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Conserved domains on  [gi|254772434|sp|C3PI20|]
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RecName: Full=Deoxyribose-phosphate aldolase; Short=DERA; AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase; AltName: Full=Phosphodeoxyriboaldolase; Short=Deoxyriboaldolase

Protein Classification

2-deoxyribose-5-phosphate aldolase( domain architecture ID 10000957)

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

CATH:  3.20.20.70|3.20.20.70
EC:  4.1.2.4
Gene Symbol:  deoC
Gene Ontology:  GO:0004139|GO:0009264|GO:0004139|GO:0009264
PubMed:  12206759|30284013
SCOP:  4003216

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
6-218 1.83e-104

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


:

Pssm-ID: 440043  Cd Length: 219  Bit Score: 300.06  E-value: 1.83e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   6 DVAQMIDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDVP----SGVHVATVVGFPSGAVKTEVKAAETGRAV 81
Cdd:COG0274    2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEYGFAAVCVNPCYVPLAAEllkgSGVKVATVIGFPLGATTTEVKVAEAKEAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  82 KDGAEEIDMVVNLSQVKSHDYAAVEADIKAVRDAApAPVIVKVIIESAALDDEEIVATCQAAERAGADFVKTSTGFHPaG 161
Cdd:COG0274   82 ADGADEIDMVINIGALKSGDYDAVEEEIAAVVEAA-GGAVLKVILETGLLTDEEIRKACELAIEAGADFVKTSTGFGP-G 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 254772434 162 GASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLSSSAAVLEGFEA 218
Cdd:COG0274  160 GATVEDVRLMRETVGGRVGVKASGGIRTLEDALAMIEAGATRIGTSSGVAILEGLEA 216
 
Name Accession Description Interval E-value
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
6-218 1.83e-104

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 300.06  E-value: 1.83e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   6 DVAQMIDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDVP----SGVHVATVVGFPSGAVKTEVKAAETGRAV 81
Cdd:COG0274    2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEYGFAAVCVNPCYVPLAAEllkgSGVKVATVIGFPLGATTTEVKVAEAKEAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  82 KDGAEEIDMVVNLSQVKSHDYAAVEADIKAVRDAApAPVIVKVIIESAALDDEEIVATCQAAERAGADFVKTSTGFHPaG 161
Cdd:COG0274   82 ADGADEIDMVINIGALKSGDYDAVEEEIAAVVEAA-GGAVLKVILETGLLTDEEIRKACELAIEAGADFVKTSTGFGP-G 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 254772434 162 GASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLSSSAAVLEGFEA 218
Cdd:COG0274  160 GATVEDVRLMRETVGGRVGVKASGGIRTLEDALAMIEAGATRIGTSSGVAILEGLEA 216
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
 7-207 2.96e-84

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: 248.60  E-value: 2.96e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   7 VAQMIDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDV----PSGVHVATVVGFPSGAVKTEVKAAETGRAVK 82
Cdd:cd00959    1 LASLIDHTLLKPDATEEDIRKLCDEAKEYGFAAVCVNPCFVPLARealkGSGVKVCTVIGFPLGATTTEVKVAEAREAIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  83 DGAEEIDMVVNLSQVKSHDYAAVEADIKAVRDAAPaPVIVKVIIESAALDDEEIVATCQAAERAGADFVKTSTGFHPaGG 162
Cdd:cd00959   81 DGADEIDMVINIGALKSGDYEAVYEEIAAVVEACG-GAPLKVILETGLLTDEEIIKACEIAIEAGADFIKTSTGFGP-GG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 254772434 163 ASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLS 207
Cdd:cd00959  159 ATVEDVKLMKEAVGGRVGVKAAGGIRTLEDALAMIEAGATRIGTS 203
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
 6-214 2.00e-64

