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Conserved domains on  [gi|663851100|ref|NP_001287708|]
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deoxyribose-phosphate aldolase isoform 2 [Homo sapiens]

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 ...
50-234 8.98e-58

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: 473867  Cd Length: 203  Bit Score: 183.50  E-value: 8.98e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  50 AVTFIDLTTLSGDDTSSNIQRLCYKAKYPiredllkalnmhdkgiTTAAVCVYPARVCDAVKALKAagcNIPVASVAAGF 129
Cdd:cd00959    1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE---------------------------------------- 169
Cdd:cd00959   62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEavyeeiaavveacggaplkviletglltdeeiikaceiai 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663851100 170 --GSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKIGFKPAGGIRSAKDSLAWLSLVKEELG 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 8.98e-58

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: 183.50  E-value: 8.98e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  50 AVTFIDLTTLSGDDTSSNIQRLCYKAKYPiredllkalnmhdkgiTTAAVCVYPARVCDAVKALKAagcNIPVASVAAGF 129
Cdd:cd00959    1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE---------------------------------------- 169
Cdd:cd00959   62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEavyeeiaavveacggaplkviletglltdeeiikaceiai 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663851100 170 --GSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKIGFKPAGGIRSAKDSLAWLSLVKEELG 234
Cdd:cd00959  142 eaGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
49-257 1.23e-55

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 178.33  E-value: 1.23e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  49 KAVTFIDLTTLSGDDTSSNIQRLCYKAKYPIredllkalnmhdkgitTAAVCVYPARVCDAVKALKaaGCNIPVASVAaG 128
Cdd:COG0274    2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEYG----------------FAAVCVNPCYVPLAAELLK--GSGVKVATVI-G 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 129 FPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE--------------------------------------- 169
Cdd:COG0274   63 FPLGATTTEVKVAEAKEAVADGADEIDMVINIGALKSGDYDaveeeiaavveaaggavlkviletglltdeeirkacela 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 170 ---GSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKIGFKPAGGIRSAKDSLAWLSLVKEelgdewlkpelfRIG 246
Cdd:COG0274  143 ieaGADFVKTSTGFGPGGATVEDVRLMRETV-------GGRVGVKASGGIRTLEDALAMIEAGAT------------RIG 203
                        250
                 ....*....|.
gi 663851100 247 ASTLLSDIERQ 257
Cdd:COG0274  204 TSSGVAILEGL 214
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-255 2.88e-32

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: 117.95  E-value: 2.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100   53 FIDLTTLSGDDTSSNIQRLCYKAKYPiredllkalnmhdkgiTTAAVCVYPARVCDAVKALKaaGCNIPVASVAaGFPAG 132
Cdd:TIGR00126   5 LIDHTALKADTTEEDIITLCAQAKTY----------------KFAAVCVNPSYVPLAKELLK--GTEVRICTVV-GFPLG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  133 QTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE------------------------------------------G 170
Cdd:TIGR00126  66 ASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEvvyddiravveacagvllkviietglltdeeirkaceicidaG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  171 SDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKIGFKPAGGIRSAKDSLAWLslvkeELGDEwlkpelfRIGASTL 250
Cdd:TIGR00126 146 ADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKASGGVRTAEDAIAMI-----EAGAS-------RIGASAG 206

                  ....*
gi 663851100  251 LSDIE 255
Cdd:TIGR00126 207 VAIIQ 211
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-235 1.72e-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, 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: 47.77  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100   54 IDLTTLSGDDTSS---NIQRLCYKAKYPiredllkalnmhdkgiTTAAVCVYPARVCDAVKALKAagcNIPVAsvaAGFP 130
Cdd:pfam01791   6 MDQGVANGPDFAFaleDPKVLVAEAATP----------------GANAVLLDPGFIARAHRGYGK---DIGLI---VALN 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  131 AGQTHLKTR------LEEIRLAVEDGATEIDVVINRSLVLTGQWE----------------------------------- 169
Cdd:pfam01791  64 HGTDLIPINgrdvdcVASVEEAKAMGADAVKVVVYYRVDGSEEEQqmldeigrvkedchewgmplilegylrgeaikdek 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  170 ---------------GSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTgnkigFKPAGGIrSAKDSLAWLSLVKEELG 234
Cdd:pfam01791 144 dpdlvadaarlgaelGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY-----VVLAGGV-SEEDFLRTVRDAMIEAG 217

