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Conserved domains on  [gi|333961631|gb|AEG28404|]
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GTP cyclohydrolase I [Serratia sp. AS13]

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

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List of domain hits

Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
7-308 1.49e-103

GTP cyclohydrolase I FolE2;


:

Pssm-ID: 237466  Cd Length: 271  Bit Score: 303.65  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631   7 PPRQPLPDAQAWRgEMSEVGLDWVGMQEIALPLELAGK-----PLMAKVNAGINLRAGrqgVRGIHMSRLYLALDELAQG 81
Cdd:PRK13674   4 MMKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRdggtqTTVARVDLTVSLPAD---FKGIHMSRLYELLEEHAEQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  82 ELTPQRIGRTLDAFLASQpeHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSL-TVGVPYSSTCPSS 160
Cdd:PRK13674  80 ELSPASLEQLLRDMLESL--ESRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLElKVEVPVSSLCPCS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631 161 AALSRQlaqqqfqfdfeqesdrvdrqqvidwlgeqgmpaTPHSQRSWAWVTLTLSGsESALPVISLIDRIEHALGTPSQT 240
Cdd:PRK13674 158 KAISRY---------------------------------TAHSQRSVATVKVRLAA-DAQLWIEDLIDLAEAAASTPLQT 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333961631 241 LVKRRDEQAFALANGQNLMFCEDAARRLYRMLRSQCGLRGFSLRVEHQESLHAHNAVAELSWREESDA 308
Cdd:PRK13674 204 LLKRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDKRGAA 271
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
7-308 1.49e-103

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 303.65  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631   7 PPRQPLPDAQAWRgEMSEVGLDWVGMQEIALPLELAGK-----PLMAKVNAGINLRAGrqgVRGIHMSRLYLALDELAQG 81
Cdd:PRK13674   4 MMKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRdggtqTTVARVDLTVSLPAD---FKGIHMSRLYELLEEHAEQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  82 ELTPQRIGRTLDAFLASQpeHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSL-TVGVPYSSTCPSS 160
Cdd:PRK13674  80 ELSPASLEQLLRDMLESL--ESRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLElKVEVPVSSLCPCS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631 161 AALSRQlaqqqfqfdfeqesdrvdrqqvidwlgeqgmpaTPHSQRSWAWVTLTLSGsESALPVISLIDRIEHALGTPSQT 240
Cdd:PRK13674 158 KAISRY---------------------------------TAHSQRSVATVKVRLAA-DAQLWIEDLIDLAEAAASTPLQT 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333961631 241 LVKRRDEQAFALANGQNLMFCEDAARRLYRMLRSQCGLRGFSLRVEHQESLHAHNAVAELSWREESDA 308
Cdd:PRK13674 204 LLKRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDKRGAA 271
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
11-305 2.50e-92

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: 275.10  E-value: 2.50e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  11 PLPDAQAWRGEmSEVGLDWVGMQEIALPLELAGK-----PLMAKVNAGINLRAGRqgvRGIHMSRLYLALDELAQGELTP 85
Cdd:COG1469    1 TLPDVQSSPDD-RNIPLDRVGIKGVRLPVRIADKdggpqHTVATFDMYVDLPADQ---KGTHMSRFVEVLDEHLEEALSV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  86 QRIGRTLDAFLASQpeHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSLTVG--VPYSSTCPSSAAL 163
Cdd:COG1469   77 ESLEALLEEMAERL--YAERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGEFRKTLGveVPVTSLCPCSKEI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631 164 SRQLAQqqfqfdfeqesdrvdrqqvidwlgEQGMPATPHSQRSWAWVTLTLSGSEsALPVISLIDRIEHALGTPSQTLVK 243
Cdd:COG1469  155 SRQLAQ------------------------ERGIPYGAHNQRSHATISVELDEDE-DVWIEDLIDLAESAASTPVYTLLK 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333961631 244 RRDEQAFALANGQNLMFCEDAARRLYRMLRSQCGLRGFSLRVEHQESLHAHNAVAELSWREE 305
Cdd:COG1469  210 RPDEKAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAYAEIERDKR 271
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
25-298 5.21e-83

