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Conserved domains on  [gi|488976912|ref|WP_002887784|]
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MULTISPECIES: deoxyribose-phosphate aldolase [Klebsiella]

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 ...
10-233 1.05e-91

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: 269.33  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   10 RALKLMDLTTLNDDDTNEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLneQGTpDIRIATVTNFPHGNDDIDIALAE 89
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELL--KGT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   90 TRAAIAYGADEVDVVFPYRALIAGNEQVGFELVkaCKEACAAANVLLKVIIETGELKEEAlIRKASEISIKAGADFIKTS 169
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976912  170 TGKVPVNATPESARIMMEVIRDmgvekTVGFKPAGGVRSAEDAQQFLAIADELFGADWADSRHY 233
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 ...
10-233 1.05e-91

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: 269.33  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   10 RALKLMDLTTLNDDDTNEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLneQGTpDIRIATVTNFPHGNDDIDIALAE 89
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELL--KGT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   90 TRAAIAYGADEVDVVFPYRALIAGNEQVGFELVkaCKEACAAANVLLKVIIETGELKEEAlIRKASEISIKAGADFIKTS 169
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976912  170 TGKVPVNATPESARIMMEVIRDmgvekTVGFKPAGGVRSAEDAQQFLAIADELFGADWADSRHY 233
Cdd:TIGR00126 153 TGFGAGGATVEDVRLMRNTVGD-----TIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAIIQ 211
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
10-225 3.31e-84

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 250.75  E-value: 3.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  10 RALKLMDLTTLNDDDTNEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLneQGTpDIRIATVTNFPHGNDDIDIALAE 89
Cdd:COG0274    2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEY--GFAAVCVNPCYVPLAAELL--KGS-GVKVATVIGFPLGATTTEVKVAE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  90 TRAAIAYGADEVDVVFPYRALIAGNEQVGFELVkaCKEACAAANVLLKVIIETGELKEEAlIRKASEISIKAGADFIKTS 169
Cdd:COG0274   77 AKEAVADGADEIDMVINIGALKSGDYDAVEEEI--AAVVEAAGGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488976912 170 TGKVPVNATPESARIMMEVIRDMgvektVGFKPAGGVRSAEDAQQFLAIADELFGA 225
Cdd:COG0274  154 TGFGPGGATVEDVRLMRETVGGR-----VGVKASGGIRTLEDALAMIEAGATRIGT 204
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
11-225 1.50e-74

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: 225.49  E-value: 1.50e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  11 ALKLMDLTTLNDDDTNEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLNEqgtPDIRIATVTNFPHGNDDIDIALAET 90
Cdd:cd00959    1 LASLIDHTLLKPDATEEDIRKLCDEAKEY--GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGFPLGATTTEVKVAEA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  91 RAAIAYGADEVDVVFPYRALIAGNEQVGFELVkaCKEACAAANVLLKVIIETGELKEEaLIRKASEISIKAGADFIKTST 170
Cdd:cd00959   76 REAIADGADEIDMVINIGALKSGDYEAVYEEI--AAVVEACGGAPLKVILETGLLTDE-EIIKACEIAIEAGADFIKTST 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488976912 171 GKVPVNATPESARIMMEVIRDmgvekTVGFKPAGGVRSAEDAQQFLAIADELFGA 225
Cdd:cd00959  153 GFGPGGATVEDVKLMKEAVGG-----RVGVKAAGGIRTLEDALAMIEAGATRIGT 202
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
10-214 3.17e-41

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: 141.37  E-value: 3.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   10 RALKLMDLTTLNDDDT---NEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLNEqgtpdiRIATVTNFPHGNDDIDI- 85
Cdd:pfam01791   1 TSILAMDQGVANGPDFafaLEDPKVLVAEAATP--GANAVLLDPGFIARAHRGYGK------DIGLIVALNHGTDLIPIn 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   86 -----ALAETRAAIAYGADEVDVVFPYRALIAGNEQVGFELVKACKEACAaaNVLLKVIIEtGELKEEA--------LIR 152
Cdd:pfam01791  73 grdvdCVASVEEAKAMGADAVKVVVYYRVDGSEEEQQMLDEIGRVKEDCH--EWGMPLILE-GYLRGEAikdekdpdLVA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976912  153 KASEISIKAGADFIKTSTGKVPVNATPESARIMMEVIRDMGVEKtvgFKPAGGVrSAEDAQQ 214
Cdd:pfam01791 150 DAARLGAELGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY---VVLAGGV-SEEDFLR 207
 
Name Accession Description Interval E-value
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
10-233 1.05e-91