                  .
gi 663851100  235 D 235
Cdd:pfam01791 218 A 218
 
Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-234 8.98e-58

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: 183.50  E-value: 8.98e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  50 AVTFIDLTTLSGDDTSSNIQRLCYKAKYPiredllkalnmhdkgiTTAAVCVYPARVCDAVKALKAagcNIPVASVAAGF 129
Cdd:cd00959    1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE---------------------------------------- 169
Cdd:cd00959   62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEavyeeiaavveacggaplkviletglltdeeiikaceiai 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663851100 170 --GSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKIGFKPAGGIRSAKDSLAWLSLVKEELG 234
Cdd:cd00959  142 eaGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
49-257 1.23e-55

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 178.33  E-value: 1.23e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  49 KAVTFIDLTTLSGDDTSSNIQRLCYKAKYPIredllkalnmhdkgitTAAVCVYPARVCDAVKALKaaGCNIPVASVAaG 128
Cdd:COG0274    2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEYG----------------FAAVCVNPCYVPLAAELLK--GSGVKVATVI-G 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 129 FPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE--------------------------------------- 169
Cdd:COG0274   63 FPLGATTTEVKVAEAKEAVADGADEIDMVINIGALKSGDYDaveeeiaavveaaggavlkviletglltdeeirkacela 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 170 ---GSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKIGFKPAGGIRSAKDSLAWLSLVKEelgdewlkpelfRIG 246
Cdd:COG0274  143 ieaGADFVKTSTGFGPGGATVEDVRLMRETV-------GGRVGVKASGGIRTLEDALAMIEAGAT------------RIG 203
                        250
                 ....*....|.
gi 663851100 247 ASTLLSDIERQ 257
Cdd:COG0274  204 TSSGVAILEGL 214
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
54-228 2.50e-35

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: 125.52  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  54 IDLTTLSGDDTSSNIQRLCYKAKypiredllkalnmhDKGIttAAVCVYPARVCDAVKALKAAGcniPVASVAAGFPAGQ 133
Cdd:cd00945    1 IDLTLLHPDATLEDIAKLCDEAI--------------EYGF--AAVCVNPGYVRLAADALAGSD---VPVIVVVGFPTGL 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100 134 THLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE-------------------------------------------- 169
Cdd:cd00945   62 TTTEVKVAEVEEAIDLGADEIDVVINIGSLKEGDWEevleeiaavveaadgglplkviletrglktadeiakaariaaea 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663851100 170 GSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKIGFKPAGGIRSAKDSLAWLSL 228
Cdd:cd00945  142 GADFIKTSTGFGGGGATVEDVKLMKEAV-------GGRVGVKAAGGIKTLEDALAAIEA 193
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-255 2.88e-32

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: 117.95  E-value: 2.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100   53 FIDLTTLSGDDTSSNIQRLCYKAKYPiredllkalnmhdkgiTTAAVCVYPARVCDAVKALKaaGCNIPVASVAaGFPAG 132
Cdd:TIGR00126   5 LIDHTALKADTTEEDIITLCAQAKTY----------------KFAAVCVNPSYVPLAKELLK--GTEVRICTVV-GFPLG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  133 QTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWE------------------------------------------G 170
Cdd:TIGR00126  66 ASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEvvyddiravveacagvllkviietglltdeeirkaceicidaG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  171 SDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKIGFKPAGGIRSAKDSLAWLslvkeELGDEwlkpelfRIGASTL 250
Cdd:TIGR00126 146 ADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKASGGVRTAEDAIAMI-----EAGAS-------RIGASAG 206

                  ....*
gi 663851100  251 LSDIE 255
Cdd:TIGR00126 207 VAIIQ 211
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-235 1.72e-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, 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: 47.77  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100   54 IDLTTLSGDDTSS---NIQRLCYKAKYPiredllkalnmhdkgiTTAAVCVYPARVCDAVKALKAagcNIPVAsvaAGFP 130
Cdd:pfam01791   6 MDQGVANGPDFAFaleDPKVLVAEAATP----------------GANAVLLDPGFIARAHRGYGK---DIGLI---VALN 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  131 AGQTHLKTR------LEEIRLAVEDGATEIDVVINRSLVLTGQWE----------------------------------- 169
Cdd:pfam01791  64 HGTDLIPINgrdvdcVASVEEAKAMGADAVKVVVYYRVDGSEEEQqmldeigrvkedchewgmplilegylrgeaikdek 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663851100  170 ---------------GSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTgnkigFKPAGGIrSAKDSLAWLSLVKEELG 234
Cdd:pfam01791 144 dpdlvadaarlgaelGADIVKVSYPKNMKNAGEEDADVFKRVIKAAPVPY-----VVLAGGV-SEEDFLRTVRDAMIEAG 217

                  .
gi 663851100  235 D 235
Cdd:pfam01791 218 A 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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