAEAREAIADGADEIDMVINIG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338 109 ALIAGNHGVGFQLVSACKKACasAGVLLKVIIESGELkTAELIRQASEQAIAAGADFIKTSTGKVAINATPDAAEIMLRV 188
Cdd:cd00959   94 ALKSGDYEAVYEEIAAVVEAC--GGAPLKVILETGLL-TDEEIIKACEIAIEAGADFIKTSTGFGPGGATVEDVKLMKEA 170
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 510817338 189 IadkglGQQVGFKPAGGVKTAEEAARYLALADDILG 224
Cdd:cd00959  171 V-----GGRVGVKAAGGIRTLEDALAMIEAGATRIG 201
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
29-224 2.02e-32

DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.


Pssm-ID: 460332  Cd Length: 230  Bit Score: 118.26  E-value: 2.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338   29 VIALCRQACTPagNTAAVCIYPRFIPVACKTLREqgtpdiRIATVTNFPHGNDDIDI------ALAETRAAIAYGADEVD 102
Cdd:pfam01791  23 PKVLVAEAATP--GANAVLLDPGFIARAHRGYGK------DIGLIVALNHGTDLIPIngrdvdCVASVEEAKAMGADAVK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  103 VVFPWRALIAGNHGVGFQLVSACKKACASAGvlLKVIIEsGELKT--------AELIRQASEQAIAAGADFIKTSTGKVA 174
Cdd:pfam01791  95 VVVYYRVDGSEEEQQMLDEIGRVKEDCHEWG--MPLILE-GYLRGeaikdekdPDLVADAARLGAELGADIVKVSYPKNM 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 510817338  175 INATPDAAEIMLRVIADKGLGQqvgFKPAGGVkTAEEAARYLALADDILG 224
Cdd:pfam01791 172 KNAGEEDADVFKRVIKAAPVPY---VVLAGGV-SEEDFLRTVRDAMIEAG 217
 
Name Accession Description Interval E-value
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
29-245 7.01e-74

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 224.17  E-value: 7.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  29 VIALCRQACTPagNTAAVCIYPRFIPVACKTLREQgtpDIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPWR 108
Cdd:COG0274   21 IEKLCEEAKEY--GFAAVCVNPCYVPLAAELLKGS---GVKVATVIGFPLGATTTEVKVAEAKEAVADGADEIDMVINIG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338 109 ALIAGNHGVGFQLVSACKKACasAGVLLKVIIESGELKTAElIRQASEQAIAAGADFIKTSTGKVAINATPDAAEIMLRV 188
Cdd:COG0274   96 ALKSGDYDAVEEEIAAVVEAA--GGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTSTGFGPGGATVEDVRLMRET 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510817338 189 IadkglGQQVGFKPAGGVKTAEEAARYLALADDilgrgwvdvrhfRFGASGLLGNLL 245
Cdd:COG0274  173 V-----GGRVGVKASGGIRTLEDALAMIEAGAT------------RIGTSSGVAILE 212
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
10-232 6.95e-66

deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism of nucleotides and deoxyriibonucleotides. The catalytic process is as follows: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. It is found in both gram-postive and gram-negative bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]


Pssm-ID: 272921  Cd Length: 211  Bit Score: 203.85  E-value: 6.95e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338   10 RALQLMDLTTLNDDDTDDNVIALCRQACTPagNTAAVCIYPRFIPVACKTLReqGTpDIRIATVTNFPHGNDDIDIALAE 89
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELLK--GT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338   90 TRAAIAYGADEVDVVFPWRALIAGNHGVGFQLVsaCKKACASAGVLLKVIIESGELKTAElIRQASEQAIAAGADFIKTS 169
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510817338  170 TGKVAINATPDAAEIMLRVIADkglgqQVGFKPAGGVKTAEEAARYLALADDILGRGWVDVRH 232
Cdd:TIGR00126 153 TGFGAGGATVEDVRLMRNTVGD-----TIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAII 210
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
29-224 5.53e-62

2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.


Pssm-ID: 188646  Cd Length: 203  Bit Score: 193.52  E-value: 5.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  29 VIALCRQACTPagNTAAVCIYPRFIPVACKTLREqgtPDIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPWR 108
Cdd:cd00959   19 IRKLCDEAKEY--GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGFPLGATTTEVKVAEAREAIADGADEIDMVINIG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338 109 ALIAGNHGVGFQLVSACKKACasAGVLLKVIIESGELkTAELIRQASEQAIAAGADFIKTSTGKVAINATPDAAEIMLRV 188
Cdd:cd00959   94 ALKSGDYEAVYEEIAAVVEAC--GGAPLKVILETGLL-TDEEIIKACEIAIEAGADFIKTSTGFGPGGATVEDVKLMKEA 170
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 510817338 189 IadkglGQQVGFKPAGGVKTAEEAARYLALADDILG 224
Cdd:cd00959  171 V-----GGRVGVKAAGGIRTLEDALAMIEAGATRIG 201
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
29-226 3.82e-47

Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188634 [Multi-domain]  Cd Length: 201  Bit Score: 155.56  E-value: 3.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  29 VIALCRQACtpAGNTAAVCIYPRFIPVACKTLREQgtpDIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPWR 108
Cdd:cd00945   15 IAKLCDEAI--EYGFAAVCVNPGYVRLAADALAGS---DVPVIVVVGFPTGLTTTEVKVAEVEEAIDLGADEIDVVINIG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338 109 ALIAGNHGVGFQLVSACKKACAsAGVLLKVIIESGELKTAELIRQASEQAIAAGADFIKTSTGKVAINATPDAAEIMLRV 188
Cdd:cd00945   90 SLKEGDWEEVLEEIAAVVEAAD-GGLPLKVILETRGLKTADEIAKAARIAAEAGADFIKTSTGFGGGGATVEDVKLMKEA 168
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 510817338 189 IadkglGQQVGFKPAGGVKTAEEAARYLALADDILGRG 226
Cdd:cd00945  169 V-----GGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
29-224 2.02e-32

DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.


Pssm-ID: 460332  Cd Length: 230  Bit Score: 118.26  E-value: 2.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338   29 VIALCRQACTPagNTAAVCIYPRFIPVACKTLREqgtpdiRIATVTNFPHGNDDIDI------ALAETRAAIAYGADEVD 102
Cdd:pfam01791  23 PKVLVAEAATP--GANAVLLDPGFIARAHRGYGK------DIGLIVALNHGTDLIPIngrdvdCVASVEEAKAMGADAVK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510817338  103 VVFPWRALIAGNHGVGFQLVSACKKACASAGvlLKVIIEsGELKT--------AELIRQASEQAIAAGADFIKTSTGKVA 174
Cdd:pfam01791  95 VVVYYRVDGSEEEQQMLDEIGRVKEDCHEWG--MPLILE-GYLRGeaikdekdPDLVADAARLGAELGADIVKVSYPKNM 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 510817338  175 INATPDAAEIMLRVIADKGLGQqvgFKPAGGVkTAEEAARYLALADDILG 224
Cdd:pfam01791 172 KNAGEEDADVFKRVIKAAPVPY---VVLAGGV-SEEDFLRTVRDAMIEAG 217
 
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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