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: 269.33  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   10 RALKLMDLTTLNDDDTNEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLneQGTpDIRIATVTNFPHGNDDIDIALAE 89
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTY--KFAAVCVNPSYVPLAKELL--KGT-EVRICTVVGFPLGASTTDVKLYE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   90 TRAAIAYGADEVDVVFPYRALIAGNEQVGFELVkaCKEACAAANVLLKVIIETGELKEEAlIRKASEISIKAGADFIKTS 169
Cdd:TIGR00126  76 TKEAIKYGADEVDMVINIGALKDGNEEVVYDDI--RAVVEACAGVLLKVIIETGLLTDEE-IRKACEICIDAGADFVKTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976912  170 TGKVPVNATPESARIMMEVIRDmgvekTVGFKPAGGVRSAEDAQQFLAIADELFGADWADSRHY 233
Cdd:TIGR00126 153 TGFGAGGATVEDVRLMRNTVGD-----TIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAIIQ 211
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
10-225 3.31e-84

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 250.75  E-value: 3.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  10 RALKLMDLTTLNDDDTNEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLneQGTpDIRIATVTNFPHGNDDIDIALAE 89
Cdd:COG0274    2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEY--GFAAVCVNPCYVPLAAELL--KGS-GVKVATVIGFPLGATTTEVKVAE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  90 TRAAIAYGADEVDVVFPYRALIAGNEQVGFELVkaCKEACAAANVLLKVIIETGELKEEAlIRKASEISIKAGADFIKTS 169
Cdd:COG0274   77 AKEAVADGADEIDMVINIGALKSGDYDAVEEEI--AAVVEAAGGAVLKVILETGLLTDEE-IRKACELAIEAGADFVKTS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488976912 170 TGKVPVNATPESARIMMEVIRDMgvektVGFKPAGGVRSAEDAQQFLAIADELFGA 225
Cdd:COG0274  154 TGFGPGGATVEDVRLMRETVGGR-----VGVKASGGIRTLEDALAMIEAGATRIGT 204
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
11-225 1.50e-74

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: 225.49  E-value: 1.50e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  11 ALKLMDLTTLNDDDTNEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLNEqgtPDIRIATVTNFPHGNDDIDIALAET 90
Cdd:cd00959    1 LASLIDHTLLKPDATEEDIRKLCDEAKEY--GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGFPLGATTTEVKVAEA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  91 RAAIAYGADEVDVVFPYRALIAGNEQVGFELVkaCKEACAAANVLLKVIIETGELKEEaLIRKASEISIKAGADFIKTST 170
Cdd:cd00959   76 REAIADGADEIDMVINIGALKSGDYEAVYEEI--AAVVEACGGAPLKVILETGLLTDE-EIIKACEIAIEAGADFIKTST 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488976912 171 GKVPVNATPESARIMMEVIRDmgvekTVGFKPAGGVRSAEDAQQFLAIADELFGA 225
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 ...
15-217 4.60e-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: 168.28  E-value: 4.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  15 MDLTTLNDDDTNEKVIALCHQAKTpvGNTAAVCIYPRFIPIARKTLneqGTPDIRIATVTNFPHGNDDIDIALAETRAAI 94
Cdd:cd00945    1 IDLTLLHPDATLEDIAKLCDEAIE--YGFAAVCVNPGYVRLAADAL---AGSDVPVIVVVGFPTGLTTTEVKVAEVEEAI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912  95 AYGADEVDVVFPYRALIAGNEQVGFELVKACKEACAAaNVLLKVIIETGELKEEALIRKASEISIKAGADFIKTSTGKVP 174
Cdd:cd00945   76 DLGADEIDVVINIGSLKEGDWEEVLEEIAAVVEAADG-GLPLKVILETRGLKTADEIAKAARIAAEAGADFIKTSTGFGG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488976912 175 VNATPESARIMMEVIRDmgvekTVGFKPAGGVRSAEDAQQFLA 217
Cdd:cd00945  155 GGATVEDVKLMKEAVGG-----RVGVKAAGGIKTLEDALAAIE 192
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
10-214 3.17e-41

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: 141.37  E-value: 3.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   10 RALKLMDLTTLNDDDT---NEKVIALCHQAKTPvgNTAAVCIYPRFIPIARKTLNEqgtpdiRIATVTNFPHGNDDIDI- 85
Cdd:pfam01791   1 TSILAMDQGVANGPDFafaLEDPKVLVAEAATP--GANAVLLDPGFIARAHRGYGK------DIGLIVALNHGTDLIPIn 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976912   86 -----ALAETRAAIAYGADEVDVVFPYRALIAGNEQVGFELVKACKEACAaaNVLLKVIIEtGELKEEA--------LIR 152
Cdd:pfam01791  73 grdvdCVASVEEAKAMGADAVKVVVYYRVDGSEEEQQMLDEIGRVKEDCH--EWGMPLILE-GYLRGEAikdekdpdLVA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976912  153 KASEISIKAGADFIKTSTGKVPVNATPESARIMMEVIRDMGVEKtvgFKPAGGVrSAEDAQQ 214
Cdd:pfam01791 150 DAARLGAELGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY---VVLAGGV-SEEDFLR 207
 
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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