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: 198.46  E-value: 2.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434    6 DVAQMIDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDVP----SGVHVATVVGFPSGAVKTEVKAAETGRAV 81
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTYKFAAVCVNPSYVPLAKEllkgTEVRICTVVGFPLGASTTDVKLYETKEAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   82 KDGAEEIDMVVNLSQVKSHDYAAVEADIKAVRDAApAPVIVKVIIESAALDDEEIVATCQAAERAGADFVKTSTGFHpAG 161
Cdd:TIGR00126  81 KYGADEVDMVINIGALKDGNEEVVYDDIRAVVEAC-AGVLLKVIIETGLLTDEEIRKACEICIDAGADFVKTSTGFG-AG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 254772434  162 GASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLSSSAAVLE 214
Cdd:TIGR00126 159 GATVEDVRLMRNTVGDTIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAIIQ 211
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
107-202 4.80e-07

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 49.39  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 107 ADIKAVRD--AAPAPVIVKViieSAALDDEEIVATCQAAERAGAD------------FVKTSTGFHPAGG--------AS 164
Cdd:PRK05286 199 AALKEAQAelHGYVPLLVKI---APDLSDEELDDIADLALEHGIDgviatnttlsrdGLKGLPNADEAGGlsgrplfeRS 275

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 254772434 165 VHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGAT 202
Cdd:PRK05286 276 TEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGAS 313
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
 24-215 1.49e-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: 47.38  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   24 QVAALAKEAGELGTYSICVSPNQL-PVDVPSGVHVATVVGFPSG------AVKTEVKAAETGRAVKDGAEEIDMVVNLSQ 96
Cdd:pfam01791  22 DPKVLVAEAATPGANAVLLDPGFIaRAHRGYGKDIGLIVALNHGtdlipiNGRDVDCVASVEEAKAMGADAVKVVVYYRV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   97 VKSHDYAAVEADIKAVRDAAPA---PVIVKVIIESAALDDE---EIVATC-QAAERAGADFVKTSTGFHpAGGASVHAVK 169
Cdd:pfam01791 102 DGSEEEQQMLDEIGRVKEDCHEwgmPLILEGYLRGEAIKDEkdpDLVADAaRLGAELGADIVKVSYPKN-MKNAGEEDAD 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 254772434  170 LMAETVEG--RLGVKASGGIRDAEAAQ----AMIDAGATrlGLSSSAAVLEG 215
Cdd:pfam01791 181 VFKRVIKAapVPYVVLAGGVSEEDFLRtvrdAMIEAGAM--GVSSGRNIFQK 230
 
Name Accession Description Interval E-value
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
6-218 1.83e-104

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 300.06  E-value: 1.83e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   6 DVAQMIDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDVP----SGVHVATVVGFPSGAVKTEVKAAETGRAV 81
Cdd:COG0274    2 ELAKLIDHTLLKPDATEEDIEKLCEEAKEYGFAAVCVNPCYVPLAAEllkgSGVKVATVIGFPLGATTTEVKVAEAKEAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  82 KDGAEEIDMVVNLSQVKSHDYAAVEADIKAVRDAApAPVIVKVIIESAALDDEEIVATCQAAERAGADFVKTSTGFHPaG 161
Cdd:COG0274   82 ADGADEIDMVINIGALKSGDYDAVEEEIAAVVEAA-GGAVLKVILETGLLTDEEIRKACELAIEAGADFVKTSTGFGP-G 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 254772434 162 GASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLSSSAAVLEGFEA 218
Cdd:COG0274  160 GATVEDVRLMRETVGGRVGVKASGGIRTLEDALAMIEAGATRIGTSSGVAILEGLEA 216
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
 7-207 2.96e-84

