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Conserved domains on  [gi|16974931|pdb|1JCJ|A]
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Chain A, Deoxyribose-phosphate Aldolase

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
11-234 7.92e-95

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 TIGR00126:

Pssm-ID: 473867  Cd Length: 211  Bit Score: 277.42  E-value: 7.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         11 RALKLMDLTTLNDDDTDEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKeqGTpEIRIATVTNFPHGNDDIDIALAE 90
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELLK--GT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         91 TRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVkaCKEACAAANVLLKVIIETGELKDEAlIRKASEISIKAGADFIKTS 170
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1JCJ_A        171 TGKVAVNATPESARIMMEVIRDmgvekTVGFLPAGGVRTAEDAQKYLAIADELFGADWADARHY 234
Cdd:TIGR00126 153 TGFGAGGATVEDVRLMRNTVGD-----TIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAIIQ 211
 
Name Accession Description Interval E-value
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
11-234 7.92e-95

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: 277.42  E-value: 7.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         11 RALKLMDLTTLNDDDTDEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKeqGTpEIRIATVTNFPHGNDDIDIALAE 90
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELLK--GT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         91 TRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVkaCKEACAAANVLLKVIIETGELKDEAlIRKASEISIKAGADFIKTS 170
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1JCJ_A        171 TGKVAVNATPESARIMMEVIRDmgvekTVGFLPAGGVRTAEDAQKYLAIADELFGADWADARHY 234
Cdd:TIGR00126 153 TGFGAGGATVEDVRLMRNTVGD-----TIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAIIQ 211
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
11-226 1.14e-82

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 246.90  E-value: 1.14e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       11 RALKLMDLTTLNDDDTDEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKEQGtpeIRIATVTNFPHGNDDIDIALAE 90
Cdd:COG0274   2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEY--GFAAVCVNPCYVPLAAELLKGSG---VKVATVIGFPLGATTTEVKVAE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       91 TRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVkaCKEACAAANVLLKVIIETGELKDEAlIRKASEISIKAGADFIKTS 170
Cdd:COG0274  77 AKEAVADGADEIDMVINIGALKSGDYDAVEEEI--AAVVEAAGGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTS 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
1JCJ_A      171 TGKVAVNATPESARIMMEVIRDMgvektVGFLPAGGVRTAEDAQKYLAIADELFGA 226
Cdd:COG0274 154 TGFGPGGATVEDVRLMRETVGGR-----VGVKASGGIRTLEDALAMIEAGATRIGT 204
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
12-226 1.66e-73

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: 222.79  E-value: 1.66e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       12 ALKLMDLTTLNDDDTDEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKEQGtpeIRIATVTNFPHGNDDIDIALAET 91
Cdd:cd00959   1 LASLIDHTLLKPDATEEDIRKLCDEAKEY--GFAAVCVNPCFVPLAREALKGSG---VKVCTVIGFPLGATTTEVKVAEA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       92 RAAIAYGADEVDVVFPYRALMAGNEQVGFDLVkaCKEACAAANVLLKVIIETGELKDEaLIRKASEISIKAGADFIKTST 171
Cdd:cd00959  76 REAIADGADEIDMVINIGALKSGDYEAVYEEI--AAVVEACGGAPLKVILETGLLTDE-EIIKACEIAIEAGADFIKTST 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
1JCJ_A      172 GKVAVNATPESARIMMEVIRDmgvekTVGFLPAGGVRTAEDAQKYLAIADELFGA 226
Cdd:cd00959 153 GFGPGGATVEDVKLMKEAVGG-----RVGVKAAGGIRTLEDALAMIEAGATRIGT 202
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
11-215 8.93e-43

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: 145.22  E-value: 8.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         11 RALKLMDLTTLNDDDT---DEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKEqgtpeiRIATVTNFPHGNDDIDI- 86
Cdd:pfam01791   1 TSILAMDQGVANGPDFafaLEDPKVLVAEAATP--GANAVLLDPGFIARAHRGYGK------DIGLIVALNHGTDLIPIn 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         87 -----ALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAaaNVLLKVIIEtGELKDEA--------LIR 153
Cdd:pfam01791  73 grdvdCVASVEEAKAMGADAVKVVVYYRVDGSEEEQQMLDEIGRVKEDCH--EWGMPLILE-GYLRGEAikdekdpdLVA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1JCJ_A        154 KASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKtvgFLPAGGV------RTAEDAQK 215
Cdd:pfam01791 150 DAARLGAELGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY---VVLAGGVseedflRTVRDAMI 214
 
Name Accession Description Interval E-value
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
11-234 7.92e-95

