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Conserved domains on  [gi|38492509|pdb|1N3T|I]
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Chain I, GTP cyclohydrolase I

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 ...
39-219 2.30e-102

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 TIGR00063:

Pssm-ID: 469697 [Multi-domain]  Cd Length: 180  Bit Score: 293.59  E-value: 2.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I         39 IAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVdEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTID 118
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYV-EIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        119 GKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTTTS 198
Cdd:TIGR00063  80 GKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSA 159
                         170       180
                  ....*....|....*....|.
1N3T_I        199 LGGLFKSSQNTRHEFLRAVRH 219
Cdd:TIGR00063 160 LGGLFKSDQKTRAEFLRLVRH 180
 
Name Accession Description Interval E-value
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
39-219 2.30e-102

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: 293.59  E-value: 2.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I         39 IAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVdEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTID 118
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYV-EIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        119 GKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTTTS 198
Cdd:TIGR00063  80 GKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSA 159
                         170       180
                  ....*....|....*....|.
1N3T_I        199 LGGLFKSSQNTRHEFLRAVRH 219
Cdd:TIGR00063 160 LGGLFKSDQKTRAEFLRLVRH 180
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
34-219 9.03e-93

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: 269.64  E-value: 9.03e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       34 TRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVdEIFSGLDYA-NFPKITLIENKmKVDEMVTVRDITLTSTCEH 112
Cdd:cd00642   1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQ-EITSGYDQAlNDPKNTAIFDE-DHDEMVIVKDITLFSMCEH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I      113 HFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATS 192
Cdd:cd00642  79 HLVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGS 158
                       170       180
                ....*....|....*....|....*..
1N3T_I      193 ATTTTSLGGLFKSSQNTRHEFLRAVRH 219
Cdd:cd00642 159 KTVTSAMLGVFKEDPKTREEFLRLIRK 185
folE PRK09347
GTP cyclohydrolase I; Provisional
32-219 4.33e-92

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 267.80  E-value: 4.33e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        32 NETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYvDEIFSGldYANFPKITL---IENKMKVDEMVTVRDITLTS 108
Cdd:PRK09347   1 NEPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMY-EELFSG--YANDPKEVLnktFEEEMGYDEMVLVKDITFYS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       109 TCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIR 188
Cdd:PRK09347  78 MCEHHLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVR 157
                        170       180       190
                 ....*....|....*....|....*....|.
1N3T_I       189 DATSATTTTSLGGLFKSSQNTRHEFLRAVRH 219
Cdd:PRK09347 158 KPGSKTVTSALRGLFKTDPATRAEFLSLIRH 188
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
32-219 1.12e-82

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: 243.85  E-value: 1.12e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       32 NETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYvDEIFSGLDYANFPKITLIENKmKVDEMVTVRDITLTSTCE 111
Cdd:COG0302   1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAY-EELFSGYDQDPAEVLNTTFEE-GYDEMVLVKDIEFYSMCE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I      112 HHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDAT 191
Cdd:COG0302  79 HHLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPG 158
                       170       180
                ....*....|....*....|....*...
1N3T_I      192 SATTTTSLGGLFKSSQNTRHEFLRAVRH 219
Cdd:COG0302 159 SSTVTSAMRGVFREDPATRAEFLSLIRG 186
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
39-215 2.24e-66

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: 202.37  E-value: 2.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I         39 IAGHMTEIMQLLNLDLADDSLMETPHRIAKMYvDEIFSGLDYANfpkITLIENKMKV--DEMVTVRDITLTSTCEHHFVT 116
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMY-EELFSGYHEDP---EKVLKATFEEgyDEMVLVKDIEFYSMCEHHLLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        117 IDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTT 196
Cdd:pfam01227  77 FFGKAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVT 156
                         170
                  ....*....|....*....
1N3T_I        197 TSLGGLFKSSQNTRHEFLR 215
Cdd:pfam01227 157 SAFRGVFKTDPALRAEFLA 175
 
Name Accession Description Interval E-value
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
39-219 2.30e-102

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: 293.59  E-value: 2.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I         39 IAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVdEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTID 118
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYV-EIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        119 GKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTTTS 198
Cdd:TIGR00063  80 GKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSA 159
                         170       180
                  ....*....|....*....|.
1N3T_I        199 LGGLFKSSQNTRHEFLRAVRH 219
Cdd:TIGR00063 160 LGGLFKSDQKTRAEFLRLVRH 180
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
34-219 9.03e-93

