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Conserved domains on  [gi|2572895190|ref|NP_001411034|]
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GTP cyclohydrolase 1 isoform 5 [Homo sapiens]

Protein Classification

tunnelling fold family protein( domain architecture ID 365)

Tunnelling fold (T-fold) family protein such as dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA) , GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl tetrahydropterin synthetase (PTPS), and uricase (UO,uroate/urate oxidase)

PubMed:  10737935
SCOP:  3000283

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TFold super family cl00263
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
 17-152 9.31e-92

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.


The actual alignment was detected with superfamily member cd00642:

Pssm-ID: 469697 [Multi-domain]  Cd Length: 185  Bit Score: 263.86  E-value: 9.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAIT 96
Cdd:cd00642    50 DPKNTAIFDEDHDEMVIVKDITLFSMCEHHLVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQ 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2572895190  97 EALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:cd00642   130 EILGPQGVAVVIEATHMCMVMRGVRKPGSKTVTSAMLGVFKEDPKTREEFLRLIRK 185
 
Name Accession Description Interval E-value
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
 17-152 9.31e-92

GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate. The enzyme product is the precursor of tetrahydrofolate in eubacteria, fungi, and plants and of the folate analogs in methanogenic bacteria. In vertebrates and insects it is the biosynthtic precursor of tetrahydrobiopterin (BH4) which is involved in the formation of catacholamines, nitric oxide, and the stimulation of T lymphocytes. The biosynthetic reaction of BH4 is controlled by a regulatory protein GFRP which mediates feedback inhibition of GTP-CH-I by BH4. This inhibition is reversed by phenylalanine. The decameric GTP-CH-I forms a complex with two pentameric GFRP in the presence of phenylalanine or a combination of GTP and BH4, respectively.


Pssm-ID: 238349 [Multi-domain]  Cd Length: 185  Bit Score: 263.86  E-value: 9.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAIT 96
Cdd:cd00642    50 DPKNTAIFDEDHDEMVIVKDITLFSMCEHHLVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQ 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2572895190  97 EALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:cd00642   130 EILGPQGVAVVIEATHMCMVMRGVRKPGSKTVTSAMLGVFKEDPKTREEFLRLIRK 185
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
 17-152 3.25e-90

GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440071 [Multi-domain]  Cd Length: 186  Bit Score: 260.03  E-value: 3.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNdAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAIT 96
Cdd:COG0302    52 EVLN-TTFEEGYDEMVLVKDIEFYSMCEHHLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQ 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2572895190  97 EALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:COG0302   131 EVLGPRGVAVVIEAEHMCMTMRGVRKPGSSTVTSAMRGVFREDPATRAEFLSLIRG 186
folE PRK09347
GTP cyclohydrolase I; Provisional
 17-152 1.64e-85

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 248.15  E-value: 1.64e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDED-HDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAI 95
Cdd:PRK09347   52 EVLNKTFEEEMgYDEMVLVKDITFYSMCEHHLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADAL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2572895190  96 TEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:PRK09347  132 QEILGPRGVAVVIEAEHMCMTMRGVRKPGSKTVTSALRGLFKTDPATRAEFLSLIRH 188
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
 19-149 1.28e-84

GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related bacterial proteins.


Pssm-ID: 426139 [Multi-domain]  Cd Length: 176  Bit Score: 245.51  E-value: 1.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  19 LNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEA 98
Cdd:pfam01227  46 VLKATFEEGYDEMVLVKDIEFYSMCEHHLLPFFGKAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEI 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2572895190  99 LRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTL 149
Cdd:pfam01227 126 LKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAFRGVFKTDPALRAEFLAL 176
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
 17-152 1.25e-77

GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 129173 [Multi-domain]  Cd Length: 180  Bit Score: 228.10  E-value: 1.25e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAIT 96
Cdd:TIGR00063  45 PKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDGKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQ 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2572895190  97 EALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:TIGR00063 125 EILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSALGGLFKSDQKTRAEFLRLVRH 180
 
Name Accession Description Interval E-value
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
 17-152 9.31e-92

GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate. The enzyme product is the precursor of tetrahydrofolate in eubacteria, fungi, and plants and of the folate analogs in methanogenic bacteria. In vertebrates and insects it is the biosynthtic precursor of tetrahydrobiopterin (BH4) which is involved in the formation of catacholamines, nitric oxide, and the stimulation of T lymphocytes. The biosynthetic reaction of BH4 is controlled by a regulatory protein GFRP which mediates feedback inhibition of GTP-CH-I by BH4. This inhibition is reversed by phenylalanine. The decameric GTP-CH-I forms a complex with two pentameric GFRP in the presence of phenylalanine or a combination of GTP and BH4, respectively.


