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Conserved domains on  [gi|87126150|gb|ABD20664|]
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dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus USA300_FPR3757]

Protein Classification

dihydroneopterin aldolase( domain architecture ID 10087926)

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
DHNA_DHNTPE cd00534
Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain ...
 3-119 1.44e-49

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: 153.57  E-value: 1.44e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150   3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:cd00534   2 DRVFIKGLRFYTIHGVFEEERLLGQKFVVDLTLWYDLSKAGESDDLADTLNYAEVAKLIKKIVEGSPFKLIETLAEEIAD 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 87126150  83 RINSQYNRVMETKVRITKENPPIPGHYDGVGIEIVRE 119
Cdd:cd00534  82 ILLEDYPKVSAIKVKVEKPNAPIPASADGVGVEIERE 118
 
Name Accession Description Interval E-value
DHNA_DHNTPE cd00534
Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain ...
 3-119 1.44e-49

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: 153.57  E-value: 1.44e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150   3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:cd00534   2 DRVFIKGLRFYTIHGVFEEERLLGQKFVVDLTLWYDLSKAGESDDLADTLNYAEVAKLIKKIVEGSPFKLIETLAEEIAD 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 87126150  83 RINSQYNRVMETKVRITKENPPIPGHYDGVGIEIVRE 119
Cdd:cd00534  82 ILLEDYPKVSAIKVKVEKPNAPIPASADGVGVEIERE 118
FolB COG1539
Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is ...
 3-121 4.61e-48

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


Pssm-ID: 441148  Cd Length: 118  Bit Score: 149.50  E-value: 4.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150   3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:COG1539   2 DRIFLEGLRVYAYHGVYDEERELGQRFVVDLELELDLRKAAASDDLADTVDYAEVAEAIKELVEGEHFNLIETLAERIAD 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 87126150  83 RINSQYNRVMETKVRITKENPPIPghYDGVGIEIVRENK 121
Cdd:COG1539  82 RLLAEFPRVEAVRVRVRKPDAPIG--ADSVGVEIERSRK 118
FolB pfam02152
Dihydroneopterin aldolase; This enzyme EC:4.1.2.25 catalyzes the conversion of 7, ...
 5-116 9.58e-46

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: 143.75  E-value: 9.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150     5 IFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIANRI 84
Cdd:pfam02152   1 IFIKGLRFYAYHGVYPEERRLGQRFVVDLELWLDLSKAAATDDLEDTVDYAEVYEAVKELVEGEPFKLLETLAERIADRL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 87126150    85 NSQYNRVMETKVRITKENPPIPGHYDGVGIEI 116
Cdd:pfam02152  81 LEEFPGVEAVRVRVEKPNAPIPGPADSVGVEI 112
folB TIGR00525
dihydroneopterin aldolase; This model describes a bacterial dihydroneopterin aldolase, shown ...
 3-118 4.75e-43

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: 137.07  E-value: 4.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150     3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:TIGR00525   1 DRVFIEGLEVFAYHGVFDHERVLGQRFVVDLELSVDETKAAESDDLGDTVNYAELYSAIEEIVAEKPRDLIETVAYRIAD 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 87126150    83 RINSQYNRVMETKVRITKENPPIPGHYDGVGIEIVR 118
Cdd:TIGR00525  81 RLFADFPQVQRVKVRVSKPNAPIPGHLDDVSVEIRR 116
FolB smart00905
Dihydroneopterin aldolase; Dihydroneopterin aldolase catalyses the conversion of 7, ...
 5-118 4.02e-40

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: 129.54  E-value: 4.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150      5 IFLKGMRFYGYHGALSAENEIGQIFKVDVTLKV-DLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIANR 83
Cdd:smart00905   1 IFIKGLRFYAYIGVLDWERELGQRFVVDLELAWdDLRKAAESDDLEDTVDYAEVSERIKELVEGSRFKLIETLAERIADL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 87126150     84 INSQYnRVMETKVRITKENPPIPGHYDgVGIEIVR 118
Cdd:smart00905  81 LLEDF-GVEAVRVKVTKPNAPIPGDSD-VGVEIER 113
folB PRK11593
bifunctional dihydroneopterin aldolase/7,8-dihydroneopterin epimerase;
3-118 2.60e-04

bifunctional dihydroneopterin aldolase/7,8-dihydroneopterin epimerase;


