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Conserved domains on  [gi|1390048914|pdb|5NF1|F]
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Chain F, Geranylgeranylglyceryl phosphate synthase

Protein Classification

geranylgeranylglyceryl/heptaprenylglyceryl phosphate synthase( domain architecture ID 10004104)

prenyltransferase catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) or heptaprenyl moiety of heptaprenyl pyrophosphate to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
4-244 4.68e-109

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


:

Pssm-ID: 441252  Cd Length: 241  Bit Score: 314.41  E-value: 4.68e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F        4 MKVEDYFHDILRER-KIHLTLIDPEEQTPEEAVEIARAAIRGGTDGIMLGGST-TDSSELDNTARALRENIDVPIILFPG 81
Cdd:COG1646   1 GKVEKYLLEKLDWKgWLHVTLIDPDKELSDEEAELAEAACESGTDAILVGGSLgVTEENLDELVSAIKEAYDVPVILFPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F       82 NTTGVSRYADAIFFMSLLNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAM 161
Cdd:COG1646  81 NPEQVSPGADAILFPSVLNSRNPYWIIGAHVEAAPLVKKLGLEVIPEGYIVLNPGTTVAYVTNARPIPLDKPDVAAAAAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F      162 AAEFLGMRLFYLEAGSGAPEHVPEEMIALVKRCTDQI-LIVGGGIRSGEDAARVAGAGADVVVTGTVVEnsDNVeDKIRE 240
Cdd:COG1646 161 AEEYLGMPIVYLEYGSGAGEPVDPEMVKAVKKALEDTpLIYGGGIRSPEKAREMAEAGADTIVVGNAIE--EDP-DLALE 237


                ....
5NF1_F      241 IVEG 244
Cdd:COG1646 238 TVEA 241
 
Name Accession Description Interval E-value
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
4-244 4.68e-109

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 314.41  E-value: 4.68e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F        4 MKVEDYFHDILRER-KIHLTLIDPEEQTPEEAVEIARAAIRGGTDGIMLGGST-TDSSELDNTARALRENIDVPIILFPG 81
Cdd:COG1646   1 GKVEKYLLEKLDWKgWLHVTLIDPDKELSDEEAELAEAACESGTDAILVGGSLgVTEENLDELVSAIKEAYDVPVILFPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F       82 NTTGVSRYADAIFFMSLLNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAM 161
Cdd:COG1646  81 NPEQVSPGADAILFPSVLNSRNPYWIIGAHVEAAPLVKKLGLEVIPEGYIVLNPGTTVAYVTNARPIPLDKPDVAAAAAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F      162 AAEFLGMRLFYLEAGSGAPEHVPEEMIALVKRCTDQI-LIVGGGIRSGEDAARVAGAGADVVVTGTVVEnsDNVeDKIRE 240
Cdd:COG1646 161 AEEYLGMPIVYLEYGSGAGEPVDPEMVKAVKKALEDTpLIYGGGIRSPEKAREMAEAGADTIVVGNAIE--EDP-DLALE 237


                ....
5NF1_F      241 IVEG 244
Cdd:COG1646 238 TVEA 241
GGGP-family TIGR01768
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ...
 19-243 2.43e-105

geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired.


Pssm-ID: 273794  Cd Length: 223  Bit Score: 304.41  E-value: 2.43e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         19 IHLTLIDPEEQTPEEAVEIARAAIRGGTDGIMLGGSTTDS-SELDNTARALReNIDVPIILFPGNTTGVSRYADAIFFMS 97
Cdd:TIGR01768   1 RHFTLIDPDKTNPEEADEIAKAAAESGTDAILIGGSQGVTyEKLDTLIEALR-RYGVPIILFPSNPTNVSRDADALFFPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         98 LLNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAMAAEFLGMRLFYLEAGS 177
Cdd:TIGR01768  80 VLNSDDPYWIIGAQIEGAPKFKKIGEEIIPEGYIIVNPGGAAARVTKAKPIPYDKEDLAAYAAMAEEMLGMPIFYLEAGS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
5NF1_F        178 GAPEHVPEEMIALVKRCTD-QILIVGGGIRSGEDAARVAGAGADVVVTGTVVENSDnveDKIREIVE 243
Cdd:TIGR01768 160 GAPEPVPPELVAEVKKVLDkARLFVGGGIRSVEKAREMAEAGADTVVTGNVIEESV---DKALETVE 223
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
11-244 7.13e-105

