NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27777677|ref|NP_766321|]
View 

deoxyribose-phosphate aldolase [Mus musculus]

Protein Classification

2-deoxyribose-5-phosphate aldolase (domain architecture ID 10097271)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
50-277 2.93e-82

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: 247.44  E-value: 2.93e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  50 AVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVASVATGF 129
Cdd:cd00959   1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILATGELgSLTNVYKASLVA 209
Cdd:cd00959  62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEAVYEEIAAVVEACGGAPLKVILETGLL-TDEEIIKACEIA 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27777677 210 MMAGSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKVGFKPAGGIRTAKESLAWLSLVKEELG 277
Cdd:cd00959 141 IEAGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
 
Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-277 2.93e-82

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: 247.44  E-value: 2.93e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  50 AVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVASVATGF 129
Cdd:cd00959   1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILATGELgSLTNVYKASLVA 209
Cdd:cd00959  62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEAVYEEIAAVVEACGGAPLKVILETGLL-TDEEIIKACEIA 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27777677 210 MMAGSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKVGFKPAGGIRTAKESLAWLSLVKEELG 277
Cdd:cd00959 141 IEAGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
PRK05283 PRK05283
deoxyribose-phosphate aldolase; Provisional
48-297 7.08e-69

deoxyribose-phosphate aldolase; Provisional


Pssm-ID: 235387  Cd Length: 257  Bit Score: 215.22  E-value: 7.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   48 LKAVTFIDLTTLSGDDTFSNVQRLCYKAKYPIRadllkalnmddkgiTTAAVCVYPARVCDAVKALKAAGC-SIPVASVa 126
Cdd:PRK05283   8 LRALSLMDLTTLNDDDTDEKVIALCHQAKTPVG--------------NTAAICIYPRFIPIARKTLREQGTpEIRIATV- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  127 TGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAH-LKTILATGELGSLTNVYKA 205
Cdd:PRK05283  73 TNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFELVKACKEACAANVlLKVIIETGELKDEALIRKA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  206 SLVAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDFfwKTGNKVGFKPAGGIRTAKESLAWLSLVKEELGDEWLTPDL 285
Cdd:PRK05283 153 SEIAIKAGADFIKTSTGKVPVNATLEAARIMLEVIRDM--GVAKTVGFKPAGGVRTAEDAAQYLALADEILGADWADARH 230
                        250
                 ....*....|..
gi 27777677  286 FRIGASSLLSDI 297
Cdd:PRK05283 231 FRFGASSLLASL 242
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
43-308 1.48e-65

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 223351  Cd Length: 228  Bit Score: 205.55  E-value: 1.48e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  43 QAAWLlKAVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAAGcSIPV 122
Cdd:COG0274   2 KASRM-QLAKLIDHTLLKPDATEEDIARLCAEAKEY----------------GFAAVCVNPSYVPLAKEALKGST-VVRV 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 123 ASVaTGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGE-AHLKTILATGELGSLTN 201
Cdd:COG0274  64 CTV-IGFPLGANTTAVKAAEAREAIENGADEIDMVINIGALKSGNWEAVEREIRAVVEACADaVVLKVILETGLLTDEEK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 202 VyKASLVAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKVGFKPAGGIRTAKESLAWLslvkeELGdewl 281
Cdd:COG0274 143 R-KACEIAIEAGADFVKTSTGFSAGGATVEDVKLMKETV-------GGRVGVKASGGIRTAEDAKAMI-----EAG---- 205
                       250       260
                ....*....|....*....|....*..
gi 27777677 282 tpdLFRIGASSLLsDIERQIYHHVTGR 308
Cdd:COG0274 206 ---ATRIGTSSGV-AILEGLEHLVGGK 228
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-291 2.52e-45

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: 153.00  E-value: 2.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677    53 FIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKaaGCSIPVASVaTGFPAG 132
Cdd:TIGR00126   5 LIDHTALKADTTEEDIITLCAQAKTY----------------KFAAVCVNPSYVPLAKELLK--GTEVRICTV-VGFPLG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   133 QTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILATGElgsLTN--VYKASLVAM 210
Cdd:TIGR00126  66 ASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEVVYDDIRAVVEACAGVLLKVIIETGL---LTDeeIRKACEICI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   211 MAGSDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKVGFKPAGGIRTAKESLAWLslvkeELGDEwltpdlfRIGA 290
Cdd:TIGR00126 143 DAGADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKASGGVRTAEDAIAMI-----EAGAS-------RIGA 203

                  .
gi 27777677   291 S 291
Cdd:TIGR00126 204 S 204
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-259 1.76e-18