Pssm-ID: 183219  Cd Length: 119  Bit Score: 37.86  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150    3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:PRK11593   2 DIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETVISHVEGARFALVERVAEEVAE 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 87126150   83 RINSQYNrvmETKVRITKENPPIPGHYDGVGIEIVR 118
Cdd:PRK11593  82 LLLARFN---SPWVRIKLSKPGAVARAANVGVIIER 114
 
Name Accession Description Interval E-value
DHNA_DHNTPE cd00534
Dihydroneopterin aldolase (DHNA) and 7,8-dihydroneopterin triphosphate epimerase domain ...
 3-119 1.44e-49

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: 153.57  E-value: 1.44e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150   3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:cd00534   2 DRVFIKGLRFYTIHGVFEEERLLGQKFVVDLTLWYDLSKAGESDDLADTLNYAEVAKLIKKIVEGSPFKLIETLAEEIAD 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 87126150  83 RINSQYNRVMETKVRITKENPPIPGHYDGVGIEIVRE 119
Cdd:cd00534  82 ILLEDYPKVSAIKVKVEKPNAPIPASADGVGVEIERE 118
FolB COG1539
Dihydroneopterin aldolase [Coenzyme transport and metabolism]; Dihydroneopterin aldolase is ...
 3-121 4.61e-48

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


Pssm-ID: 441148  Cd Length: 118  Bit Score: 149.50  E-value: 4.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150   3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:COG1539   2 DRIFLEGLRVYAYHGVYDEERELGQRFVVDLELELDLRKAAASDDLADTVDYAEVAEAIKELVEGEHFNLIETLAERIAD 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 87126150  83 RINSQYNRVMETKVRITKENPPIPghYDGVGIEIVRENK 121
Cdd:COG1539  82 RLLAEFPRVEAVRVRVRKPDAPIG--ADSVGVEIERSRK 118
FolB pfam02152
Dihydroneopterin aldolase; This enzyme EC:4.1.2.25 catalyzes the conversion of 7, ...
 5-116 9.58e-46

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: 143.75  E-value: 9.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150     5 IFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIANRI 84
Cdd:pfam02152   1 IFIKGLRFYAYHGVYPEERRLGQRFVVDLELWLDLSKAAATDDLEDTVDYAEVYEAVKELVEGEPFKLLETLAERIADRL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 87126150    85 NSQYNRVMETKVRITKENPPIPGHYDGVGIEI 116
Cdd:pfam02152  81 LEEFPGVEAVRVRVEKPNAPIPGPADSVGVEI 112
folB TIGR00525
dihydroneopterin aldolase; This model describes a bacterial dihydroneopterin aldolase, shown ...
 3-118 4.75e-43

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: 137.07  E-value: 4.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150     3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:TIGR00525   1 DRVFIEGLEVFAYHGVFDHERVLGQRFVVDLELSVDETKAAESDDLGDTVNYAELYSAIEEIVAEKPRDLIETVAYRIAD 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 87126150    83 RINSQYNRVMETKVRITKENPPIPGHYDGVGIEIVR 118
Cdd:TIGR00525  81 RLFADFPQVQRVKVRVSKPNAPIPGHLDDVSVEIRR 116
FolB smart00905
Dihydroneopterin aldolase; Dihydroneopterin aldolase catalyses the conversion of 7, ...
 5-118 4.02e-40

