|
Name |
Accession |
Description |
Interval |
E-value |
| PdxT |
COG0311 |
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ... |
4-200 |
2.77e-116 |
|
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440080 [Multi-domain] Cd Length: 191 Bit Score: 328.18 E-value: 2.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 4 PTIGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCAG 83
Cdd:COG0311 1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 84 MIMLATEVLDgrADQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVPGGGFHAVFIRAPWVERVGAGVEVIGTVTGgpaa 163
Cdd:COG0311 81 LILLAKEIED--PDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPYIEEVGPGVEVLATVDG---- 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 663337446 164 eRIVAVRQGNLLATSFHPELTGDPRVHAYFVELARTA 200
Cdd:COG0311 155 -RIVAVRQGNILATSFHPELTDDLRVHEYFLEMVRGA 190
|
|
| PRK13525 |
PRK13525 |
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
3-198 |
4.82e-113 |
|
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 320.18 E-value: 4.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 3 RPTIGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCA 82
Cdd:PRK13525 1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 83 GMIMLATEVLDgrADQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVpGGGFHAVFIRAPWVERVGAGVEVIGTVtggpa 162
Cdd:PRK13525 81 GMILLAKEIEG--YEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGL-GEPFPAVFIRAPYIEEVGPGVEVLATV----- 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 663337446 163 AERIVAVRQGNLLATSFHPELTGDPRVHAYFVELAR 198
Cdd:PRK13525 153 GGRIVAVRQGNILATSFHPELTDDTRVHRYFLEMVK 188
|
|
| GATase1_PB |
cd01749 |
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
6-194 |
4.11e-100 |
|
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.
Pssm-ID: 153220 [Multi-domain] Cd Length: 183 Bit Score: 287.11 E-value: 4.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 6 IGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCAGMI 85
Cdd:cd01749 1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 86 MLATEVLDGRaDQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVPGGGFHAVFIRAPWVERVGAGVEVIGTVTGgpaaeR 165
Cdd:cd01749 81 LLAKEVEDQG-GQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLGPFPAVFIRAPVIEEVGPGVEVLAEYDG-----K 154
|
170 180
....*....|....*....|....*....
gi 663337446 166 IVAVRQGNLLATSFHPELTGDPRVHAYFV 194
Cdd:cd01749 155 IVAVRQGNVLATSFHPELTDDTRIHEYFL 183
|
|
| PLP_synth_Pdx2 |
TIGR03800 |
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ... |
6-195 |
7.47e-89 |
|
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 274792 [Multi-domain] Cd Length: 184 Bit Score: 258.90 E-value: 7.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 6 IGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCAGMI 85
Cdd:TIGR03800 2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 86 MLATEVLDGRADQRGfaGIDMTVRRNAFGRQVDSFEAPVEITGVPGGGFHAVFIRAPWVERVGAGVEVIGTVTGgpaaeR 165
Cdd:TIGR03800 82 MLAKEIIGQKEGQLG--LLDMTVERNAYGRQVDSFEAEVDIKGVGDDPITGVFIRAPKIVSVGNGVEILAKVGN-----R 154
|
170 180 190
....*....|....*....|....*....|
gi 663337446 166 IVAVRQGNLLATSFHPELTGDPRVHAYFVE 195
Cdd:TIGR03800 155 IVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
|
|
| SNO |
pfam01174 |
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ... |
8-195 |
1.46e-56 |
|
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.