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: 251.27  E-value: 5.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631   25 VGLDWVGMQEIALPLELAGK-----PLMAKVNAGINLRAGRqgvRGIHMSRLYLALDELAQgELTPQRIGRTLDAFLASQ 99
Cdd:pfam02649  12 IPLDRVGVKGVRKPVRVKDKdgrpqHLVATFDLFVDLPADR---KGIHMSRFVEALDEHEE-VLSEESLEDILEELLERH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  100 pEHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSLTVG--VPYSSTCPSSAALSRQLAQqqfqfdfe 177
Cdd:pfam02649  88 -EYAERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGGVRKELGveVPVTTLCPCSKEISRQLIQ-------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  178 qesdrvdrqqvidwlgEQGMPATPHSQRSWAWVTLTLSGSESaLPVISLIDRIEHALGTPSQTLVKRRDEQAFALANGQN 257
Cdd:pfam02649 159 ----------------LDGIPYGAHNQRSHATITVELKDGKF-VWIEDLIDIAESSASSPVYTLLKRPDEKAVTERAYEN 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 333961631  258 LMFCEDAARRLYRMLRSQCGLRGFSLRVEHQESLHAHNAVA 298
Cdd:pfam02649 222 PKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAYA 262
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
202-299 5.33e-07

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: 50.24  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  202 HSQRSWAWVTLTLSGSESaLPVISLIDRIEHALGTPSQTLVKRRDEQAFALANGQNLMFCEDAAR----RLYRMLRSQCG 277
Cdd:TIGR00294 192 HNQRGRGRIFTEVPSLPS-IVIADLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRlmaaRLVELFPHLPD 270
                          90       100
                  ....*....|....*....|..
gi 333961631  278 LRGFSLRVEHQESLHAHNAVAE 299
Cdd:TIGR00294 271 DTEVECRQINEESIHRHNAFAE 292
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
7-308 1.49e-103

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 303.65  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631   7 PPRQPLPDAQAWRgEMSEVGLDWVGMQEIALPLELAGK-----PLMAKVNAGINLRAGrqgVRGIHMSRLYLALDELAQG 81
Cdd:PRK13674   4 MMKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRdggtqTTVARVDLTVSLPAD---FKGIHMSRLYELLEEHAEQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  82 ELTPQRIGRTLDAFLASQpeHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSL-TVGVPYSSTCPSS 160
Cdd:PRK13674  80 ELSPASLEQLLRDMLESL--ESRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLElKVEVPVSSLCPCS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631 161 AALSRQlaqqqfqfdfeqesdrvdrqqvidwlgeqgmpaTPHSQRSWAWVTLTLSGsESALPVISLIDRIEHALGTPSQT 240
Cdd:PRK13674 158 KAISRY---------------------------------TAHSQRSVATVKVRLAA-DAQLWIEDLIDLAEAAASTPLQT 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333961631 241 LVKRRDEQAFALANGQNLMFCEDAARRLYRMLRSQCGLRGFSLRVEHQESLHAHNAVAELSWREESDA 308
Cdd:PRK13674 204 LLKRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDKRGAA 271
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
11-305 2.50e-92

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: 275.10  E-value: 2.50e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  11 PLPDAQAWRGEmSEVGLDWVGMQEIALPLELAGK-----PLMAKVNAGINLRAGRqgvRGIHMSRLYLALDELAQGELTP 85
Cdd:COG1469    1 TLPDVQSSPDD-RNIPLDRVGIKGVRLPVRIADKdggpqHTVATFDMYVDLPADQ---KGTHMSRFVEVLDEHLEEALSV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  86 QRIGRTLDAFLASQpeHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSLTVG--VPYSSTCPSSAAL 163
Cdd:COG1469   77 ESLEALLEEMAERL--YAERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGEFRKTLGveVPVTSLCPCSKEI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631 164 SRQLAQqqfqfdfeqesdrvdrqqvidwlgEQGMPATPHSQRSWAWVTLTLSGSEsALPVISLIDRIEHALGTPSQTLVK 243
Cdd:COG1469  155 SRQLAQ------------------------ERGIPYGAHNQRSHATISVELDEDE-DVWIEDLIDLAESAASTPVYTLLK 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333961631 244 RRDEQAFALANGQNLMFCEDAARRLYRMLRSQCGLRGFSLRVEHQESLHAHNAVAELSWREE 305
Cdd:COG1469  210 RPDEKAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAYAEIERDKR 271
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
25-298 5.21e-83

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: 251.27  E-value: 5.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631   25 VGLDWVGMQEIALPLELAGK-----PLMAKVNAGINLRAGRqgvRGIHMSRLYLALDELAQgELTPQRIGRTLDAFLASQ 99
Cdd:pfam02649  12 IPLDRVGVKGVRKPVRVKDKdgrpqHLVATFDLFVDLPADR---KGIHMSRFVEALDEHEE-VLSEESLEDILEELLERH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  100 pEHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSLTVG--VPYSSTCPSSAALSRQLAQqqfqfdfe 177
Cdd:pfam02649  88 -EYAERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGGVRKELGveVPVTTLCPCSKEISRQLIQ-------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  178 qesdrvdrqqvidwlgEQGMPATPHSQRSWAWVTLTLSGSESaLPVISLIDRIEHALGTPSQTLVKRRDEQAFALANGQN 257
Cdd:pfam02649 159 ----------------LDGIPYGAHNQRSHATITVELKDGKF-VWIEDLIDIAESSASSPVYTLLKRPDEKAVTERAYEN 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 333961631  258 LMFCEDAARRLYRMLRSQCGLRGFSLRVEHQESLHAHNAVA 298
Cdd:pfam02649 222 PKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAYA 262
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
9-299 4.87e-16

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 76.89  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631   9 RQPLPDAQAWRGEMsEVGLDWVGMQEIALPLELAGKP-----LMAKVNAGINLRAGRqgvRGIHMSRLYLALDELAQ--- 80
Cdd:PRK13675   1 MMQLPDVQASEPDI-KIGLTRVGVTNVKKLVKIKRKGkrpivLIPTFEVFVDLPSDR---KGIHMSRNVEVIDEVLEeav 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  81 -------GELTPQRIGRTLDAFlasqpEHSDHANLSIRGELLVSRPALLSPHRGWKAYPLCIDATLTQTLTLSLTVGVPY 153
Cdd:PRK13675  77 eeevyeiEDLCGDIAKRLLEKH-----EYATRAEVRMRSEYMMRRETPVSKKKSQEVVDIIAGAIATRDGNVRKEIGAEV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631 154 S--STCPSSAALSRQLAQQQFQFDFeqesdrVDRQQVIDWLGEqgMPATPHSQRSWAWVTLTLSGSESAlPVISLIDRIE 231
Cdd:PRK13675 152 VgmTACPCAQEMMKERARKKLAELG------VDEETIEKFLDN--VPMATHNQRGRGTLTIEVPGDEDV-SLEDIIDIIE 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333961631 232 HALGTPSQTLVKRRDEQAFALANGQNLMFCEDAARRL-YRMLRSQCGLRGFS---LRVEHQESLHAHNAVAE 299
Cdd:PRK13675 223 SSMSSPIYELLKRPDENAVVYEAHKNPKFVEDCVREMaKKVVEEFPHLPDDAvvtVRQINEESIHRHNAFAE 294
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
202-299 5.33e-07

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: 50.24  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333961631  202 HSQRSWAWVTLTLSGSESaLPVISLIDRIEHALGTPSQTLVKRRDEQAFALANGQNLMFCEDAAR----RLYRMLRSQCG 277
Cdd:TIGR00294 192 HNQRGRGRIFTEVPSLPS-IVIADLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRlmaaRLVELFPHLPD 270
                          90       100
                  ....*....|....*....|..
gi 333961631  278 LRGFSLRVEHQESLHAHNAVAE 299
Cdd:TIGR00294 271 DTEVECRQINEESIHRHNAFAE 292
 
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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