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: 269.64  E-value: 9.03e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       34 TRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVdEIFSGLDYA-NFPKITLIENKmKVDEMVTVRDITLTSTCEH 112
Cdd:cd00642   1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQ-EITSGYDQAlNDPKNTAIFDE-DHDEMVIVKDITLFSMCEH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I      113 HFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATS 192
Cdd:cd00642  79 HLVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGS 158
                       170       180
                ....*....|....*....|....*..
1N3T_I      193 ATTTTSLGGLFKSSQNTRHEFLRAVRH 219
Cdd:cd00642 159 KTVTSAMLGVFKEDPKTREEFLRLIRK 185
folE PRK09347
GTP cyclohydrolase I; Provisional
32-219 4.33e-92

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 267.80  E-value: 4.33e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        32 NETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYvDEIFSGldYANFPKITL---IENKMKVDEMVTVRDITLTS 108
Cdd:PRK09347   1 NEPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMY-EELFSG--YANDPKEVLnktFEEEMGYDEMVLVKDITFYS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       109 TCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIR 188
Cdd:PRK09347  78 MCEHHLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVR 157
                        170       180       190
                 ....*....|....*....|....*....|.
1N3T_I       189 DATSATTTTSLGGLFKSSQNTRHEFLRAVRH 219
Cdd:PRK09347 158 KPGSKTVTSALRGLFKTDPATRAEFLSLIRH 188
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
32-219 1.12e-82

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: 243.85  E-value: 1.12e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       32 NETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYvDEIFSGLDYANFPKITLIENKmKVDEMVTVRDITLTSTCE 111
Cdd:COG0302   1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAY-EELFSGYDQDPAEVLNTTFEE-GYDEMVLVKDIEFYSMCE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I      112 HHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDAT 191
Cdd:COG0302  79 HHLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPG 158
                       170       180
                ....*....|....*....|....*...
1N3T_I      192 SATTTTSLGGLFKSSQNTRHEFLRAVRH 219
Cdd:COG0302 159 SSTVTSAMRGVFREDPATRAEFLSLIRG 186
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
39-215 2.24e-66

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: 202.37  E-value: 2.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I         39 IAGHMTEIMQLLNLDLADDSLMETPHRIAKMYvDEIFSGLDYANfpkITLIENKMKV--DEMVTVRDITLTSTCEHHFVT 116
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMY-EELFSGYHEDP---EKVLKATFEEgyDEMVLVKDIEFYSMCEHHLLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        117 IDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTT 196
Cdd:pfam01227  77 FFGKAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVT 156
                         170
                  ....*....|....*....
1N3T_I        197 TSLGGLFKSSQNTRHEFLR 215
Cdd:pfam01227 157 SAFRGVFKTDPALRAEFLA 175
PTZ00484 PTZ00484
GTP cyclohydrolase I; Provisional
2-219 1.16e-62

GTP cyclohydrolase I; Provisional


Pssm-ID: 240434  Cd Length: 259  Bit Score: 195.85  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I         2 SLSKEAALVHEALVARGLETPlRPPVHEMDNETRKSLIAGHMTEIMQLLN-LDLADDSLMETPHRIAKMY---------- 70
Cdd:PTZ00484  40 LLDEDASLGKGRQSNSGPSTE-SSPTCATLMEEKKGAIESARRKILKSLEgEDPDRDGLKKTPKRVAKALefltkgyhms 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        71 VDEIFSGLDYANFPKITlienkmkvDEMVTVRDITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQV 150
Cdd:PTZ00484 119 VEEVIKKALFKVEPKNN--------DEMVKVRDIDIFSLCEHHLLPFEGECTIGYIPNKKVLGLSKFARIIEIFSRRLQV 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1N3T_I       151 QERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRH 219
Cdd:PTZ00484 191 QERLTQQIANALQKYLKPMGVAVVIVASHMCMNMRGVQKHDASTTTSAYLGVFRSDPKLRAEFFSLIKR 259
PRK12606 PRK12606
GTP cyclohydrolase I; Reviewed
42-217 1.18e-41