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: 277.42  E-value: 7.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         11 RALKLMDLTTLNDDDTDEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKeqGTpEIRIATVTNFPHGNDDIDIALAE 90
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELLK--GT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         91 TRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVkaCKEACAAANVLLKVIIETGELKDEAlIRKASEISIKAGADFIKTS 170
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1JCJ_A        171 TGKVAVNATPESARIMMEVIRDmgvekTVGFLPAGGVRTAEDAQKYLAIADELFGADWADARHY 234
Cdd:TIGR00126 153 TGFGAGGATVEDVRLMRNTVGD-----TIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAIIQ 211
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
11-226 1.14e-82

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 246.90  E-value: 1.14e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       11 RALKLMDLTTLNDDDTDEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKEQGtpeIRIATVTNFPHGNDDIDIALAE 90
Cdd:COG0274   2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEY--GFAAVCVNPCYVPLAAELLKGSG---VKVATVIGFPLGATTTEVKVAE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       91 TRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVkaCKEACAAANVLLKVIIETGELKDEAlIRKASEISIKAGADFIKTS 170
Cdd:COG0274  77 AKEAVADGADEIDMVINIGALKSGDYDAVEEEI--AAVVEAAGGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTS 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
1JCJ_A      171 TGKVAVNATPESARIMMEVIRDMgvektVGFLPAGGVRTAEDAQKYLAIADELFGA 226
Cdd:COG0274 154 TGFGPGGATVEDVRLMRETVGGR-----VGVKASGGIRTLEDALAMIEAGATRIGT 204
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
12-226 1.66e-73

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: 222.79  E-value: 1.66e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       12 ALKLMDLTTLNDDDTDEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKEQGtpeIRIATVTNFPHGNDDIDIALAET 91
Cdd:cd00959   1 LASLIDHTLLKPDATEEDIRKLCDEAKEY--GFAAVCVNPCFVPLAREALKGSG---VKVCTVIGFPLGATTTEVKVAEA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       92 RAAIAYGADEVDVVFPYRALMAGNEQVGFDLVkaCKEACAAANVLLKVIIETGELKDEaLIRKASEISIKAGADFIKTST 171
Cdd:cd00959  76 REAIADGADEIDMVINIGALKSGDYEAVYEEI--AAVVEACGGAPLKVILETGLLTDE-EIIKACEIAIEAGADFIKTST 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
1JCJ_A      172 GKVAVNATPESARIMMEVIRDmgvekTVGFLPAGGVRTAEDAQKYLAIADELFGA 226
Cdd:cd00959 153 GFGPGGATVEDVKLMKEAVGG-----RVGVKAAGGIRTLEDALAMIEAGATRIGT 202
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
16-218 3.29e-52

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: 168.66  E-value: 3.29e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       16 MDLTTLNDDDTDEKVIALCHQAKTpvGNTAAICIYPRFIPIARKTLKEQGtpeIRIATVTNFPHGNDDIDIALAETRAAI 95
Cdd:cd00945   1 IDLTLLHPDATLEDIAKLCDEAIE--YGFAAVCVNPGYVRLAADALAGSD---VPVIVVVGFPTGLTTTEVKVAEVEEAI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A       96 AYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAaNVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVA 175
Cdd:cd00945  76 DLGADEIDVVINIGSLKEGDWEEVLEEIAAVVEAADG-GLPLKVILETRGLKTADEIAKAARIAAEAGADFIKTSTGFGG 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
1JCJ_A      176 VNATPESARIMMEVIRDmgvekTVGFLPAGGVRTAEDAQKYLA 218
Cdd:cd00945 155 GGATVEDVKLMKEAVGG-----RVGVKAAGGIKTLEDALAAIE 192
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
11-215 8.93e-43

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: 145.22  E-value: 8.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         11 RALKLMDLTTLNDDDT---DEKVIALCHQAKTPvgNTAAICIYPRFIPIARKTLKEqgtpeiRIATVTNFPHGNDDIDI- 86
Cdd:pfam01791   1 TSILAMDQGVANGPDFafaLEDPKVLVAEAATP--GANAVLLDPGFIARAHRGYGK------DIGLIVALNHGTDLIPIn 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JCJ_A         87 -----ALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAaaNVLLKVIIEtGELKDEA--------LIR 153
Cdd:pfam01791  73 grdvdCVASVEEAKAMGADAVKVVVYYRVDGSEEEQQMLDEIGRVKEDCH--EWGMPLILE-GYLRGEAikdekdpdLVA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1JCJ_A        154 KASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKtvgFLPAGGV------RTAEDAQK 215
Cdd:pfam01791 150 DAARLGAELGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY---VVLAGGVseedflRTVRDAMI 214
 
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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