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Conserved domains on  [gi|1907172312|ref|XP_036021982|]
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deoxyribose-phosphate aldolase isoform X1 [Mus musculus]

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 ...
50-234 5.62e-57

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 cd00959:

Pssm-ID: 451249  Cd Length: 203  Bit Score: 181.19  E-value: 5.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  50 AVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVASVATGF 129
Cdd:cd00959     1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE---------------------------------------- 169
Cdd:cd00959    62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEavyeeiaavveacggaplkviletglltdeeiikaceiai 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172312 170 --GSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKVGFKPAGGIRTAKESLAWLSLVKEELG 234
Cdd:cd00959   142 eaGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
 
Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-234 5.62e-57

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: 181.19  E-value: 5.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  50 AVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVASVATGF 129
Cdd:cd00959     1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE---------------------------------------- 169
Cdd:cd00959    62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEavyeeiaavveacggaplkviletglltdeeiikaceiai 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172312 170 --GSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKVGFKPAGGIRTAKESLAWLSLVKEELG 234
Cdd:cd00959   142 eaGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
43-265 1.77e-45

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 223351  Cd Length: 228  Bit Score: 152.78  E-value: 1.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  43 QAAWLlKAVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAAGcSIPV 122
Cdd:COG0274     2 KASRM-QLAKLIDHTLLKPDATEEDIARLCAEAKEY----------------GFAAVCVNPSYVPLAKEALKGST-VVRV 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 123 ASVaTGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE--------------------------------- 169
Cdd:COG0274    64 CTV-IGFPLGANTTAVKAAEAREAIENGADEIDMVINIGALKSGNWEavereiravveacadavvlkviletglltdeek 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 170 ----------GSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKVGFKPAGGIRTAKESLAWLslvkeELGdewlt 239
Cdd:COG0274   143 rkaceiaieaGADFVKTSTGFSAGGATVEDVKLMKETV-------GGRVGVKASGGIRTAEDAKAMI-----EAG----- 205
                         250       260
                  ....*....|....*....|....*.
gi 1907172312 240 pdLFRIGASSLLsDIERQIYHHVTGR 265
Cdd:COG0274   206 --ATRIGTSSGV-AILEGLEHLVGGK 228
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-248 1.57e-30

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: 113.33  E-value: 1.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  53 FIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKaaGCSIPVASVaTGFPAG 132
Cdd:TIGR00126   5 LIDHTALKADTTEEDIITLCAQAKTY----------------KFAAVCVNPSYVPLAKELLK--GTEVRICTV-VGFPLG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 133 QTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE------------------------------------------G 170
Cdd:TIGR00126  66 ASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEvvyddiravveacagvllkviietglltdeeirkaceicidaG 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172312 171 SDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKVGFKPAGGIRTAKESLAWLslvkeELGDEwltpdlfRIGAS 248
Cdd:TIGR00126 146 ADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKASGGVRTAEDAIAMI-----EAGAS-------RIGAS 204
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-216 7.31e-06

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. 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: 426437  Cd Length: 230  Bit Score: 45.84  E-value: 7.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  54 IDLTTLSGDDTFS---NVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVAsvaTGFP 130
Cdd:pfam01791   6 MDQGVANGPDFAFaleDPKVLVAEAATP----------------GANAVLLDPGFIARAHRGYGK---DIGLI---VALN 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 131 AGQTHLKTR------LEEIRLAVEDGATEIDVVINRTLVLTGQWE----------------------------------- 169
Cdd:pfam01791  64 HGTDLIPINgrdvdcVASVEEAKAMGADAVKVVVYYRVDGSEEEQqmldeigrvkedchewgmplilegylrgeaikdek 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907172312 170 ---------------GSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTgnkvgFKPAGGI 216
Cdd:pfam01791 144 dpdlvadaarlgaelGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY-----VVLAGGV 200
 
Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-234 5.62e-57

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: 181.19  E-value: 5.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  50 AVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVASVATGF 129
Cdd:cd00959     1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE---------------------------------------- 169
Cdd:cd00959    62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEavyeeiaavveacggaplkviletglltdeeiikaceiai 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172312 170 --GSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKVGFKPAGGIRTAKESLAWLSLVKEELG 234
Cdd:cd00959   142 eaGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
43-265 1.77e-45

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 223351  Cd Length: 228  Bit Score: 152.78  E-value: 1.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  43 QAAWLlKAVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAAGcSIPV 122
Cdd:COG0274     2 KASRM-QLAKLIDHTLLKPDATEEDIARLCAEAKEY----------------GFAAVCVNPSYVPLAKEALKGST-VVRV 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 123 ASVaTGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE--------------------------------- 169
Cdd:COG0274    64 CTV-IGFPLGANTTAVKAAEAREAIENGADEIDMVINIGALKSGNWEavereiravveacadavvlkviletglltdeek 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 170 ----------GSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKVGFKPAGGIRTAKESLAWLslvkeELGdewlt 239
Cdd:COG0274   143 rkaceiaieaGADFVKTSTGFSAGGATVEDVKLMKETV-------GGRVGVKASGGIRTAEDAKAMI-----EAG----- 205
                         250       260
                  ....*....|....*....|....*.
gi 1907172312 240 pdLFRIGASSLLsDIERQIYHHVTGR 265
Cdd:COG0274   206 --ATRIGTSSGV-AILEGLEHLVGGK 228
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
54-228 1.52e-34

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: 123.59  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  54 IDLTTLSGDDTFSNVQRLCYKAKypiradllkalnmdDKGIttAAVCVYPARVCDAVKALKAAGcsiPVASVATGFPAGQ 133
Cdd:cd00945     1 IDLTLLHPDATLEDIAKLCDEAI--------------EYGF--AAVCVNPGYVRLAADALAGSD---VPVIVVVGFPTGL 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 134 THLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE-------------------------------------------- 169
Cdd:cd00945    62 TTTEVKVAEVEEAIDLGADEIDVVINIGSLKEGDWEevleeiaavveaadgglplkviletrglktadeiakaariaaea 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172312 170 GSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKVGFKPAGGIRTAKESLAWLSL 228
Cdd:cd00945   142 GADFIKTSTGFGGGGATVEDVKLMKEAV-------GGRVGVKAAGGIKTLEDALAAIEA 193
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-248 1.57e-30

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: 113.33  E-value: 1.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  53 FIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKaaGCSIPVASVaTGFPAG 132
Cdd:TIGR00126   5 LIDHTALKADTTEEDIITLCAQAKTY----------------KFAAVCVNPSYVPLAKELLK--GTEVRICTV-VGFPLG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 133 QTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWE------------------------------------------G 170
Cdd:TIGR00126  66 ASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEvvyddiravveacagvllkviietglltdeeirkaceicidaG 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172312 171 SDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKVGFKPAGGIRTAKESLAWLslvkeELGDEwltpdlfRIGAS 248
Cdd:TIGR00126 146 ADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKASGGVRTAEDAIAMI-----EAGAS-------RIGAS 204
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-216 7.31e-06

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. 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: 426437  Cd Length: 230  Bit Score: 45.84  E-value: 7.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312  54 IDLTTLSGDDTFS---NVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVAsvaTGFP 130
Cdd:pfam01791   6 MDQGVANGPDFAFaleDPKVLVAEAATP----------------GANAVLLDPGFIARAHRGYGK---DIGLI---VALN 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172312 131 AGQTHLKTR------LEEIRLAVEDGATEIDVVINRTLVLTGQWE----------------------------------- 169
Cdd:pfam01791  64 HGTDLIPINgrdvdcVASVEEAKAMGADAVKVVVYYRVDGSEEEQqmldeigrvkedchewgmplilegylrgeaikdek 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907172312 170 ---------------GSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTgnkvgFKPAGGI 216
Cdd:pfam01791 144 dpdlvadaarlgaelGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY-----VVLAGGV 200
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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