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: 248.60  E-value: 2.96e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   7 VAQMIDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDV----PSGVHVATVVGFPSGAVKTEVKAAETGRAVK 82
Cdd:cd00959    1 LASLIDHTLLKPDATEEDIRKLCDEAKEYGFAAVCVNPCFVPLARealkGSGVKVCTVIGFPLGATTTEVKVAEAREAIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  83 DGAEEIDMVVNLSQVKSHDYAAVEADIKAVRDAAPaPVIVKVIIESAALDDEEIVATCQAAERAGADFVKTSTGFHPaGG 162
Cdd:cd00959   81 DGADEIDMVINIGALKSGDYEAVYEEIAAVVEACG-GAPLKVILETGLLTDEEIIKACEIAIEAGADFIKTSTGFGP-GG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 254772434 163 ASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLS 207
Cdd:cd00959  159 ATVEDVKLMKEAVGGRVGVKAAGGIRTLEDALAMIEAGATRIGTS 203
deoC TIGR00126
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
 6-214 2.00e-64

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: 198.46  E-value: 2.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434    6 DVAQMIDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDVP----SGVHVATVVGFPSGAVKTEVKAAETGRAV 81
Cdd:TIGR00126   1 ELAKLIDHTALKADTTEEDIITLCAQAKTYKFAAVCVNPSYVPLAKEllkgTEVRICTVVGFPLGASTTDVKLYETKEAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   82 KDGAEEIDMVVNLSQVKSHDYAAVEADIKAVRDAApAPVIVKVIIESAALDDEEIVATCQAAERAGADFVKTSTGFHpAG 161
Cdd:TIGR00126  81 KYGADEVDMVINIGALKDGNEEVVYDDIRAVVEAC-AGVLLKVIIETGLLTDEEIRKACEICIDAGADFVKTSTGFG-AG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 254772434  162 GASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLSSSAAVLE 214
Cdd:TIGR00126 159 GATVEDVRLMRNTVGDTIGVKASGGVRTAEDAIAMIEAGASRIGASAGVAIIQ 211
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
 11-207 1.46e-56

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: 178.29  E-value: 1.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  11 IDHTLLKPEATPDQVAALAKEAGELGTYSICVSPNQLPVDVP----SGVHVATVVGFPSGAVKTEVKAAETGRAVKDGAE 86
Cdd:cd00945    1 IDLTLLHPDATLEDIAKLCDEAIEYGFAAVCVNPGYVRLAADalagSDVPVIVVVGFPTGLTTTEVKVAEVEEAIDLGAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  87 EIDMVVNLSQVKSHDYAAVEADIKAVRDAAPAPVIVKVIIESAAL-DDEEIVATCQAAERAGADFVKTSTGFHPaGGASV 165
Cdd:cd00945   81 EIDVVINIGSLKEGDWEEVLEEIAAVVEAADGGLPLKVILETRGLkTADEIAKAARIAAEAGADFIKTSTGFGG-GGATV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 254772434 166 HAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLS 207
Cdd:cd00945  160 EDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 88-202 2.37e-11

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 61.63  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  88 IDMV-VNLS--QVK------SHDYAAVEADIKAVRDAAPAPVIVKViiesaALDDEEIVATCQAAERAGADFV------- 151
Cdd:COG0167  119 ADYLeLNIScpNTPgggralGQDPEALAELLAAVKAATDKPVLVKL-----APDLTDIVEIARAAEEAGADGViainttl 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254772434 152 --------KTSTGFHPAGG--------ASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGAT 202
Cdd:COG0167  194 graidletRRPVLANEAGGlsgpalkpIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGAS 260
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 91-202 2.34e-07

Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.


Pssm-ID: 240089  Cd Length: 327  Bit Score: 50.19  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  91 VVNLSqvkS---------HDYAAVEADIKAVRDAAPA-----PVIVKViieSAALDDEEIVATCQAAERAGAD------- 149
Cdd:cd04738  165 VVNVS---SpntpglrdlQGKEALRELLTAVKEERNKlgkkvPLLVKI---APDLSDEELEDIADVALEHGVDgiiatnt 238

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254772434 150 -----FVKTSTGFHPAGG--------ASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGAT 202
Cdd:cd04738  239 tisrpGLLRSPLANETGGlsgaplkeRSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGAS 304
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 109-200 3.33e-07

