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Conserved domains on  [gi|2120575650|gb|UDL17982|]
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dihydropyrimidine dehydrogenase, partial [Homo sapiens]

Protein Classification

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 ...
 7-41 2.51e-14

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 cd02940:

Pssm-ID: 473867  Cd Length: 299  Bit Score: 63.46  E-value: 2.51e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2120575650   7 GPGQSSFLNIELISEKTAAYWCQSVTELKADFPDN 41
Cdd:cd02940    66 GRGQIGFNNIELISEKPLEYWLKEIRELKKDFPDK 100
 
Name Accession Description Interval E-value
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 7-41 2.51e-14

Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. 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 the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239244  Cd Length: 299  Bit Score: 63.46  E-value: 2.51e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2120575650   7 GPGQSSFLNIELISEKTAAYWCQSVTELKADFPDN 41
Cdd:cd02940    66 GRGQIGFNNIELISEKPLEYWLKEIRELKKDFPDK 100
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
2-40 8.09e-04

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 34.15  E-value: 8.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2120575650   2 SGPMYG----PGQS--SFLNIELISEKTAAYWCQSVTELKADFPD 40
Cdd:PRK08318   55 SSPRFGalvkEDRRfiGFNNIELITDRPLEVNLREIRRVKRDYPD 99
 
Name Accession Description Interval E-value
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 7-41 2.51e-14

Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. 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 the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239244  Cd Length: 299  Bit Score: 63.46  E-value: 2.51e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2120575650   7 GPGQSSFLNIELISEKTAAYWCQSVTELKADFPDN 41
Cdd:cd02940    66 GRGQIGFNNIELISEKPLEYWLKEIRELKKDFPDK 100
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 6-41 9.98e-05

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: 36.56  E-value: 9.98e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2120575650   6 YGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDN 41
Cdd:cd02810    64 SYPEQLGILNSFGLPNLGLDVWLQDIAKAKKEFPGQ 99
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
2-40 8.09e-04

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 34.15  E-value: 8.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2120575650   2 SGPMYG----PGQS--SFLNIELISEKTAAYWCQSVTELKADFPD 40
Cdd:PRK08318   55 SSPRFGalvkEDRRfiGFNNIELITDRPLEVNLREIRRVKRDYPD 99
 
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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