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: 396384  Cd Length: 235  Bit Score: 82.83  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677    54 IDLTTLSGDDTFSnvqrlcykAKYPIRADLlKALNMDDKGITTAAVCVYPARVCDAVKALKAAgcsipvASVATGFPAGQ 133
Cdd:pfam01791   6 MDQGVANGPDFAF--------AQTEQLEDL-KVLVKEAATPGANAVLLDPGYIARASRGYGKD------IGLIVALNHGT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   134 THLKTR------LEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILA--------TGELGSL 199
Cdd:pfam01791  71 YLIPINqrdvdcVASVEEAKAMGADAVKVVLYYDVDGSEDEQQMLDEIGRVKEDCHEWGMPLILEgylrgeaiKDEKSDP 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   200 TNVYKASLVAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTgnkvgFKPAGGI 259
Cdd:pfam01791 151 HLVADAARVGAELGADIVKVEYPKNMKNAGEEDADVFKDVIKAAPVPY-----VVLAGGV 205
 
Name Accession Description Interval E-value
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-277 2.93e-82

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: 247.44  E-value: 2.93e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  50 AVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAagcSIPVASVATGF 129
Cdd:cd00959   1 LASLIDHTLLKPDATEEDIRKLCDEAKEY----------------GFAAVCVNPCFVPLAREALKG---SGVKVCTVIGF 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 130 PAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILATGELgSLTNVYKASLVA 209
Cdd:cd00959  62 PLGATTTEVKVAEAREAIADGADEIDMVINIGALKSGDYEAVYEEIAAVVEACGGAPLKVILETGLL-TDEEIIKACEIA 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27777677 210 MMAGSDFIKTSTGKETVNATFPVAIVMLRAIRdffwktgNKVGFKPAGGIRTAKESLAWLSLVKEELG 277
Cdd:cd00959 141 IEAGADFIKTSTGFGPGGATVEDVKLMKEAVG-------GRVGVKAAGGIRTLEDALAMIEAGATRIG 201
PRK05283 PRK05283
deoxyribose-phosphate aldolase; Provisional
48-297 7.08e-69

deoxyribose-phosphate aldolase; Provisional


Pssm-ID: 235387  Cd Length: 257  Bit Score: 215.22  E-value: 7.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   48 LKAVTFIDLTTLSGDDTFSNVQRLCYKAKYPIRadllkalnmddkgiTTAAVCVYPARVCDAVKALKAAGC-SIPVASVa 126
Cdd:PRK05283   8 LRALSLMDLTTLNDDDTDEKVIALCHQAKTPVG--------------NTAAICIYPRFIPIARKTLREQGTpEIRIATV- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  127 TGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAH-LKTILATGELGSLTNVYKA 205
Cdd:PRK05283  73 TNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFELVKACKEACAANVlLKVIIETGELKDEALIRKA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  206 SLVAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDFfwKTGNKVGFKPAGGIRTAKESLAWLSLVKEELGDEWLTPDL 285
Cdd:PRK05283 153 SEIAIKAGADFIKTSTGKVPVNATLEAARIMLEVIRDM--GVAKTVGFKPAGGVRTAEDAAQYLALADEILGADWADARH 230
                        250
                 ....*....|..
gi 27777677  286 FRIGASSLLSDI 297
Cdd:PRK05283 231 FRFGASSLLASL 242
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
43-308 1.48e-65

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 223351  Cd Length: 228  Bit Score: 205.55  E-value: 1.48e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  43 QAAWLlKAVTFIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKAAGcSIPV 122
Cdd:COG0274   2 KASRM-QLAKLIDHTLLKPDATEEDIARLCAEAKEY----------------GFAAVCVNPSYVPLAKEALKGST-VVRV 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 123 ASVaTGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGE-AHLKTILATGELGSLTN 201
Cdd:COG0274  64 CTV-IGFPLGANTTAVKAAEAREAIENGADEIDMVINIGALKSGNWEAVEREIRAVVEACADaVVLKVILETGLLTDEEK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 202 VyKASLVAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKVGFKPAGGIRTAKESLAWLslvkeELGdewl 281
Cdd:COG0274 143 R-KACEIAIEAGADFVKTSTGFSAGGATVEDVKLMKETV-------GGRVGVKASGGIRTAEDAKAMI-----EAG---- 205
                       250       260
                ....*....|....*....|....*..
gi 27777677 282 tpdLFRIGASSLLsDIERQIYHHVTGR 308
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 ...
54-271 2.08e-54

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  Cd Length: 201  Bit Score: 175.98  E-value: 2.08e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  54 IDLTTLSGDDTFSNVQRLCYKAKypiradllkalnmdDKGIttAAVCVYPARVCDAVKALKAAGcsiPVASVATGFPAGQ 133
Cdd:cd00945   1 IDLTLLHPDATLEDIAKLCDEAI--------------EYGF--AAVCVNPGYVRLAADALAGSD---VPVIVVVGFPTGL 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 134 THLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKAC-GEAHLKTILATGELGSLTNVYKASLVAMMA 212
Cdd:cd00945  62 TTTEVKVAEVEEAIDLGADEIDVVINIGSLKEGDWEEVLEEIAAVVEAAdGGLPLKVILETRGLKTADEIAKAARIAAEA 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27777677 213 GSDFIKTSTGKETVNATFPVAIVMLRAIrdffwktGNKVGFKPAGGIRTAKESLAWLSL 271
Cdd:cd00945 142 GADFIKTSTGFGGGGATVEDVKLMKEAV-------GGRVGVKAAGGIKTLEDALAAIEA 193
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-291 2.52e-45