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 49.88  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 109 IKAVRDAAPA--PVIVKVIIE---SAALDDEEIVATCQAAERAGADFVKTSTGFH-----------PAGGASVHAVKLMA 172
Cdd:cd02803  198 VAAVREAVGPdfPVGVRLSADdfvPGGLTLEEAIEIAKALEEAGVDALHVSGGSYespppiipppyVPEGYFLELAEKIK 277

                         90       100
                 ....*....|....*....|....*...
gi 254772434 173 ETVEGRLGvkASGGIRDAEAAQAMIDAG 200
Cdd:cd02803  278 KAVKIPVI--AVGGIRDPEVAEEILAEG 303
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
107-202 4.80e-07

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 49.39  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 107 ADIKAVRD--AAPAPVIVKViieSAALDDEEIVATCQAAERAGAD------------FVKTSTGFHPAGG--------AS 164
Cdd:PRK05286 199 AALKEAQAelHGYVPLLVKI---APDLSDEELDDIADLALEHGIDgviatnttlsrdGLKGLPNADEAGGlsgrplfeRS 275

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 254772434 165 VHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGAT 202
Cdd:PRK05286 276 TEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGAS 313
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 100-217 6.96e-07

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 48.50  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 100 HDYAAVEADIKAVRDAAPAPVIVKViieSAALDDEEIVATCQAAERAGADFVKTSTGF---------------HPAGG-- 162
Cdd:cd02810  145 QDPEAVANLLKAVKAAVDIPLLVKL---SPYFDLEDIVELAKAAERAGADGLTAINTIsgrvvdlktvgpgpkRGTGGls 221

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254772434 163 ------ASVHAVKLMAETVEGRLGVKASGGIRDAEAAQAMIDAGATRLGLsSSAAVLEGFE 217
Cdd:cd02810  222 gapirpLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQV-ATALMWDGPD 281
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
 24-215 1.49e-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: 47.38  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   24 QVAALAKEAGELGTYSICVSPNQL-PVDVPSGVHVATVVGFPSG------AVKTEVKAAETGRAVKDGAEEIDMVVNLSQ 96
Cdd:pfam01791  22 DPKVLVAEAATPGANAVLLDPGFIaRAHRGYGKDIGLIVALNHGtdlipiNGRDVDCVASVEEAKAMGADAVKVVVYYRV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434   97 VKSHDYAAVEADIKAVRDAAPA---PVIVKVIIESAALDDE---EIVATC-QAAERAGADFVKTSTGFHpAGGASVHAVK 169
Cdd:pfam01791 102 DGSEEEQQMLDEIGRVKEDCHEwgmPLILEGYLRGEAIKDEkdpDLVADAaRLGAELGADIVKVSYPKN-MKNAGEEDAD 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 254772434  170 LMAETVEG--RLGVKASGGIRDAEAAQ----AMIDAGATrlGLSSSAAVLEG 215
Cdd:pfam01791 181 VFKRVIKAapVPYVVLAGGVSEEDFLRtvrdAMIEAGAM--GVSSGRNIFQK 230
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 85-218 1.12e-04

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 42.15  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  85 AEEIDMV-VNLS--QVKSH------DYAAVEADIKAVRDAAPAPVIVKViiesaALDDEEIVATCQAAERAGAD---FVK 152
Cdd:cd04740  113 DAGADAIeLNIScpNVKGGgmafgtDPEAVAEIVKAVKKATDVPVIVKL-----TPNVTDIVEIARAAEEAGADgltLIN 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 153 TSTG-------FHPA-----GGASVHAVKLMA--------ETVEGRL-GVkasGGIRDAEAAQAMIDAGATRLGLSSsaA 211
Cdd:cd04740  188 TLKGmaidietRKPIlgnvtGGLSGPAIKPIAlrmvyqvyKAVEIPIiGV---GGIASGEDALEFLMAGASAVQVGT--A 262


                 ....*..
gi 254772434 212 VLEGFEA 218
Cdd:cd04740  263 NFVDPEA 269
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 72-198 1.08e-03

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 39.01  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  72 VKAAEtgRAVKDGAEEIDmvVNL----SQVKSHDYAA--------VEADIKAVRDAAPAPVIVKV-IIESaalDDEEIVA 138
Cdd:cd02801   70 AEAAK--IVEELGADGID--LNMgcpsPKVTKGGAGAallkdpelVAEIVRAVREAVPIPVTVKIrLGWD---DEEETLE 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254772434 139 TCQAAERAGADFV-----KTSTGFHPAggASVHAVKLMAETVegRLGVKASGGIRDAEAAQAMID 198
Cdd:cd02801  143 LAKALEDAGASALtvhgrTREQRYSGP--ADWDYIAEIKEAV--SIPVIANGDIFSLEDALRCLE 203
PRK07259 PRK07259
dihydroorotate dehydrogenase;
83-202 1.29e-03

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 38.98  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434  83 DGAEEIDMV-VNLS--QVKS------HDYAAVEADIKAVRDAAPAPVIVKViieSAALDDeeIVATCQAAERAGAD---F 150
Cdd:PRK07259 114 SKAPNVDAIeLNIScpNVKHggmafgTDPELAYEVVKAVKEVVKVPVIVKL---TPNVTD--IVEIAKAAEEAGADglsL 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254772434 151 VKTSTGFH-------PA-----GGASVHAVKLMA--------ETVegRLGVKASGGIRDAEAAQAMIDAGAT 202
Cdd:PRK07259 189 INTLKGMAidiktrkPIlanvtGGLSGPAIKPIAlrmvyqvyQAV--DIPIIGMGGISSAEDAIEFIMAGAS 258
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
 131-203 1.34e-03

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 38.88  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 131 LDDEEIVATCQAAERAGAD-FV-KTStgfhpaG-GASVHAVKLMAETVEG---RLGVK--ASGGIRDAEAAQAMIDAGAT 202
Cdd:COG0502   73 LSVEEILEAARAAKEAGARrFClVAS------GrDPSDRDFEKVLEIVRAikeELGLEvcASLGELSEEQAKRLKEAGVD 146


                 .
gi 254772434 203 R 203
Cdd:COG0502  147 R 147
OYE_like_2_FMN cd04733
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ...
 109-202 2.83e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240084 [Multi-domain]  Cd Length: 338  Bit Score: 37.95  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 109 IKAVRDAAPAPVIVKVIIESA-----ALDDEEIVATCQAAERAGADFVKTSTG--FHPAGGASVHA------------VK 169
Cdd:cd04733  206 YDAIRAAVGPGFPVGIKLNSAdfqrgGFTEEDALEVVEALEEAGVDLVELSGGtyESPAMAGAKKEstiareayflefAE 285

                         90       100       110
                 ....*....|....*....|....*....|...
gi 254772434 170 LMAETVEGRLGVkaSGGIRDAEAAQAMIDAGAT 202
Cdd:cd04733  286 KIRKVTKTPLMV--TGGFRTRAAMEQALASGAV 316
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 104-204 8.91e-03

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 36.50  E-value: 8.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254772434 104 AVEAdIKAVRDAAPAPVIVkvIIESAALD-------DEEIVATCQAAERAGADFVKTSTGFHPA----------GGASVH 166
Cdd:cd02930  190 PVEI-VRAVRAAVGEDFII--IYRLSMLDlveggstWEEVVALAKALEAAGADILNTGIGWHEArvptiatsvpRGAFAW 266

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 254772434 167 AVKLMAETVEgrLGVKASGGIRDAEAAQAMIDAGATRL 204
Cdd:cd02930  267 ATAKLKRAVD--IPVIASNRINTPEVAERLLADGDADM 302
 
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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