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 303.27  E-value: 7.13e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F        11 HDILRERKIHLTLIDPEEQTPEEAVEiarAAIRGGTDGIMLGGSTTDSSE-LDNTARALREnIDVPIILFPGNTTGVSRY 89
Cdd:PRK04169   1 MMIDWKGWLHVTLLDPDKPLPDEALE---AICESGTDAIIVGGSDGVTEEnVDELVKAIKE-YDLPVILFPGNIEGISPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F        90 ADAIFFMSLLNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAMAAEFLGMR 169
Cdd:PRK04169  77 ADAYLFPSVLNSRNPYWIIGAHVEAAPIIKKGGLEVIPEGYIVLNPGSKVAVVGTAAPIPLDKPDIAAYAALAAEYLGMP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5NF1_F       170 LFYLEAGSGAPEHVPEEMIALVKRCTDQ-ILIVGGGIRSGEDAARVAGAGADVVVTGTVVEnsDNVEDKIREIVEG 244
Cdd:PRK04169 157 IVYLEYGGGAGDPVPPEMVKAVKKALDItPLIYGGGIRSPEQARELMAAGADTIVVGNIIE--EDPKKTVKAIKKA 230
PcrB pfam01884
PcrB family; This family contains proteins that are related to PcrB. The function of these ...
 11-245 1.97e-101

PcrB family; This family contains proteins that are related to PcrB. The function of these proteins is unknown.


Pssm-ID: 396454  Cd Length: 226  Bit Score: 294.43  E-value: 1.97e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         11 HDILRERkiHLTLIDPEEQTPEEAVEIAraaIRGGTDGIMLGGSttDSSELDNTARALREN--IDVPIILFPGNTTGVSR 88
Cdd:pfam01884   1 MDIREWR--HLTKLDPEETNPDEIIEIV---ADSGTDAVMIGGS--QNVTLDNTRRLIEKVsqYGLPIVLEPSNPSGVVR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         89 YADAIFFMSLLNSTNPYWIIGAQALGAATVKKMG--IEALPMGYLVVEPGGTVGAVGDTKpVPRNKPDIAAAYAMAAEFL 166
Cdd:pfam01884  74 YADALFVPSVLNSANGDWIVGMHYLGAQTFTEIIesEEIQPEGYLVLNPDSKVAAVTEAL-CPINKPDIAAYALVGAKLF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5NF1_F        167 GMRLFYLEAgSGAPEHvPEEMIALVKRCTDQILIVGGGIRSGEDAARVAGAgADVVVTGTVVENSDnvEDKIREIVEGM 245
Cdd:pfam01884 153 GLPIFYLEY-SGAYGN-VEEVIALKKVLDKARLFYGGGIRSREKAREMARA-ADVIVVGNVVYEKG--ERAIDAILETL 226
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 19-240 4.18e-87

PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown.


Pssm-ID: 239206  Cd Length: 219  Bit Score: 257.94  E-value: 4.18e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F       19 IHLTLIDPEEQtpEEAVEIARAAIRGGTDGIMLGGSTTDSSELDNTARALRENID-VPIILFPGNTTGVSRYADAIFFMS 97
Cdd:cd02812   1 RHVTKLDPDKE--LVDEEIAKLAEESGTDAIMVGGSDGVSSTLDNVVRLIKRIRRpVPVILFPSNPEAVSPGADAYLFPS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F       98 LLNSTNPYWIIGAQALGAATVKK--MGIEALPMGYLVVEPGGTVGAVGDTKpvPRNKPDIAAAYAMAAEFLGMRLFYLEa 175
Cdd:cd02812  79 VLNSGDPYWIIGAQAEAAPEVGKiiPWLELIPEGYLVLNPDSTVARVTGAK--TDLKPEDAAAYALAAEYLGMPIVYLE- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
5NF1_F      176 GSGAPehVPEEMIALVKRCT-DQILIVGGGIRSGEDAARVAGAGADVVVTGTVVENSDNVEDKIRE 240
Cdd:cd02812 156 YSGAY--GPPEVVRAVKKVLgDTPLIVGGGIRSGEQAKEMAEAGADTIVVGNIVEEDPNAALETVE 219
 
Name Accession Description Interval E-value
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
4-244 4.68e-109

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 314.41  E-value: 4.68e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F        4 MKVEDYFHDILRER-KIHLTLIDPEEQTPEEAVEIARAAIRGGTDGIMLGGST-TDSSELDNTARALRENIDVPIILFPG 81
Cdd:COG1646   1 GKVEKYLLEKLDWKgWLHVTLIDPDKELSDEEAELAEAACESGTDAILVGGSLgVTEENLDELVSAIKEAYDVPVILFPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F       82 NTTGVSRYADAIFFMSLLNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAM 161
Cdd:COG1646  81 NPEQVSPGADAILFPSVLNSRNPYWIIGAHVEAAPLVKKLGLEVIPEGYIVLNPGTTVAYVTNARPIPLDKPDVAAAAAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F      162 AAEFLGMRLFYLEAGSGAPEHVPEEMIALVKRCTDQI-LIVGGGIRSGEDAARVAGAGADVVVTGTVVEnsDNVeDKIRE 240
Cdd:COG1646 161 AEEYLGMPIVYLEYGSGAGEPVDPEMVKAVKKALEDTpLIYGGGIRSPEKAREMAEAGADTIVVGNAIE--EDP-DLALE 237


                ....
5NF1_F      241 IVEG 244
Cdd:COG1646 238 TVEA 241
GGGP-family TIGR01768
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ...
 19-243 2.43e-105

geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired.


Pssm-ID: 273794  Cd Length: 223  Bit Score: 304.41  E-value: 2.43e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         19 IHLTLIDPEEQTPEEAVEIARAAIRGGTDGIMLGGSTTDS-SELDNTARALReNIDVPIILFPGNTTGVSRYADAIFFMS 97
Cdd:TIGR01768   1 RHFTLIDPDKTNPEEADEIAKAAAESGTDAILIGGSQGVTyEKLDTLIEALR-RYGVPIILFPSNPTNVSRDADALFFPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         98 LLNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAMAAEFLGMRLFYLEAGS 177
Cdd:TIGR01768  80 VLNSDDPYWIIGAQIEGAPKFKKIGEEIIPEGYIIVNPGGAAARVTKAKPIPYDKEDLAAYAAMAEEMLGMPIFYLEAGS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
5NF1_F        178 GAPEHVPEEMIALVKRCTD-QILIVGGGIRSGEDAARVAGAGADVVVTGTVVENSDnveDKIREIVE 243
Cdd:TIGR01768 160 GAPEPVPPELVAEVKKVLDkARLFVGGGIRSVEKAREMAEAGADTVVTGNVIEESV---DKALETVE 223
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
11-244 7.13e-105

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 303.27  E-value: 7.13e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F        11 HDILRERKIHLTLIDPEEQTPEEAVEiarAAIRGGTDGIMLGGSTTDSSE-LDNTARALREnIDVPIILFPGNTTGVSRY 89
Cdd:PRK04169   1 MMIDWKGWLHVTLLDPDKPLPDEALE---AICESGTDAIIVGGSDGVTEEnVDELVKAIKE-YDLPVILFPGNIEGISPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F        90 ADAIFFMSLLNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAMAAEFLGMR 169
Cdd:PRK04169  77 ADAYLFPSVLNSRNPYWIIGAHVEAAPIIKKGGLEVIPEGYIVLNPGSKVAVVGTAAPIPLDKPDIAAYAALAAEYLGMP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5NF1_F       170 LFYLEAGSGAPEHVPEEMIALVKRCTDQ-ILIVGGGIRSGEDAARVAGAGADVVVTGTVVEnsDNVEDKIREIVEG 244
Cdd:PRK04169 157 IVYLEYGGGAGDPVPPEMVKAVKKALDItPLIYGGGIRSPEQARELMAAGADTIVVGNIIE--EDPKKTVKAIKKA 230
PcrB pfam01884
PcrB family; This family contains proteins that are related to PcrB. The function of these ...
 11-245 1.97e-101

PcrB family; This family contains proteins that are related to PcrB. The function of these proteins is unknown.


Pssm-ID: 396454  Cd Length: 226  Bit Score: 294.43  E-value: 1.97e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         11 HDILRERkiHLTLIDPEEQTPEEAVEIAraaIRGGTDGIMLGGSttDSSELDNTARALREN--IDVPIILFPGNTTGVSR 88
Cdd:pfam01884   1 MDIREWR--HLTKLDPEETNPDEIIEIV---ADSGTDAVMIGGS--QNVTLDNTRRLIEKVsqYGLPIVLEPSNPSGVVR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         89 YADAIFFMSLLNSTNPYWIIGAQALGAATVKKMG--IEALPMGYLVVEPGGTVGAVGDTKpVPRNKPDIAAAYAMAAEFL 166
Cdd:pfam01884  74 YADALFVPSVLNSANGDWIVGMHYLGAQTFTEIIesEEIQPEGYLVLNPDSKVAAVTEAL-CPINKPDIAAYALVGAKLF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5NF1_F        167 GMRLFYLEAgSGAPEHvPEEMIALVKRCTDQILIVGGGIRSGEDAARVAGAgADVVVTGTVVENSDnvEDKIREIVEGM 245
Cdd:pfam01884 153 GLPIFYLEY-SGAYGN-VEEVIALKKVLDKARLFYGGGIRSREKAREMARA-ADVIVVGNVVYEKG--ERAIDAILETL 226
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 19-240 4.18e-87

PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown.


Pssm-ID: 239206  Cd Length: 219  Bit Score: 257.94  E-value: 4.18e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F       19 IHLTLIDPEEQtpEEAVEIARAAIRGGTDGIMLGGSTTDSSELDNTARALRENID-VPIILFPGNTTGVSRYADAIFFMS 97
Cdd:cd02812   1 RHVTKLDPDKE--LVDEEIAKLAEESGTDAIMVGGSDGVSSTLDNVVRLIKRIRRpVPVILFPSNPEAVSPGADAYLFPS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F       98 LLNSTNPYWIIGAQALGAATVKK--MGIEALPMGYLVVEPGGTVGAVGDTKpvPRNKPDIAAAYAMAAEFLGMRLFYLEa 175
Cdd:cd02812  79 VLNSGDPYWIIGAQAEAAPEVGKiiPWLELIPEGYLVLNPDSTVARVTGAK--TDLKPEDAAAYALAAEYLGMPIVYLE- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
5NF1_F      176 GSGAPehVPEEMIALVKRCT-DQILIVGGGIRSGEDAARVAGAGADVVVTGTVVENSDNVEDKIRE 240
Cdd:cd02812 156 YSGAY--GPPEVVRAVKKVLgDTPLIVGGGIRSGEQAKEMAEAGADTIVVGNIVEEDPNAALETVE 219
GGGP TIGR01769
phosphoglycerol geranylgeranyltransferase; This model represents geranylgeranylglyceryl ...
 20-225 1.14e-83

phosphoglycerol geranylgeranyltransferase; This model represents geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The active enzyme is reported to be a homopentamer in Methanobacterium thermoautotrophicum but is reported to be a homodimer in Thermoplasma acidophilum.


Pssm-ID: 130830  Cd Length: 205  Bit Score: 248.56  E-value: 1.14e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         20 HLTLIDPEEQtpEEAVEIARAAIRGGTDGIMLGGST-TDSSELDNTARALRENIDVPIILFPGNTTGVSRYADAIFFMSL 98
Cdd:TIGR01769   1 HFTLIDPEKS--DEIEKIAKNAKDAGTDAIMVGGSLgIVESNLDQTVKKIKKITNLPVILFPGNVNGLSRYADAVFFMSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F         99 LNSTNPYWIIGAQALGAATVKKMGIEALPMGYLVVEPGGTVGAVGDTKPVPRNKPDIAAAYAMAAEFLGMRLFYLEAGSG 178
Cdd:TIGR01769  79 LNSADTYFIVGAQILGAITILKLNLEVIPMAYLIVGPGGAVGYVGKAREIPYNKPEIAAAYCLAAKYFGMKWVYLEAGSG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
5NF1_F        179 APEHVPEEMIALVKRCTDQILIVGGGIRSGEDAARVAGAGADVVVTG 225
Cdd:TIGR01769 159 ASYPVNPETISLVKKASGIPLIVGGGIRSPEIAYEIVLAGADAIVTG 205
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 185-247 1.46e-05

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 45.15  E-value: 1.46e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
5NF1_F      185 EEMIALVKRCTDQI---LIVGGGIRSGEDAARVAGAGADVVVTgtvveNSDNVEDK--IREIVEGMGS 247
Cdd:cd04731  57 ETMLDVVERVAEEVfipLTVGGGIRSLEDARRLLRAGADKVSI-----NSAAVENPelIREIAKRFGS 119
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 187-247 2.93e-05

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 44.24  E-value: 2.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
5NF1_F      187 MIALVKRCTDQILI---VGGGIRSGEDAARVAGAGAD-VVVtgtvveNSDNVEDK--IREIVEGMGS 247
Cdd:COG0107  61 MLDVVRRVAEEVFIpltVGGGIRSVEDARRLLRAGADkVSI------NSAAVKNPelITEAAERFGS 121
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 166-243 8.88e-05

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 42.64  E-value: 8.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F      166 LGMRLFY---LEAGSGAPEHVpeEMIALVKRCTDQILIVGGGIRSGEDAARVAGAGADVVVTGTVVENSDNVEDKIREIV 242
Cdd:cd04723  47 LGFRGLYiadLDAIMGRGDND--EAIRELAAAWPLGLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLAALG 124


                .
5NF1_F      243 E 243
Cdd:cd04723 125 E 125
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 177-236 1.11e-04

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 42.08  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
5NF1_F        177 SGAPEHVPEeMIALVKRCTDQILI---VGGGIRSGEDAARVAGAGADVVVTGTV-VENSDNVED 236
Cdd:pfam00977  52 DAAKEGRPV-NLDVVEEIAEEVFIpvqVGGGIRSLEDVERLLSAGADRVIIGTAaVKNPELIKE 114
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 175-245 2.98e-04

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 41.20  E-value: 2.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NF1_F      175 AGSGAPEHVpEEMIALVKRCTDQILIVGGGIRSGEDAARVAGAgADVVVTGT----VVENS------DNVEDKIREIVEG 244
Cdd:COG0159 183 ARTAVSDDL-AELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSalvkLIEEGgddealEALAAFVRELKAA 260


                .
5NF1_F      245 M 245
Cdd:COG0159 261 L 261
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 201-240 4.30e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 40.41  E-value: 4.30e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
5NF1_F      201 VGGGIRSGEDAARVAGAGADVVVTGTV-VENSDNVEDKIRE 240
Cdd:COG0106  78 VGGGIRSLEDIERLLDAGASRVILGTAaVKDPELVKEALEE 118
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 189-226 4.79e-04

Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240092  Cd Length: 294  Bit Score: 40.77  E-value: 4.79e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
5NF1_F      189 ALVKRCTDQILIVG-GGIRSGEDAARVAGAGADVVVTGT 226
Cdd:cd04741 235 TFRRLLPSEIQIIGvGGVLDGRGAFRMRLAGASAVQVGT 273
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 174-222 6.17e-04

Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.


Pssm-ID: 240089  Cd Length: 327  Bit Score: 40.56  E-value: 6.17e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
5NF1_F      174 EAG--SGAPehVPE---EMIALVKRCT-DQILIVG-GGIRSGEDAARVAGAGADVV 222
Cdd:cd04738 253 ETGglSGAP--LKErstEVLRELYKLTgGKIPIIGvGGISSGEDAYEKIRAGASLV 306
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 187-226 8.08e-04

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 39.66  E-value: 8.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
5NF1_F        187 MIALVKRCTDQILI---VGGGIRSGEDAARVAGAGADVVVTGT 226
Cdd:TIGR00735  62 MIDVVERTAETVFIpltVGGGIKSIEDVDKLLRAGADKVSINT 104
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 201-241 1.14e-03

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 39.10  E-value: 1.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
5NF1_F        201 VGGGIRSGEDAARVAGAGADVVVTGTV-VENSDNVEDKIREI 241
Cdd:TIGR00007  77 VGGGIRSLEDVEKLLDLGVDRVIIGTAaVENPDLVKELLKEY 118
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 185-241 1.20e-03

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 39.00  E-value: 1.20e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
5NF1_F      185 EEMIALVKRCTDQILI-VGGGIRSgEDAARVAGAGADVVVTGTVVENSDNVEDKIREI 241
Cdd:cd00429 154 RKLRELIPENNLNLLIeVDGGINL-ETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 201-241 1.32e-03

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 39.00  E-value: 1.32e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
5NF1_F      201 VGGGIRSGEDAARVAGAGADVVVTGTV-VENSDNVEDKIREI 241
Cdd:cd04732  78 VGGGIRSLEDIERLLDLGVSRVIIGTAaVKNPELVKELLKEY 119
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 185-245 2.23e-03

Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.


Pssm-ID: 240075  Cd Length: 242  Bit Score: 38.23  E-value: 2.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
5NF1_F      185 EEMIALVKRCTDQILIVGGGIRSGEDAARVAGAgADVVVTGTVV------ENSDNVEDKIREIVEGM 245
Cdd:cd04724 176 KELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALvkiieeGGEEEALEALKELAESL 241
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 201-240 2.55e-03

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 38.12  E-value: 2.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
5NF1_F       201 VGGGIRSGEDAARVAGAGADVVVTGTV-VENSDNVEDKIRE 240
Cdd:PRK00748  79 VGGGIRSLETVEALLDAGVSRVIIGTAaVKNPELVKEACKK 119
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 189-241 2.63e-03

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 37.86  E-value: 2.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
5NF1_F       189 ALVKRCTDQILI-VGGGIrSGEDAARVAGAGADVVVTGTVVENSDNVEDKIREI 241
Cdd:PRK05581 162 KLIDERGLDILIeVDGGI-NADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSL 214
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 196-228 3.00e-03

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 38.10  E-value: 3.00e-03
                         10        20        30
                 ....*....|....*....|....*....|...
5NF1_F       196 DQILIVGGGIRSGEDAARVAGAGADVVVTGTVV 228
Cdd:PRK13125 185 NKYLVVGFGLDSPEDARDALSAGADGVVVGTAF 217
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 179-248 3.29e-03

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 37.65  E-value: 3.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5NF1_F       179 APEHVPEEMIALVKRCTDQILIVGGGIRS-GEDAARVAGAGADVVVTGTVVENSDNVEDKIREIVEGMGSV 248
Cdd:PRK13813 145 APATRPERVRYIRSRLGDELKIISPGIGAqGGKAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIRGA 215
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 201-247 4.90e-03

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 37.19  E-value: 4.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
5NF1_F       201 VGGGIRSGEDAARVAGAGADVVVTGTV-VENSdnveDKIREIVEGMGS 247
Cdd:PRK13585  81 LGGGIRSAEDAASLLDLGVDRVILGTAaVENP----EIVRELSEEFGS 124
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
174-222 6.03e-03

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 37.45  E-value: 6.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
5NF1_F       174 EAG--SGAPehVPE---EMIALVKRCT-DQILIVG-GGIRSGEDAARVAGAGADVV 222
Cdd:PRK05286 262 EAGglSGRP--LFErstEVIRRLYKELgGRLPIIGvGGIDSAEDAYEKIRAGASLV 315
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 180-245 6.62e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 36.77  E-value: 6.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
5NF1_F       180 PEHVpEEMIALVKRCTDQI-LIVGGGIRSGEDAARVAGAGADVVVTGTVVENSDNVEDKIREIVEGM 245
Cdd:PRK04302 157 PEVV-EDAVEAVKKVNPDVkVLCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEAALRDLVSPL 222
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 185-241 8.58e-03

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 36.29  E-value: 8.58e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
5NF1_F      185 EEMIALVKRctDQILIVGGGIRSGEDAARVAGAGADVVVTGTVVENSDNVEDKIREI 241
Cdd:cd00331 163 ERLAPLIPK--DVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
 
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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