Pssm-ID: 334414 [Multi-domain] Cd Length: 188 Bit Score: 176.95 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 8 VLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADG-MPVYGSCAGMIM 86
Cdd:pfam01174 1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 87 LATEVldGRADQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVpGGGFHAVFIRAPWVERVGAGvEVIGTVTGGPAaeRI 166
Cdd:pfam01174 81 LSKQL--GNELVKTLGLLKVTVKRNAFGRQVDSFEKECDFKNL-IPKFPGVFIRAPVIEEILDP-EVVVVLYELDG--KI 154
|
170 180 190
....*....|....*....|....*....|
gi 663337446 167 VAVRQGNLLATSFHPELTGDP-RVHAYFVE 195
Cdd:pfam01174 155 VVAKQGNILATSFHPELAEDDyRVHDWFVE 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PdxT |
COG0311 |
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ... |
4-200 |
2.77e-116 |
|
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440080 [Multi-domain] Cd Length: 191 Bit Score: 328.18 E-value: 2.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 4 PTIGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCAG 83
Cdd:COG0311 1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 84 MIMLATEVLDgrADQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVPGGGFHAVFIRAPWVERVGAGVEVIGTVTGgpaa 163
Cdd:COG0311 81 LILLAKEIED--PDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPYIEEVGPGVEVLATVDG---- 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 663337446 164 eRIVAVRQGNLLATSFHPELTGDPRVHAYFVELARTA 200
Cdd:COG0311 155 -RIVAVRQGNILATSFHPELTDDLRVHEYFLEMVRGA 190
|
|
| PRK13525 |
PRK13525 |
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
3-198 |
4.82e-113 |
|
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 320.18 E-value: 4.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 3 RPTIGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCA 82
Cdd:PRK13525 1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 83 GMIMLATEVLDgrADQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVpGGGFHAVFIRAPWVERVGAGVEVIGTVtggpa 162
Cdd:PRK13525 81 GMILLAKEIEG--YEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGL-GEPFPAVFIRAPYIEEVGPGVEVLATV----- 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 663337446 163 AERIVAVRQGNLLATSFHPELTGDPRVHAYFVELAR 198
Cdd:PRK13525 153 GGRIVAVRQGNILATSFHPELTDDTRVHRYFLEMVK 188
|
|
| GATase1_PB |
cd01749 |
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
6-194 |
4.11e-100 |
|
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.
Pssm-ID: 153220 [Multi-domain] Cd Length: 183 Bit Score: 287.11 E-value: 4.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 6 IGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCAGMI 85
Cdd:cd01749 1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 86 MLATEVLDGRaDQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVPGGGFHAVFIRAPWVERVGAGVEVIGTVTGgpaaeR 165
Cdd:cd01749 81 LLAKEVEDQG-GQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLGPFPAVFIRAPVIEEVGPGVEVLAEYDG-----K 154
|
170 180
....*....|....*....|....*....
gi 663337446 166 IVAVRQGNLLATSFHPELTGDPRVHAYFV 194
Cdd:cd01749 155 IVAVRQGNVLATSFHPELTDDTRIHEYFL 183
|
|
| PLP_synth_Pdx2 |
TIGR03800 |
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ... |
6-195 |
7.47e-89 |
|
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 274792 [Multi-domain] Cd Length: 184 Bit Score: 258.90 E-value: 7.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 6 IGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCAGMI 85
Cdd:TIGR03800 2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 86 MLATEVLDGRADQRGfaGIDMTVRRNAFGRQVDSFEAPVEITGVPGGGFHAVFIRAPWVERVGAGVEVIGTVTGgpaaeR 165
Cdd:TIGR03800 82 MLAKEIIGQKEGQLG--LLDMTVERNAYGRQVDSFEAEVDIKGVGDDPITGVFIRAPKIVSVGNGVEILAKVGN-----R 154
|
170 180 190
....*....|....*....|....*....|
gi 663337446 166 IVAVRQGNLLATSFHPELTGDPRVHAYFVE 195
Cdd:TIGR03800 155 IVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
|
|
| PRK13527 |
PRK13527 |
glutamine amidotransferase subunit PdxT; Provisional |
5-197 |
4.06e-84 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 247.11 E-value: 4.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 5 TIGVLALQGDVREHLAALT------GAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVY 78
Cdd:PRK13527 2 KIGVLALQGDVEEHIDALKraldelGIDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEKIEEGLPIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 79 GSCAGMIMLATEVLDGRA---DQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVpGGGFHAVFIRAPWVERVGAGVEVIG 155
Cdd:PRK13527 82 GTCAGLILLAKEVGDDRVtktEQPLLGLMDVTVKRNAFGRQRDSFEAEIDLSGL-DGPFHAVFIRAPAITKVGGDVEVLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663337446 156 TVTGgpaaeRIVAVRQGNLLATSFHPELTGDPRVHAYFVELA 197
Cdd:PRK13527 161 KLDD-----RIVAVEQGNVLATAFHPELTDDTRIHEYFLKKV 197
|
|
| PLN02832 |
PLN02832 |
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex |
3-197 |
1.26e-63 |
|
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
Pssm-ID: 215446 [Multi-domain] Cd Length: 248 Bit Score: 196.85 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 3 RPTIGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADGMPVYGSCA 82
Cdd:PLN02832 1 MMAIGVLALQGSFNEHIAALRRLGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALREFVKSGKPVWGTCA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 83 GMIMLATEVLDGR-ADQRGFAGIDMTVRRNAFGRQVDSFEA--PVEITGVPGGG---FHAVFIRAPWVERVGAGVEVIGT 156
Cdd:PLN02832 81 GLIFLAERAVGQKeGGQELLGGLDCTVHRNFFGSQINSFETelPVPELAASEGGpetFRAVFIRAPAILSVGPGVEVLAE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 663337446 157 VTGGPAA-------------ERIVAVRQGNLLATSFHPELTGDPRVHAYFVELA 197
Cdd:PLN02832 161 YPLPSEKalyssstdaegrdKVIVAVKQGNLLATAFHPELTADTRWHSYFVKMV 214
|
|
| SNO |
pfam01174 |
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ... |
8-195 |
1.46e-56 |
|
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.
Pssm-ID: 334414 [Multi-domain] Cd Length: 188 Bit Score: 176.95 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 8 VLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIDKRIADG-MPVYGSCAGMIM 86
Cdd:pfam01174 1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 87 LATEVldGRADQRGFAGIDMTVRRNAFGRQVDSFEAPVEITGVpGGGFHAVFIRAPWVERVGAGvEVIGTVTGGPAaeRI 166
Cdd:pfam01174 81 LSKQL--GNELVKTLGLLKVTVKRNAFGRQVDSFEKECDFKNL-IPKFPGVFIRAPVIEEILDP-EVVVVLYELDG--KI 154
|
170 180 190
....*....|....*....|....*....|
gi 663337446 167 VAVRQGNLLATSFHPELTGDP-RVHAYFVE 195
Cdd:pfam01174 155 VVAKQGNILATSFHPELAEDDyRVHDWFVE 184
|
|
| PRK13526 |
PRK13526 |
glutamine amidotransferase subunit PdxT; Provisional |
5-196 |
2.49e-42 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 184113 [Multi-domain] Cd Length: 179 Bit Score: 140.47 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 5 TIGVLALQGDVREHLAALTGAGADARPVRRPGELDAVDGLVIPGGESTTISKLVDIFELREPIdKRIADGMPVYGSCAGM 84
Cdd:PRK13526 4 KVGVLAIQGGYQKHADMFKSLGVEVKLVKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKL-YNFCSSKPVFGTCAGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 85 IMLATevldgraDQRGFAGIDMTVRRNAFGRQVDSFEAPVeitGVPGGGFHAVFIRAPWVERVGAGVEVIGTVTGGPaae 164
Cdd:PRK13526 83 IILSK-------GEGYLNLLDLEVQRNAYGRQVDSFVADI---SFNDKNITGVFIRAPKFIVVGNQVDILSKYQNSP--- 149
|
170 180 190
....*....|....*....|....*....|..
gi 663337446 165 riVAVRQGNLLATSFHPELTGDPRVHAYFVEL 196
Cdd:PRK13526 150 --VLLRQANILVSSFHPELTQDPTVHEYFLAM 179
|
|
| GATase1_CobB |
cd03130 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ... |
16-194 |
1.63e-09 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobB.
Pssm-ID: 153224 [Multi-domain] Cd Length: 198 Bit Score: 54.91 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 16 REHLAALTGAGADARPVR--RPGELDAVDGLVIPGG--ESTTiSKLVDIFELREPIDKRIADGMPVYGSCAGMIMLATEV 91
Cdd:cd03130 14 PENLELLEAAGAELVPFSplKDEELPDADGLYLGGGypELFA-EELSANQSMRESIRAFAESGGPIYAECGGLMYLGESL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 92 LDGRADQRGFAGI-DMTVR---RNAFG-RQVDSFEA-PVEITG--VPGGGFHavFIRapwVERVGAGVEVIGTVTGGPAA 163
Cdd:cd03130 93 DDEEGQSYPMAGVlPGDARmtkRLGLGyREAEALGDtLLGKKGttLRGHEFH--YSR---LEPPPEPDFAATVRRGRGID 167
|
170 180 190
....*....|....*....|....*....|.
gi 663337446 164 ERIVAVRQGNLLATSFHPELTGDPRVHAYFV 194
Cdd:cd03130 168 GGEDGYVYGNVLASYLHLHWASNPDLAERFV 198
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
13-186 |
4.87e-09 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 53.72 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 13 GDVREHLAALTGAGADARPVRRPGELDAVDGLVIPG-GE-STTISKLvDIFELREPIDKRIADGMPVYGSCAGMIMLATE 90
Cdd:PRK13181 10 GNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGvGAfGQAMRSL-RESGLDEALKEHVEKKQPVLGICLGMQLLFES 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 91 VLDGRADQRGFagIDMTVRR-------------NAFGRQVDS--FEapveitGVPGGGFhAVFIRAPWVErVGAGVEVIG 155
Cdd:PRK13181 89 SEEGNVKGLGL--IPGDVKRfrseplkvpqmgwNSVKPLKESplFK------GIEEGSY-FYFVHSYYVP-CEDPEDVLA 158
|
170 180 190
....*....|....*....|....*....|....*
gi 663337446 156 TvtggpaAERIV----AVRQGNLLATSFHPELTGD 186
Cdd:PRK13181 159 T------TEYGVpfcsAVAKDNIYAVQFHPEKSGK 187
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
21-182 |
8.93e-09 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 52.89 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 21 ALTGAGADARPVRRPGELDAVDGLVIPG-GE-STTISKLVDiFELREPIDKRIADGMPVYGSCAGMIMLATEVLDGrADQ 98
Cdd:cd01748 17 ALERLGAEVIITSDPEEILSADKLILPGvGAfGDAMANLRE-RGLIEALKEAIASGKPFLGICLGMQLLFESSEEG-GGT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 99 RGFAGIDMTVRRnafgrqvdsFEAPVEITgVPGGGFHAVFIRA-----------PWV-------ERVGAGVEVIGTVT-G 159
Cdd:cd01748 95 KGLGLIPGKVVR---------FPASEGLK-VPHMGWNQLEITKesplfkgipdgSYFyfvhsyyAPPDDPDYILATTDyG 164
|
170 180
....*....|....*....|...
gi 663337446 160 GPAaerIVAVRQGNLLATSFHPE 182
Cdd:cd01748 165 GKF---PAAVEKDNIFGTQFHPE 184
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
13-198 |
4.18e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 51.02 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 13 GDVREHLAALTGAGADARPVRRPGELDAVDGLVIPG-GESTTISKLVDifELREPIDKRIADGMPVYGSCAGMIMLATEV 91
Cdd:PRK13143 11 GNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGvGAFGAAMENLS--PLRDVILEAARSGKPFLGICLGMQLLFESS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 92 LDGRaDQRGFAGIDMTVRRnafgrqvdsFEAPVEitgVPGGGFHAVFIR--APWVErvgaGVE----------------- 152
Cdd:PRK13143 89 EEGG-GVRGLGLFPGRVVR---------FPAGVK---VPHMGWNTVKVVkdCPLFE----GIDgeyvyfvhsyyaypdde 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 663337446 153 --VIGTVTGG---PAaerivAVRQGNLLATSFHPELTGDP--RVHAYFVELAR 198
Cdd:PRK13143 152 dyVVATTDYGiefPA-----AVCNDNVFGTQFHPEKSGETglKILENFVELIK 199
|
|
| PRK01077 |
PRK01077 |
cobyrinate a,c-diamide synthase; |
17-200 |
2.31e-07 |
|
cobyrinate a,c-diamide synthase;
Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 50.13 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 17 EHLAALTGAGADARPVR--RPGELDAVDGLVIPGG--EsttisklvdIF--------ELREPIDKRIADGMPVYGSCAGM 84
Cdd:PRK01077 262 ENLELLRAAGAELVFFSplADEALPDCDGLYLGGGypE---------LFaaelaantSMRASIRAAAAAGKPIYAECGGL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 85 IMLATEVLDGRADQRGFAGI-----DMTVRRNAFG-RQV----DSFEAPVEITgVPGGGFH-AVFIRAP----WVERVGA 149
Cdd:PRK01077 333 MYLGESLEDADGERHPMVGLlpgeaSMTKRLQALGyREAealeDTLLGKAGER-LRGHEFHySTLETPEeaplYRVRDAD 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 663337446 150 GVEVIGTVtggpaaerivaVRQGNLLATSFHPELTGDPRVHAYFVELARTA 200
Cdd:PRK01077 412 GRPLGEEG-----------YRRGNVLASYLHLHFASNPDAAARFLAACRRF 451
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
6-87 |
1.01e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 45.67 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 6 IGVLALQG----DVREHLAALTGAGADARPVRRPGE-------LDAVDGLVIPGGESTtISKLVDIFELREPIDKRIADG 74
Cdd:cd01653 1 VAVLLFPGfeelELASPLDALREAGAEVDVVSPDGGpvesdvdLDDYDGLILPGGPGT-PDDLARDEALLALLREAAAAG 79
|
90
....*....|...
gi 663337446 75 MPVYGSCAGMIML 87
Cdd:cd01653 80 KPILGICLGAQLL 92
|
|
| GATase1_CobQ |
cd01750 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
26-94 |
2.47e-06 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.
Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 46.08 E-value: 2.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663337446 26 GADARPVRRPGELDAVDGLVIPGGEStTISKLV--DIFELREPIDKRIADGMPVYGSCAGMIMLATEVLDG 94
Cdd:cd01750 23 GVDVRYVEVPEGLGDADLIILPGSKD-TIQDLAwlRKRGLAEAIKNYARAGGPVLGICGGYQMLGKYIVDP 92
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
6-87 |
3.40e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 43.73 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 6 IGVLALQG----DVREHLAALTGAGADARPVRRPGE-------LDAVDGLVIPGGESTtISKLVDIFELREPIDKRIADG 74
Cdd:cd03128 1 VAVLLFGGseelELASPLDALREAGAEVDVVSPDGGpvesdvdLDDYDGLILPGGPGT-PDDLAWDEALLALLREAAAAG 79
|
90
....*....|...
gi 663337446 75 MPVYGSCAGMIML 87
Cdd:cd03128 80 KPVLGICLGAQLL 92
|
|
| GATase_3 |
pfam07685 |
CobB/CobQ-like glutamine amidotransferase domain; |
39-93 |
2.04e-05 |
|
CobB/CobQ-like glutamine amidotransferase domain;
Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 43.38 E-value: 2.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 663337446 39 DAVDGLVIPGGESTtISKLV--DIFELREPIDKRIADGMPVYGSCAGMIMLATEVLD 93
Cdd:pfam07685 41 PDADLIILPGGKPT-IQDLAllRNSGMDEAIKEAAEDGGPVLGICGGYQMLGETIED 96
|
|
| CobB |
COG1797 |
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ... |
16-198 |
2.51e-05 |
|
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441402 [Multi-domain] Cd Length: 459 Bit Score: 43.94 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 16 REHLAALTGAGADARPVR--RPGEL-DAVDGLVIPGG--EsTTISKLVDIFELREPIDKRIADGMPVYGSCAGMIMLATE 90
Cdd:COG1797 264 PENLELLEAAGAELVFFSplRDEALpEDVDGLYLGGGfpE-LFAEELSANRSMRESIREAAEAGMPIYAECGGLMYLCRS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663337446 91 VLDGRADQRGFAGI-----DMTVRRNAFG-RQV----DSFEAPV--EITG--------VPGGGFHAVFIrapwVERvGAG 150
Cdd:COG1797 343 ITDFEGKGYPMVGVlpgdaVMTKRLQGLGyREAtalgDSPLGPAgeRIRGhefhystlTPEGDLRPAYR----LRR-GRG 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663337446 151 vevIGTVTGGpaaerivaVRQGNLLATSFHPELTGDPRVHAYFVELAR 198
Cdd:COG1797 418 ---IDGGRDG--------FVYGNVLASYLHLHFASNPEWAERFVAACR 454
|
|
| |
