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Conserved domains on  [gi|1370462025|ref|XP_024304769|]
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deoxyribose-phosphate aldolase isoform X1 [Homo sapiens]

Protein Classification

deoxyribose-phosphate aldolase( domain architecture ID 10097271)

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

CATH:  3.20.20.70
EC:  4.1.2.4
Gene Ontology:  GO:0004139|GO:0009264
PubMed:  12206759|30284013
SCOP:  4003216

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
8-189 9.84e-77

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: 229.73  E-value: 9.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKAagcNIPVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:cd00959    31 FAAVCVNPCFVPLAREALKG---SGVKVCTVIGFPLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEAVYEEI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKACGEAHLKTILATGELgTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKIGFKP 167
Cdd:cd00959   108 AAVVEACGGAPLKVILETGLL-TDEEIIKACEIAIEAGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKA 179
                         170       180
                  ....*....|....*....|..
gi 1370462025 168 AGGIRSAKDSLAWLSLVKEELG 189
Cdd:cd00959   180 AGGIRTLEDALAMIEAGATRIG 201
 
Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
8-189 9.84e-77

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: 229.73  E-value: 9.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKAagcNIPVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:cd00959    31 FAAVCVNPCFVPLAREALKG---SGVKVCTVIGFPLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEAVYEEI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKACGEAHLKTILATGELgTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKIGFKP 167
Cdd:cd00959   108 AAVVEACGGAPLKVILETGLL-TDEEIIKACEIAIEAGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKA 179
                         170       180
                  ....*....|....*....|..
gi 1370462025 168 AGGIRSAKDSLAWLSLVKEELG 189
Cdd:cd00959   180 AGGIRTLEDALAMIEAGATRIG 201
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
8-212 2.55e-73

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 221.86  E-value: 2.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKaaGCNIPVASVAaGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:COG0274    33 FAAVCVNPCYVPLAAELLK--GSGVKVATVI-GFPLGATTTEVKVAEAKEAVADGADEIDMVINIGALKSGDYDAVEEEI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKACGEAHLKTILATGELGTLTnVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKIGFKP 167
Cdd:COG0274   110 AAVVEAAGGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTSTGFGPGGATVEDVRLMRETV-------GGRVGVKA 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370462025 168 AGGIRSAKDSLAWLSLVKEelgdewlkpelfRIGASTLLSDIERQ 212
Cdd:COG0274   182 SGGIRTLEDALAMIEAGAT------------RIGTSSGVAILEGL 214
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
8-210 1.79e-43

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: 145.30  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKaaGCNIPVASVAaGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:TIGR00126  32 FAAVCVNPSYVPLAKELLK--GTEVRICTVV-GFPLGASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEVVYDDI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKACGEAHLKTILATGELgTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKIGFKP 167
Cdd:TIGR00126 109 RAVVEACAGVLLKVIIETGLL-TDEEIRKACEICIDAGADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKA 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370462025 168 AGGIRSAKDSLAWLslvkeELGDEwlkpelfRIGASTLLSDIE 210
Cdd:TIGR00126 181 SGGVRTAEDAIAMI-----EAGAS-------RIGASAGVAIIQ 211
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
8-190 1.92e-19

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: 83.21  E-value: 1.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKAagcNIPVAsvaAGFPAGQTHLKTR------LEEIRLAVEDGATEIDVVINRSLVLTGQWE 81
Cdd:pfam01791  35 ANAVLLDPGFIARAHRGYGK---DIGLI---VALNHGTDLIPINgrdvdcVASVEEAKAMGADAVKVVVYYRVDGSEEEQ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  82 ALYDEIRQFRKACGEAHLKTILAtGELGTLT--------NVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIR 153
Cdd:pfam01791 109 QMLDEIGRVKEDCHEWGMPLILE-GYLRGEAikdekdpdLVADAARLGAELGADIVKVSYPKNMKNAGEEDADVFKRVIK 187
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370462025 154 DFFWKTgnkigFKPAGGIrSAKDSLAWLSLVKEELGD 190
Cdd:pfam01791 188 AAPVPY-----VVLAGGV-SEEDFLRTVRDAMIEAGA 218
 
Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
8-189 9.84e-77

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: 229.73  E-value: 9.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKAagcNIPVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:cd00959    31 FAAVCVNPCFVPLAREALKG---SGVKVCTVIGFPLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEAVYEEI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKACGEAHLKTILATGELgTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKIGFKP 167
Cdd:cd00959   108 AAVVEACGGAPLKVILETGLL-TDEEIIKACEIAIEAGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKA 179
                         170       180
                  ....*....|....*....|..
gi 1370462025 168 AGGIRSAKDSLAWLSLVKEELG 189
Cdd:cd00959   180 AGGIRTLEDALAMIEAGATRIG 201
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
8-212 2.55e-73

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 221.86  E-value: 2.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKaaGCNIPVASVAaGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:COG0274    33 FAAVCVNPCYVPLAAELLK--GSGVKVATVI-GFPLGATTTEVKVAEAKEAVADGADEIDMVINIGALKSGDYDAVEEEI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKACGEAHLKTILATGELGTLTnVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKIGFKP 167
Cdd:COG0274   110 AAVVEAAGGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTSTGFGPGGATVEDVRLMRETV-------GGRVGVKA 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370462025 168 AGGIRSAKDSLAWLSLVKEelgdewlkpelfRIGASTLLSDIERQ 212
Cdd:COG0274   182 SGGIRTLEDALAMIEAGAT------------RIGTSSGVAILEGL 214
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
8-183 1.86e-51

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: 165.58  E-value: 1.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKAAGcniPVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:cd00945    27 FAAVCVNPGYVRLAADALAGSD---VPVIVVVGFPTGLTTTEVKVAEVEEAIDLGADEIDVVINIGSLKEGDWEEVLEEI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKAC-GEAHLKTILATGELGTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKIGFK 166
Cdd:cd00945   104 AAVVEAAdGGLPLKVILETRGLKTADEIAKAARIAAEAGADFIKTSTGFGGGGATVEDVKLMKEAV-------GGRVGVK 176
                         170
                  ....*....|....*..
gi 1370462025 167 PAGGIRSAKDSLAWLSL 183
Cdd:cd00945   177 AAGGIKTLEDALAAIEA 193
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
8-210 1.79e-43

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: 145.30  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKaaGCNIPVASVAaGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEI 87
Cdd:TIGR00126  32 FAAVCVNPSYVPLAKELLK--GTEVRICTVV-GFPLGASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEVVYDDI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  88 RQFRKACGEAHLKTILATGELgTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKIGFKP 167
Cdd:TIGR00126 109 RAVVEACAGVLLKVIIETGLL-TDEEIRKACEICIDAGADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKA 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370462025 168 AGGIRSAKDSLAWLslvkeELGDEwlkpelfRIGASTLLSDIE 210
Cdd:TIGR00126 181 SGGVRTAEDAIAMI-----EAGAS-------RIGASAGVAIIQ 211
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
8-190 1.92e-19

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: 83.21  E-value: 1.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025   8 TAAVCVYPARVCDAVKALKAagcNIPVAsvaAGFPAGQTHLKTR------LEEIRLAVEDGATEIDVVINRSLVLTGQWE 81
Cdd:pfam01791  35 ANAVLLDPGFIARAHRGYGK---DIGLI---VALNHGTDLIPINgrdvdcVASVEEAKAMGADAVKVVVYYRVDGSEEEQ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370462025  82 ALYDEIRQFRKACGEAHLKTILAtGELGTLT--------NVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIR 153
Cdd:pfam01791 109 QMLDEIGRVKEDCHEWGMPLILE-GYLRGEAikdekdpdLVADAARLGAELGADIVKVSYPKNMKNAGEEDADVFKRVIK 187
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370462025 154 DFFWKTgnkigFKPAGGIrSAKDSLAWLSLVKEELGD 190
Cdd:pfam01791 188 AAPVPY-----VVLAGGV-SEEDFLRTVRDAMIEAGA 218
 
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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