GTP cyclohydrolase I; Reviewed


Pssm-ID: 237149  Cd Length: 201  Bit Score: 140.27  E-value: 1.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        42 HMTEIMQLLNLDLADDSLMETPHRIAKMYvDEIFSGLdYANFPKI--TLIENKMkvDEMVTVRDITLTSTCEHHFVTIDG 119
Cdd:PRK12606  25 AVRELLEALGEDPDREGLLDTPQRVAKAM-QYLCDGY-EQDPAEAlgALFDSDN--DEMVIVRDIELYSLCEHHLLPFIG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       120 KATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTTTSL 199
Cdd:PRK12606 101 VAHVAYLPGGKVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQARGAAVVIEAEHLCMMMRGVRKQNSRMITSVM 180
                        170
                 ....*....|....*...
1N3T_I       200 GGLFKSSQNTRHEFLRAV 217
Cdd:PRK12606 181 LGAFRDSAQTRNEFLRLI 198
PLN03044 PLN03044
GTP cyclohydrolase I; Provisional
45-220 1.71e-34

GTP cyclohydrolase I; Provisional


Pssm-ID: 215549 [Multi-domain]  Cd Length: 188  Bit Score: 121.52  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        45 EIMQLLNLDLADDSLMETPHRIAKM-------YVDEIFSGLDYANFPKITLIENKmkvDEMVTVRDITLTSTCEHHFVTI 117
Cdd:PLN03044   7 TILECLGEDVEREGLLDTPKRVAKAllfmtqgYDQDPEVVLGTALFHEPEVHDGH---EEMVVVRDIDIHSTCEETMVPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       118 DGKATVAYIPKDSVI-GLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYSVKARGIRDATSATTT 196
Cdd:PLN03044  84 TGRIHVGYIPNAGVIlGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMVVVEAAHFCMVMRGVEKHGASTTT 163
                        170       180
                 ....*....|....*....|....
1N3T_I       197 TSLGGLFKSSQNTRHEFLRAVRHH 220
Cdd:PLN03044 164 SAVRGCFASNPKLRAEFFRIIRGG 187
PLN02531 PLN02531
GTP cyclohydrolase I
20-217 3.60e-19

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 85.21  E-value: 3.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        20 ETPLRPPVHEMDNEtrksliaghMTEIMQLLNLDLADDSLMETPHRIAK----------MYVDEIfSGLDYANFPKITLI 89
Cdd:PLN02531 259 SSASPEPNPAMVSA---------VESILRSLGEDPLRKELVLTPSRFVRwllnstqgsrMGRNLE-MKLNGFACEKMDPL 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        90 ENKMKVDEMVTVRDITLTSTCEHHFVTIDGKATVAYIPKDSV------IGLSKINRIVQFFAQRPQVQERLTQQILIALQ 163
Cdd:PLN02531 329 HANLNEKTMHTELNLPFWSQCEHHLLPFYGVVHVGYFCAEGGrgnrnpISRSLLQSIVHFYGFRLQVQERLTRQIAETVS 408
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
1N3T_I       164 TLLGtNNVAVSIDAVHYSVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAV 217
Cdd:PLN02531 409 SLLG-GDVMVVVEASHTCMISRGVEKFGSSTATIAVLGRFSSDAKARAMFLQSI 461
PLN02531 PLN02531
GTP cyclohydrolase I
46-179 1.21e-13

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 69.03  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I        46 IMQLLNLDLADDSLMETPHRIAK----------MYVDEIFSGldyANFPKITLIENKMK---VDEMVTVRDITLTSTCEH 112
Cdd:PLN02531  42 LLQGLGEDVNREGLKKTPLRVAKalreatrgykQSAKDIVGG---ALFPEAGLDDGVGHgggCGGLVVVRDLDLFSYCES 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1N3T_I       113 HFVTIDGKATVAYIPKDS-VIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVH 179
Cdd:PLN02531 119 CLLPFQVKCHIGYVPSGQrVVGLSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLECSH 186
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
96-189 1.63e-07

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: 48.59  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N3T_I       96 DEMVTVRDITLTSTC----EHHFVTIDGKATVAYIPKDSV----------IGLSKINRIVQFFAQRPQVQERLTQQILIA 161
Cdd:cd00651   1 TDGVRVKDLLKVTRLgfvtLERTVGQIFEVDVTLSWDGKKaaasddvatdTVYNTIYRLAKEYVEGSQLIERLAEEIAYL 80
                        90       100       110
                ....*....|....*....|....*....|
1N3T_I      162 LQT--LLGTNNVAVSIDAVHYSVKARGIRD 189
Cdd:cd00651  81 IAEhfLSSVAEVKVEEKKPHAVIPDRGVFK 110
 
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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