NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907688203|gb|QNU64133|]
View 

GTP cyclohydrolase I FolE2 [Vreelandella titanicae]

Protein Classification

GTP cyclohydrolase I FolE2( domain architecture ID 10014323)

GTP cyclohydrolase FolE2, a type Ib GTP cyclohydrolase, converts GTP to 7,8-dihydroneopterin triphosphate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-300 6.57e-111

GTP cyclohydrolase I FolE2;


:

Pssm-ID: 237466  Cd Length: 271  Bit Score: 322.14  E-value: 6.57e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   1 MTVLTLPDVASQTARSPAALTWVGMEGIALPIRLDSRS-----VTAKLNAGVSLDdADARGIHMSRLYLALAPLEEAPLT 75
Cdd:PRK13674    4 MMKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVDTRDggtqtTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  76 LQAVKDILNAFLTSQDglSQHAYLSIEGELPLKRQALISPLAGWKSYPFTLRCQLTPAGFQAELDLTVGYSSTCPCSAAL 155
Cdd:PRK13674   83 PASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 156 ARQliqqafeedfaeipltksavsawlgseegilaTPHSQRSSVECSLRLSESEngewplADFIENSIDRIERALGTALQ 235
Cdd:PRK13674  161 SRY--------------------------------TAHSQRSVATVKVRLAADA------QLWIEDLIDLAEAAASTPLQ 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907688203 236 TAVKRIDEQAFALANGQNLMFCEDAARRLDKALRQAPGVSGFQLKVVHAESLHAHDAVARSEWNW 300
Cdd:PRK13674  203 TLLKRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDK 267
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-300 6.57e-111

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 322.14  E-value: 6.57e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   1 MTVLTLPDVASQTARSPAALTWVGMEGIALPIRLDSRS-----VTAKLNAGVSLDdADARGIHMSRLYLALAPLEEAPLT 75
Cdd:PRK13674    4 MMKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVDTRDggtqtTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  76 LQAVKDILNAFLTSQDglSQHAYLSIEGELPLKRQALISPLAGWKSYPFTLRCQLTPAGFQAELDLTVGYSSTCPCSAAL 155
Cdd:PRK13674   83 PASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 156 ARQliqqafeedfaeipltksavsawlgseegilaTPHSQRSSVECSLRLSESEngewplADFIENSIDRIERALGTALQ 235
Cdd:PRK13674  161 SRY--------------------------------TAHSQRSVATVKVRLAADA------QLWIEDLIDLAEAAASTPLQ 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907688203 236 TAVKRIDEQAFALANGQNLMFCEDAARRLDKALRQAPGVSGFQLKVVHAESLHAHDAVARSEWNW 300
Cdd:PRK13674  203 TLLKRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDK 267
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
5-299 1.00e-95

GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441078  Cd Length: 271  Bit Score: 283.58  E-value: 1.00e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   5 TLPDVASQTARSPAALTWVGMEGIALPIRLDSRS-----VTAKLNAGVSLDdADARGIHMSRLYLALAPLEEAPLTLQAV 79
Cdd:COG1469     1 TLPDVQSSPDDRNIPLDRVGIKGVRLPVRIADKDggpqhTVATFDMYVDLP-ADQKGTHMSRFVEVLDEHLEEALSVESL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  80 KDILNAFLTSQDglSQHAYLSIEGELPLKRQALISPLAGWKSYPFTLRCQLTPAG-FQAELDLTVGYSSTCPCSAALARQ 158
Cdd:COG1469    80 EALLEEMAERLY--AERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGeFRKTLGVEVPVTSLCPCSKEISRQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 159 LIQQafeedfaeipltksavsawlgseEGILATPHSQRSSVECSLRLSESENgewplaDFIENSIDRIERALGTALQTAV 238
Cdd:COG1469   158 LAQE-----------------------RGIPYGAHNQRSHATISVELDEDED------VWIEDLIDLAESAASTPVYTLL 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907688203 239 KRIDEQAFALANGQNLMFCEDAARRLDKALRQAPGVSGFQLKVVHAESLHAHDAVARSEWN 299
Cdd:COG1469   209 KRPDEKAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAYAEIERD 269
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
7-294 2.05e-89

Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP cyclohydrolase activity. GTP cyclohydrolase I is the first enzyme of the de novo tetrahydrofolate biosynthetic pathway present in bacteria, fungi, and plants, and encoded in Escherichia coli by the folE gene; it is also the first enzyme of the biopterin (BH4) pathway in Homo sapiens. The invariate, highly conserved glutamate residue at position 216 in Swiss:Q5F9K6 is likely to be the substrate ligand and the metal ligand is likely to be the cysteine at position 147. The enzyme is Zinc 2+ dependent.