Pssm-ID: 238349 [Multi-domain]  Cd Length: 185  Bit Score: 263.86  E-value: 9.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAIT 96
Cdd:cd00642    50 DPKNTAIFDEDHDEMVIVKDITLFSMCEHHLVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQ 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2572895190  97 EALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:cd00642   130 EILGPQGVAVVIEATHMCMVMRGVRKPGSKTVTSAMLGVFKEDPKTREEFLRLIRK 185
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
 17-152 3.25e-90

GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440071 [Multi-domain]  Cd Length: 186  Bit Score: 260.03  E-value: 3.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNdAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAIT 96
Cdd:COG0302    52 EVLN-TTFEEGYDEMVLVKDIEFYSMCEHHLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQ 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2572895190  97 EALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:COG0302   131 EVLGPRGVAVVIEAEHMCMTMRGVRKPGSSTVTSAMRGVFREDPATRAEFLSLIRG 186
folE PRK09347
GTP cyclohydrolase I; Provisional
 17-152 1.64e-85

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 248.15  E-value: 1.64e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDED-HDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAI 95
Cdd:PRK09347   52 EVLNKTFEEEMgYDEMVLVKDITFYSMCEHHLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADAL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2572895190  96 TEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:PRK09347  132 QEILGPRGVAVVIEAEHMCMTMRGVRKPGSKTVTSALRGLFKTDPATRAEFLSLIRH 188
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
 19-149 1.28e-84

GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related bacterial proteins.


Pssm-ID: 426139 [Multi-domain]  Cd Length: 176  Bit Score: 245.51  E-value: 1.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  19 LNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEA 98
Cdd:pfam01227  46 VLKATFEEGYDEMVLVKDIEFYSMCEHHLLPFFGKAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEI 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2572895190  99 LRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTL 149
Cdd:pfam01227 126 LKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAFRGVFKTDPALRAEFLAL 176
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
 17-152 1.25e-77

GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 129173 [Multi-domain]  Cd Length: 180  Bit Score: 228.10  E-value: 1.25e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAIT 96
Cdd:TIGR00063  45 PKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDGKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQ 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2572895190  97 EALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:TIGR00063 125 EILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSALGGLFKSDQKTRAEFLRLVRH 180
PTZ00484 PTZ00484
GTP cyclohydrolase I; Provisional
 17-152 1.04e-75

GTP cyclohydrolase I; Provisional


Pssm-ID: 240434  Cd Length: 259  Bit Score: 226.28  E-value: 1.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFD---EDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAV 93
Cdd:PTZ00484  121 EVIKKALFKvepKNNDEMVKVRDIDIFSLCEHHLLPFEGECTIGYIPNKKVLGLSKFARIIEIFSRRLQVQERLTQQIAN 200

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2572895190  94 AITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS 152
Cdd:PTZ00484  201 ALQKYLKPMGVAVVIVASHMCMNMRGVQKHDASTTTSAYLGVFRSDPKLRAEFFSLIKR 259
PRK12606 PRK12606
GTP cyclohydrolase I; Reviewed
 22-150 4.70e-71

GTP cyclohydrolase I; Reviewed


Pssm-ID: 237149  Cd Length: 201  Bit Score: 212.30  E-value: 4.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  22 AIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRP 101
Cdd:PRK12606   70 ALFDSDNDEMVIVRDIELYSLCEHHLLPFIGVAHVAYLPGGKVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQA 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2572895190 102 AGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLI 150
Cdd:PRK12606  150 RGAAVVIEAEHLCMMMRGVRKQNSRMITSVMLGAFRDSAQTRNEFLRLI 198
PLN03044 PLN03044
GTP cyclohydrolase I; Provisional
 17-151 3.45e-65

GTP cyclohydrolase I; Provisional


Pssm-ID: 215549 [Multi-domain]  Cd Length: 188  Bit Score: 197.02  E-value: 3.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  17 DVLNDAIFDED-----HDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNK-QVLGLSKLARIVEIYSRRLQVQERLTKQ 90
Cdd:PLN03044   45 VVLGTALFHEPevhdgHEEMVVVRDIDIHSTCEETMVPFTGRIHVGYIPNAgVILGLSKLARIAEVYARRLQTQERLTRQ 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2572895190  91 IAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIR 151
Cdd:PLN03044  125 IADAIVESVEPLGVMVVVEAAHFCMVMRGVEKHGASTTTSAVRGCFASNPKLRAEFFRIIR 185
PLN02531 PLN02531
GTP cyclohydrolase I
 29-150 5.51e-44

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 150.31  E-value: 5.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  29 DEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQV------LGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALrPA 102
Cdd:PLN02531  335 KTMHTELNLPFWSQCEHHLLPFYGVVHVGYFCAEGGrgnrnpISRSLLQSIVHFYGFRLQVQERLTRQIAETVSSLL-GG 413

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2572895190 103 GVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLI 150
Cdd:PLN02531  414 DVMVVVEASHTCMISRGVEKFGSSTATIAVLGRFSSDAKARAMFLQSI 461
PLN02531 PLN02531
GTP cyclohydrolase I
 31-113 1.87e-29

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 111.40  E-value: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  31 MVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQ-VLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVE 109
Cdd:PLN02531  104 LVVVRDLDLFSYCESCLLPFQVKCHIGYVPSGQrVVGLSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLE 183


                  ....
gi 2572895190 110 ATHM 113
Cdd:PLN02531  184 CSHI 187
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
 29-134 4.89e-17

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: 72.09  E-value: 4.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572895190  29 DEMVIVKDIDMFSMC----EHHLVPFVGKVHIGYLPNKQV----------LGLSKLARIVEIYSRRLQVQERLTKQIAVA 94
Cdd:cd00651     1 TDGVRVKDLLKVTRLgfvtLERTVGQIFEVDVTLSWDGKKaaasddvatdTVYNTIYRLAKEYVEGSQLIERLAEEIAYL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2572895190  95 ITEAL--RPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLG 134
Cdd:cd00651    81 IAEHFlsSVAEVKVEEKKPHAVIPDRGVFKPTDSPGVTIERG 122
 
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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