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: 129.54  E-value: 4.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150      5 IFLKGMRFYGYHGALSAENEIGQIFKVDVTLKV-DLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIANR 83
Cdd:smart00905   1 IFIKGLRFYAYIGVLDWERELGQRFVVDLELAWdDLRKAAESDDLEDTVDYAEVSERIKELVEGSRFKLIETLAERIADL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 87126150     84 INSQYnRVMETKVRITKENPPIPGHYDgVGIEIVR 118
Cdd:smart00905  81 LLEDF-GVEAVRVKVTKPNAPIPGDSD-VGVEIER 113
folB_dom TIGR00526
FolB domain; Two paralogous genes of E. coli, folB (dihydroneopterin aldolase) and folX ...
 3-120 2.96e-28

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: 99.70  E-value: 2.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150     3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:TIGR00526   2 DRVHIKNLEMHTIIGVFEWERLLPQKVVVDLTLGYDASKAANSDDLSDSLNYAEIASNITKFVEENPFKLIETLAKSVSE 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 87126150    83 RINSQYNRVMETKVRITKENpPIPGHYDGVGIEIVREN 120
Cdd:TIGR00526  82 VVLDDYQKVTEVELEVSKPK-PIPLLADGVSVIIRRER 118
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
 2-119 1.65e-22

Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with different functions: dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA) , GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl tetrahydropterin synthetase (PTPS), and uricase (UO,uroate/urate oxidase). They bind to substrates belonging to the purine or pterin families, and share a fold-related binding site with a glutamate or glutamine residue anchoring the substrate and a lot of conserved interactions. They also share a similar oligomerization mode: several T-folds join together to form a beta(2n)alpha(n) barrel, then two barrels join together in a head-to-head fashion to made up the native enzymes. The functional enzyme is a tetramer for UO, a hexamer for PTPS, an octamer for DHNA/DHNTPE and a decamer for GTPCH-1. The substrate is located in a deep and narrow pocket at the interface between monomers. In PTPS, the active site is located at the interface of three monomers, two from one trimer and one from the other trimer. In GTPCH-1, it is also located at the interface of three subunits, two from one pentamer and one from the other pentamer. There are four equivalent active sites in UO, six in PTPS, eight in DHNA/DHNTPE and ten in GTPCH-1. Each globular multimeric enzyme encloses a tunnel which is lined with charged residues for DHNA and UO, and with basic residues in PTPS. The N and C-terminal ends are located on one side of the T-fold while the residues involved in the catalytic activity are located at the opposite side. In PTPS, UO and DHNA/DHNTPE, the N and C-terminal extremities of the enzyme are located on the exterior side of the functional multimeric enzyme. In GTPCH-1, the extra C-terminal helix places the extremity inside the tunnel.


Pssm-ID: 238351  Cd Length: 122  Bit Score: 85.19  E-value: 1.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150   2 QDTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKavNLLEHLAERIA 81
Cdd:cd00651   1 TDGVRVKDLLKVTRLGFVTLERTVGQIFEVDVTLSWDGKKAAASDDVATDTVYNTIYRLAKEYVEGS--QLIERLAEEIA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 87126150  82 NRINSQYNR-VMETKVRITKENPPIPG-----HYDGVGIEIVRE 119
Cdd:cd00651  79 YLIAEHFLSsVAEVKVEEKKPHAVIPDrgvfkPTDSPGVTIERG 122
folB PRK11593
bifunctional dihydroneopterin aldolase/7,8-dihydroneopterin epimerase;
3-118 2.60e-04

bifunctional dihydroneopterin aldolase/7,8-dihydroneopterin epimerase;


Pssm-ID: 183219  Cd Length: 119  Bit Score: 37.86  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87126150    3 DTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLAEAGRTDNVIDTVHYGEVFEEVKSIMEGKAVNLLEHLAERIAN 82
Cdd:PRK11593   2 DIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETVISHVEGARFALVERVAEEVAE 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 87126150   83 RINSQYNrvmETKVRITKENPPIPGHYDGVGIEIVR 118
Cdd:PRK11593  82 LLLARFN---SPWVRIKLSKPGAVARAANVGVIIER 114
 
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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