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: 153.00  E-value: 2.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677    53 FIDLTTLSGDDTFSNVQRLCYKAKYPiradllkalnmddkgiTTAAVCVYPARVCDAVKALKaaGCSIPVASVaTGFPAG 132
Cdd:TIGR00126   5 LIDHTALKADTTEEDIITLCAQAKTY----------------KFAAVCVNPSYVPLAKELLK--GTEVRICTV-VGFPLG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   133 QTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILATGElgsLTN--VYKASLVAM 210
Cdd:TIGR00126  66 ASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEVVYDDIRAVVEACAGVLLKVIIETGL---LTDeeIRKACEICI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   211 MAGSDFIKTSTGKETVNATFPVAIVMLRAIRDffwktgnKVGFKPAGGIRTAKESLAWLslvkeELGDEwltpdlfRIGA 290
Cdd:TIGR00126 143 DAGADFVKTSTGFGAGGATVEDVRLMRNTVGD-------TIGVKASGGVRTAEDAIAMI-----EAGAS-------RIGA 203

                  .
gi 27777677   291 S 291
Cdd:TIGR00126 204 S 204
PRK00507 PRK00507
deoxyribose-phosphate aldolase; Provisional
53-292 1.45e-39

deoxyribose-phosphate aldolase; Provisional


Pssm-ID: 234784  Cd Length: 221  Bit Score: 138.38  E-value: 1.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   53 FIDLTTLSGDDTFSNVQRLCYKAKypiradllkALNmddkgitTAAVCVYPARVCDAVKALKAAGcsIPVASVAtGFPAG 132
Cdd:PRK00507   9 YIDHTLLKPEATEEDIDKLCDEAK---------EYG-------FASVCVNPSYVKLAAELLKGSD--VKVCTVI-GFPLG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  133 QTHLKTRLEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILATGELgSLTNVYKASLVAMMA 212
Cdd:PRK00507  70 ANTTAVKAFEAKDAIANGADEIDMVINIGALKSGDWDAVEADIRAVVEAAGGAVLKVIIETCLL-TDEEKVKACEIAKEA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677  213 GSDFIKTSTGKETVNATfPVAIVMLRAIrdffwkTGNKVGFKPAGGIRTAKESLAWLslvkeELGdewltpdLFRIGASS 292
Cdd:PRK00507 149 GADFVKTSTGFSTGGAT-VEDVKLMRET------VGPRVGVKASGGIRTLEDALAMI-----EAG-------ATRLGTSA 209
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-259 1.76e-18

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: 396384  Cd Length: 235  Bit Score: 82.83  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677    54 IDLTTLSGDDTFSnvqrlcykAKYPIRADLlKALNMDDKGITTAAVCVYPARVCDAVKALKAAgcsipvASVATGFPAGQ 133
Cdd:pfam01791   6 MDQGVANGPDFAF--------AQTEQLEDL-KVLVKEAATPGANAVLLDPGYIARASRGYGKD------IGLIVALNHGT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   134 THLKTR------LEEIRLAVEDGATEIDVVINRTLVLTGQWEALYDEVTQFRKACGEAHLKTILA--------TGELGSL 199
Cdd:pfam01791  71 YLIPINqrdvdcVASVEEAKAMGADAVKVVLYYDVDGSEDEQQMLDEIGRVKEDCHEWGMPLILEgylrgeaiKDEKSDP 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677   200 TNVYKASLVAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTgnkvgFKPAGGI 259
Cdd:pfam01791 151 HLVADAARVGAELGADIVKVEYPKNMKNAGEEDADVFKDVIKAAPVPY-----VVLAGGV 205
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis];
103-199 3.32e-03

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 223120  Cd Length: 323  Bit Score: 38.46  E-value: 3.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777677 103 PARVCDAVKALKAAGCSIPVaSVatgfpagqthlKTRL---------EEIRLAVEDGATEIDVVINRTLVLTGQWEALYD 173
Cdd:COG0042 120 PELLAEIVKAMVEAVGDIPV-TV-----------KIRLgwddddilaLEIARILEDAGADALTVHGRTRAQGYLGPADWD 187
                        90       100
                ....*....|....*....|....*.
gi 27777677 174 EVTQFRKACGEahlKTILATGELGSL 199
Cdd:COG0042 188 YIKELKEAVPS---IPVIANGDIKSL 210
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH