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Conserved domains on  [gi|151425422|dbj|BAF72925|]
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conserved hypothetical protein [Sulfurovum sp. NBC37-1]

Protein Classification

dihydroneopterin aldolase( domain architecture ID 10003951)

dihydroneopterin aldolase (DHNA) catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin and may also catalyze the epimerization of carbon 2' of dihydroneopterin to dihydromonapterin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FolB COG1539
Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is ...
 2-98 3.25e-12

Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is part of the Pathway/BioSystem: Folate biosynthesis


:

Pssm-ID: 441148  Cd Length: 118  Bit Score: 57.83  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422   2 TIHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDYDE-------ENFIDYADIVILIETELKEKRYelleeallglK-- 72
Cdd:COG1539    3 RIFLEGLRVYAYHGVYDEERELGQRFVVDLELELDLRKaaasddlADTVDYAEVAEAIKELVEGEHF----------Nli 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 151425422  73 --------SVITTAYPQIETLSLKITKPDILPKC 98
Cdd:COG1539   73 etlaeriaDRLLAEFPRVEAVRVRVRKPDAPIGA 106
 
Name Accession Description Interval E-value
FolB COG1539
Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is ...
 2-98 3.25e-12

Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441148  Cd Length: 118  Bit Score: 57.83  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422   2 TIHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDYDE-------ENFIDYADIVILIETELKEKRYelleeallglK-- 72
Cdd:COG1539    3 RIFLEGLRVYAYHGVYDEERELGQRFVVDLELELDLRKaaasddlADTVDYAEVAEAIKELVEGEHF----------Nli 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 151425422  73 --------SVITTAYPQIETLSLKITKPDILPKC 98
Cdd:COG1539   73 etlaeriaDRLLAEFPRVEAVRVRVRKPDAPIGA 106
FolB smart00905
Dihydroneopterin aldolase; Dihydroneopterin aldolase catalyses the conversion of 7, ...
 3-96 1.36e-10

Dihydroneopterin aldolase; Dihydroneopterin aldolase catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. In the opportunistic pathogen Pneumocystis carinii, dihydroneopterin aldolase function is expressed as the N-terminal portion of the multifunctional folic acid synthesis protein (Fas). This region encompasses two domains, FasA and FasB, which are 27% amino acid identical. FasA and FasB also share significant amino acid sequence similarity with bacterial dihydroneopterin aldolases. This region consists of two tandem sequences each homologous to folB and which form tetramers.


Pssm-ID: 214902  Cd Length: 113  Bit Score: 53.66  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422     3 IHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDY--------DEENFIDYADIVILIETELKEKRYELLEEALLGLKSV 74
Cdd:smart00905   1 IFIKGLRFYAYIGVLDWERELGQRFVVDLELAWDDlrkaaesdDLEDTVDYAEVSERIKELVEGSRFKLIETLAERIADL 80

                           90       100
                   ....*....|....*....|..
gi 151425422    75 ItTAYPQIETLSLKITKPDILP 96
Cdd:smart00905  81 L-LEDFGVEAVRVKVTKPNAPI 101
FolB pfam02152
Dihydroneopterin aldolase; This enzyme EC:4.1.2.25 catalyzes the conversion of 7, ...
 3-93 1.29e-09

Dihydroneopterin aldolase; This enzyme EC:4.1.2.25 catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate.


Pssm-ID: 460466  Cd Length: 113  Bit Score: 51.31  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422    3 IHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDYDE-------ENFIDYADIVILIETELKEKRYelleeallglKSV- 74
Cdd:pfam02152   1 IFIKGLRFYAYHGVYPEERRLGQRFVVDLELWLDLSKaaatddlEDTVDYAEVYEAVKELVEGEPF----------KLLe 70

                          90       100
                  ....*....|....*....|....*...
gi 151425422   75 ---------ITTAYPQIETLSLKITKPD 93
Cdd:pfam02152  71 tlaeriadrLLEEFPGVEAVRVRVEKPN 98
DHNA_DHNTPE cd00534
Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain ...
 2-96 2.17e-09

Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain (DHNTPE); these enzymes have been designated folB and folX, respectively. Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids, as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is DHNA which catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. Though it is known that DHNTPE catalyzes the epimerization of dihydroneopterin triphosphate to dihydromonapterin triphosphate, the biological role of this enzyme is still unclear. It is hypothesized that it is not an essential protein since a folX knockout in E. coli has a normal phenotype and the fact that folX is not present in H. influenza. In addition both enzymes have been shown to be able to compensate for the other's activity albeit at slower reaction rates. The functional enzyme for both is an octamer of identical subunits. Mammals lack many of the enzymes in the folate pathway including, DHNA and DHNTPE.


Pssm-ID: 238298  Cd Length: 118  Bit Score: 50.72  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422   2 TIHIKALTLDVIIGLLDFEREHTQKVIIDTEADYD-------YDEENFIDYADIVILIETELKEKRYELLEEALLGLKSV 74
Cdd:cd00534    3 RVFIKGLRFYTIHGVFEEERLLGQKFVVDLTLWYDlskagesDDLADTLNYAEVAKLIKKIVEGSPFKLIETLAEEIADI 82

                         90       100
                 ....*....|....*....|..
gi 151425422  75 ITTAYPQIETLSLKITKPDILP 96
Cdd:cd00534   83 LLEDYPKVSAIKVKVEKPNAPI 104
folB_dom TIGR00526
FolB domain; Two paralogous genes of E. coli, folB (dihydroneopterin aldolase) and folX ...
 3-96 5.63e-09

FolB domain; Two paralogous genes of E. coli, folB (dihydroneopterin aldolase) and folX (d-erythro-7,8-dihydroneopterin triphosphate epimerase) are homologous to each other and homo-octameric. In Pneumocystis carinii, a multifunctional enzyme of folate synthesis has an N-terminal region active as dihydroneopterin aldolase. This region consists of two tandem sequences each homologous to folB and forms tetramers.


Pssm-ID: 273120  Cd Length: 118  Bit Score: 49.62  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422    3 IHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDY-------DEENFIDYADIVILIETELKEKRYELLEEALLGLKSVI 75
Cdd:TIGR00526   4 VHIKNLEMHTIIGVFEWERLLPQKVVVDLTLGYDAskaansdDLSDSLNYAEIASNITKFVEENPFKLIETLAKSVSEVV 83

                          90       100
                  ....*....|....*....|.
gi 151425422   76 TTAYPQIETLSLKITKPDILP 96
Cdd:TIGR00526  84 LDDYQKVTEVELEVSKPKPIP 104
 
Name Accession Description Interval E-value
FolB COG1539
Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is ...
 2-98 3.25e-12

Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441148  Cd Length: 118  Bit Score: 57.83  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422   2 TIHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDYDE-------ENFIDYADIVILIETELKEKRYelleeallglK-- 72
Cdd:COG1539    3 RIFLEGLRVYAYHGVYDEERELGQRFVVDLELELDLRKaaasddlADTVDYAEVAEAIKELVEGEHF----------Nli 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 151425422  73 --------SVITTAYPQIETLSLKITKPDILPKC 98
Cdd:COG1539   73 etlaeriaDRLLAEFPRVEAVRVRVRKPDAPIGA 106
FolB smart00905
Dihydroneopterin aldolase; Dihydroneopterin aldolase catalyses the conversion of 7, ...
 3-96 1.36e-10

Dihydroneopterin aldolase; Dihydroneopterin aldolase catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. In the opportunistic pathogen Pneumocystis carinii, dihydroneopterin aldolase function is expressed as the N-terminal portion of the multifunctional folic acid synthesis protein (Fas). This region encompasses two domains, FasA and FasB, which are 27% amino acid identical. FasA and FasB also share significant amino acid sequence similarity with bacterial dihydroneopterin aldolases. This region consists of two tandem sequences each homologous to folB and which form tetramers.


Pssm-ID: 214902  Cd Length: 113  Bit Score: 53.66  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422     3 IHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDY--------DEENFIDYADIVILIETELKEKRYELLEEALLGLKSV 74
Cdd:smart00905   1 IFIKGLRFYAYIGVLDWERELGQRFVVDLELAWDDlrkaaesdDLEDTVDYAEVSERIKELVEGSRFKLIETLAERIADL 80

                           90       100
                   ....*....|....*....|..
gi 151425422    75 ItTAYPQIETLSLKITKPDILP 96
Cdd:smart00905  81 L-LEDFGVEAVRVKVTKPNAPI 101
FolB pfam02152
Dihydroneopterin aldolase; This enzyme EC:4.1.2.25 catalyzes the conversion of 7, ...
 3-93 1.29e-09

Dihydroneopterin aldolase; This enzyme EC:4.1.2.25 catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate.


Pssm-ID: 460466  Cd Length: 113  Bit Score: 51.31  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422    3 IHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDYDE-------ENFIDYADIVILIETELKEKRYelleeallglKSV- 74
Cdd:pfam02152   1 IFIKGLRFYAYHGVYPEERRLGQRFVVDLELWLDLSKaaatddlEDTVDYAEVYEAVKELVEGEPF----------KLLe 70

                          90       100
                  ....*....|....*....|....*...
gi 151425422   75 ---------ITTAYPQIETLSLKITKPD 93
Cdd:pfam02152  71 tlaeriadrLLEEFPGVEAVRVRVEKPN 98
DHNA_DHNTPE cd00534
Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain ...
 2-96 2.17e-09

Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain (DHNTPE); these enzymes have been designated folB and folX, respectively. Folate derivatives are essential cofactors in the biosynthesis of purines, pyrimidines, and amino acids, as well as formyl-tRNA. Mammalian cells are able to utilize pre-formed folates after uptake by a carrier-mediated active transport system. Most microbes and plants lack this system and must synthesize folates de novo from guanosine triphosphate. One enzyme from this pathway is DHNA which catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. Though it is known that DHNTPE catalyzes the epimerization of dihydroneopterin triphosphate to dihydromonapterin triphosphate, the biological role of this enzyme is still unclear. It is hypothesized that it is not an essential protein since a folX knockout in E. coli has a normal phenotype and the fact that folX is not present in H. influenza. In addition both enzymes have been shown to be able to compensate for the other's activity albeit at slower reaction rates. The functional enzyme for both is an octamer of identical subunits. Mammals lack many of the enzymes in the folate pathway including, DHNA and DHNTPE.


Pssm-ID: 238298  Cd Length: 118  Bit Score: 50.72  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422   2 TIHIKALTLDVIIGLLDFEREHTQKVIIDTEADYD-------YDEENFIDYADIVILIETELKEKRYELLEEALLGLKSV 74
Cdd:cd00534    3 RVFIKGLRFYTIHGVFEEERLLGQKFVVDLTLWYDlskagesDDLADTLNYAEVAKLIKKIVEGSPFKLIETLAEEIADI 82

                         90       100
                 ....*....|....*....|..
gi 151425422  75 ITTAYPQIETLSLKITKPDILP 96
Cdd:cd00534   83 LLEDYPKVSAIKVKVEKPNAPI 104
folB_dom TIGR00526
FolB domain; Two paralogous genes of E. coli, folB (dihydroneopterin aldolase) and folX ...
 3-96 5.63e-09

FolB domain; Two paralogous genes of E. coli, folB (dihydroneopterin aldolase) and folX (d-erythro-7,8-dihydroneopterin triphosphate epimerase) are homologous to each other and homo-octameric. In Pneumocystis carinii, a multifunctional enzyme of folate synthesis has an N-terminal region active as dihydroneopterin aldolase. This region consists of two tandem sequences each homologous to folB and forms tetramers.


Pssm-ID: 273120  Cd Length: 118  Bit Score: 49.62  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422    3 IHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDY-------DEENFIDYADIVILIETELKEKRYELLEEALLGLKSVI 75
Cdd:TIGR00526   4 VHIKNLEMHTIIGVFEWERLLPQKVVVDLTLGYDAskaansdDLSDSLNYAEIASNITKFVEENPFKLIETLAKSVSEVV 83

                          90       100
                  ....*....|....*....|.
gi 151425422   76 TTAYPQIETLSLKITKPDILP 96
Cdd:TIGR00526  84 LDDYQKVTEVELEVSKPKPIP 104
folB TIGR00525
dihydroneopterin aldolase; This model describes a bacterial dihydroneopterin aldolase, shown ...
 2-93 1.33e-04

dihydroneopterin aldolase; This model describes a bacterial dihydroneopterin aldolase, shown to form homo-octamers in E. coli. The equivalent activity is catalyzed by domains of larger folate biosynthesis proteins in other systems. The closely related parologous enzyme in E. coli, dihydroneopterin triphosphate epimerase, which is also homo-octameric, and dihydroneopterin aldolase domains of larger proteins, score below the trusted cutoff but may score well above the noise cutoff. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 213537  Cd Length: 116  Bit Score: 38.07  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151425422    2 TIHIKALTLDVIIGLLDFEREHTQKVIIDTEADYDY-------DEENFIDYADIVILIETELKEKRYELLEEALLGLKSV 74
Cdd:TIGR00525   2 RVFIEGLEVFAYHGVFDHERVLGQRFVVDLELSVDEtkaaesdDLGDTVNYAELYSAIEEIVAEKPRDLIETVAYRIADR 81

                          90
                  ....*....|....*....
gi 151425422   75 ITTAYPQIETLSLKITKPD 93
Cdd:TIGR00525  82 LFADFPQVQRVKVRVSKPN 100
 
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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