Pssm-ID: 460638  Cd Length: 262  Bit Score: 267.06  E-value: 2.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   7 PDVASQTARSPAALTWVGMEGIALPIRLDSRS-----VTAKLNAGVSLDdADARGIHMSRLYLALAPLEEaPLTLQAVKD 81
Cdd:pfam02649   1 PDVQSEPPDRNIPLDRVGVKGVRKPVRVKDKDgrpqhLVATFDLFVDLP-ADRKGIHMSRFVEALDEHEE-VLSEESLED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  82 ILNAFLTSQDGlSQHAYLSIEGELPLKRQALISPLAGWKSYPFTLRCQLTPAG-FQAELDLTVGYSSTCPCSAALARQLI 160
Cdd:pfam02649  79 ILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGgVRKELGVEVPVTTLCPCSKEISRQLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 161 QqafeedfaeipltksavsawlgsEEGILATPHSQRSSVECSLRLSESENgewplaDFIENSIDRIERALGTALQTAVKR 240
Cdd:pfam02649 158 Q-----------------------LDGIPYGAHNQRSHATITVELKDGKF------VWIEDLIDIAESSASSPVYTLLKR 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907688203 241 IDEQAFALANGQNLMFCEDAARRLDKALRQAPGVSGFQLKVVHAESLHAHDAVA 294
Cdd:pfam02649 209 PDEKAVTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAYA 262
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
149-294 5.31e-06

GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases involved in methanopterin in archaea (MptA) and de novo tetrahydrofolate biosynthesis in bacteria (FolE2). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 129395  Cd Length: 308  Bit Score: 47.16  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 149 CPCSAALARQLIQQAFEE---DFAEIPLTKSAVsawlgseegILATpHSQRSSVECSLRLSESENgewplaDFIENSIDR 225
Cdd:TIGR00294 155 CPCAQELVKEKSQPFLQEagfSDETIPKILDIV---------EFAT-HNQRGRGRIFTEVPSLPS------IVIADLIDI 218
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907688203 226 IERALGTALQTAVKRIDEQAFALANGQNLMFCEDAAR----RLDKALRQAPGVSGFQLKVVHAESLHAHDAVA 294
Cdd:TIGR00294 219 AESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRlmaaRLVELFPHLPDDTEVECRQINEESIHRHNAFA 291
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-300 6.57e-111

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 322.14  E-value: 6.57e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   1 MTVLTLPDVASQTARSPAALTWVGMEGIALPIRLDSRS-----VTAKLNAGVSLDdADARGIHMSRLYLALAPLEEAPLT 75
Cdd:PRK13674    4 MMKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVDTRDggtqtTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  76 LQAVKDILNAFLTSQDglSQHAYLSIEGELPLKRQALISPLAGWKSYPFTLRCQLTPAGFQAELDLTVGYSSTCPCSAAL 155
Cdd:PRK13674   83 PASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 156 ARQliqqafeedfaeipltksavsawlgseegilaTPHSQRSSVECSLRLSESEngewplADFIENSIDRIERALGTALQ 235
Cdd:PRK13674  161 SRY--------------------------------TAHSQRSVATVKVRLAADA------QLWIEDLIDLAEAAASTPLQ 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907688203 236 TAVKRIDEQAFALANGQNLMFCEDAARRLDKALRQAPGVSGFQLKVVHAESLHAHDAVARSEWNW 300
Cdd:PRK13674  203 TLLKRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDK 267
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
5-299 1.00e-95

GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441078  Cd Length: 271  Bit Score: 283.58  E-value: 1.00e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   5 TLPDVASQTARSPAALTWVGMEGIALPIRLDSRS-----VTAKLNAGVSLDdADARGIHMSRLYLALAPLEEAPLTLQAV 79
Cdd:COG1469     1 TLPDVQSSPDDRNIPLDRVGIKGVRLPVRIADKDggpqhTVATFDMYVDLP-ADQKGTHMSRFVEVLDEHLEEALSVESL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  80 KDILNAFLTSQDglSQHAYLSIEGELPLKRQALISPLAGWKSYPFTLRCQLTPAG-FQAELDLTVGYSSTCPCSAALARQ 158
Cdd:COG1469    80 EALLEEMAERLY--AERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGeFRKTLGVEVPVTSLCPCSKEISRQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 159 LIQQafeedfaeipltksavsawlgseEGILATPHSQRSSVECSLRLSESENgewplaDFIENSIDRIERALGTALQTAV 238
Cdd:COG1469   158 LAQE-----------------------RGIPYGAHNQRSHATISVELDEDED------VWIEDLIDLAESAASTPVYTLL 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907688203 239 KRIDEQAFALANGQNLMFCEDAARRLDKALRQAPGVSGFQLKVVHAESLHAHDAVARSEWN 299
Cdd:COG1469   209 KRPDEKAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAYAEIERD 269
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
7-294 2.05e-89

Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP cyclohydrolase activity. GTP cyclohydrolase I is the first enzyme of the de novo tetrahydrofolate biosynthetic pathway present in bacteria, fungi, and plants, and encoded in Escherichia coli by the folE gene; it is also the first enzyme of the biopterin (BH4) pathway in Homo sapiens. The invariate, highly conserved glutamate residue at position 216 in Swiss:Q5F9K6 is likely to be the substrate ligand and the metal ligand is likely to be the cysteine at position 147. The enzyme is Zinc 2+ dependent.


Pssm-ID: 460638  Cd Length: 262  Bit Score: 267.06  E-value: 2.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   7 PDVASQTARSPAALTWVGMEGIALPIRLDSRS-----VTAKLNAGVSLDdADARGIHMSRLYLALAPLEEaPLTLQAVKD 81
Cdd:pfam02649   1 PDVQSEPPDRNIPLDRVGVKGVRKPVRVKDKDgrpqhLVATFDLFVDLP-ADRKGIHMSRFVEALDEHEE-VLSEESLED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  82 ILNAFLTSQDGlSQHAYLSIEGELPLKRQALISPLAGWKSYPFTLRCQLTPAG-FQAELDLTVGYSSTCPCSAALARQLI 160
Cdd:pfam02649  79 ILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGgVRKELGVEVPVTTLCPCSKEISRQLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 161 QqafeedfaeipltksavsawlgsEEGILATPHSQRSSVECSLRLSESENgewplaDFIENSIDRIERALGTALQTAVKR 240
Cdd:pfam02649 158 Q-----------------------LDGIPYGAHNQRSHATITVELKDGKF------VWIEDLIDIAESSASSPVYTLLKR 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907688203 241 IDEQAFALANGQNLMFCEDAARRLDKALRQAPGVSGFQLKVVHAESLHAHDAVA 294
Cdd:pfam02649 209 PDEKAVTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAYA 262
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
6-294 9.58e-11

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 61.49  E-value: 9.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203   6 LPDVASQTARSPAALTWVGMEGIALPIRL---DSRSVTAKLNAGVSLD-DADARGIHMSRLYLAL-----APLEEAPLTL 76
Cdd:PRK13675    4 LPDVQASEPDIKIGLTRVGVTNVKKLVKIkrkGKRPIVLIPTFEVFVDlPSDRKGIHMSRNVEVIdevleEAVEEEVYEI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203  77 QAV-KDILNAFLTSQDgLSQHAYLSIEGELPLKRQaliSPLAGWKSY-PFTLRCQLTpAGFQAELDLTVGYSST----CP 150
Cdd:PRK13675   84 EDLcGDIAKRLLEKHE-YATRAEVRMRSEYMMRRE---TPVSKKKSQeVVDIIAGAI-ATRDGNVRKEIGAEVVgmtaCP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 151 CsaalARQLIQQAFEEDFAEIPLTKSAVSAWLgsEEGILATpHSQRSSVECSLRLSESENGEwpladfIENSIDRIERAL 230
Cdd:PRK13675  159 C----AQEMMKERARKKLAELGVDEETIEKFL--DNVPMAT-HNQRGRGTLTIEVPGDEDVS------LEDIIDIIESSM 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907688203 231 GTALQTAVKRIDEQAFALANGQNLMFCEDAARRLDKALRQ----APGVSGFQLKVVHAESLHAHDAVA 294
Cdd:PRK13675  226 SSPIYELLKRPDENAVVYEAHKNPKFVEDCVREMAKKVVEefphLPDDAVVTVRQINEESIHRHNAFA 293
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
149-294 5.31e-06

GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases involved in methanopterin in archaea (MptA) and de novo tetrahydrofolate biosynthesis in bacteria (FolE2). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 129395  Cd Length: 308  Bit Score: 47.16  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907688203 149 CPCSAALARQLIQQAFEE---DFAEIPLTKSAVsawlgseegILATpHSQRSSVECSLRLSESENgewplaDFIENSIDR 225
Cdd:TIGR00294 155 CPCAQELVKEKSQPFLQEagfSDETIPKILDIV---------EFAT-HNQRGRGRIFTEVPSLPS------IVIADLIDI 218
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907688203 226 IERALGTALQTAVKRIDEQAFALANGQNLMFCEDAAR----RLDKALRQAPGVSGFQLKVVHAESLHAHDAVA 294
Cdd:TIGR00294 219 AESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRlmaaRLVELFPHLPDDTEVECRQINEESIHRHNAFA 291
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH