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Conserved domains on  [gi|446482785|ref|WP_000560639|]
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MULTISPECIES: imidazole glycerol phosphate synthase subunit HisH [Bacillus]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10793738)

imidazole glycerol phosphate synthase subunit HisH catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR

CATH:  3.40.50.880
EC:  4.3.2.10|3.5.1.2
Gene Ontology:  GO:0004359|GO:0000107|GO:0016829
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 7.80e-122

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 343.27  E-value: 7.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEELKDCSGLSLLPGVIRKLK--VPYKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYAD-CPKGIVYG 157
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFPpeEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADpCDEEYVAA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446482785 158 ASEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNFKGVVEAW 202
Cdd:PRK13141 161 TTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 7.80e-122

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 343.27  E-value: 7.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEELKDCSGLSLLPGVIRKLK--VPYKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYAD-CPKGIVYG 157
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFPpeEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADpCDEEYVAA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446482785 158 ASEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNFKGVVEAW 202
Cdd:PRK13141 161 TTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-193 1.46e-107

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 306.96  E-value: 1.46e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:COG0118    2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEELKDCSGLSLLPGVIRKLK-VPYKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADCP-KGIVYGA 158
Cdd:COG0118   82 GMQLLFERSEENGDTEGLGLIPGEVVRFPaSDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDdPEDVVAT 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446482785 159 SEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILK 193
Cdd:COG0118  162 TDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-195 2.29e-102

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: 293.64  E-value: 2.29e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICLG 81
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  82 MQLLFEKSEELKDCSGLSLLPGVIRKLKVP--YKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADC-PKGIVYGA 158
Cdd:cd01748   81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASegLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPdDPDYILAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446482785 159 SEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:cd01748  161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-198 7.45e-85

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 249.55  E-value: 7.45e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785    2 IAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   82 MQLLFEKSEELKDCSGLSLLPGVIRKLKVPyKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADCPKGIVYGASEY 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR-KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEAVLAYADY 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446482785  162 GVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNFKGV 198
Cdd:TIGR01855 160 GEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase pfam00117
Glutamine amidotransferase class-I;
3-195 7.69e-26

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 98.46  E-value: 7.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785    3 AIVDYGMGNICSVEQALKYIGAEYIV---TDDREEILRS--DGVIL-PGVGAfPKAMDVLEEkklvfVLKEIGNLGKPFL 76
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpnDTPAEEILEEnpDGIILsGGPGS-PGAAGGAIE-----AIREARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   77 GICLGMQLLFEKSEelkdcsglsllpGVIRKLKvpyKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYAD---CPKG 153
Cdd:pfam00117  75 GICLGHQLLALAFG------------GKVVKAK---KFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDpdtLPDG 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446482785  154 I-VYGASEYGVQVPGFVAKGN-VFGAQFHPEK-SGEVGIQILKNF 195
Cdd:pfam00117 140 LeVTATSENDGTIMGIRHKKLpIFGVQFHPESiLTPHGPEILFNF 184
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 7.80e-122

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 343.27  E-value: 7.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEELKDCSGLSLLPGVIRKLK--VPYKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYAD-CPKGIVYG 157
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFPpeEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADpCDEEYVAA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446482785 158 ASEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNFKGVVEAW 202
Cdd:PRK13141 161 TTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-193 1.46e-107

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 306.96  E-value: 1.46e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:COG0118    2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEELKDCSGLSLLPGVIRKLK-VPYKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADCP-KGIVYGA 158
Cdd:COG0118   82 GMQLLFERSEENGDTEGLGLIPGEVVRFPaSDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDdPEDVVAT 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446482785 159 SEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILK 193
Cdd:COG0118  162 TDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-195 2.29e-102

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: 293.64  E-value: 2.29e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICLG 81
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  82 MQLLFEKSEELKDCSGLSLLPGVIRKLKVP--YKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADC-PKGIVYGA 158
Cdd:cd01748   81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASegLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPdDPDYILAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446482785 159 SEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:cd01748  161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-195 4.41e-90

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 262.88  E-value: 4.41e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:PRK13181   1 MIAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEElKDCSGLSLLPGVIRKLK-VPYKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADC-PKGIVYGA 158
Cdd:PRK13181  81 GMQLLFESSEE-GNVKGLGLIPGDVKRFRsEPLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVPCeDPEDVLAT 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446482785 159 SEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:PRK13181 160 TEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNF 196
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-195 6.10e-87

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 255.09  E-value: 6.10e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNICSVEQALKYIGAEY--IVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNL-GKPFLGI 78
Cdd:PRK13146   4 VAIIDYGSGNLRSAAKALERAGAGAdvVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAVLAaGRPFLGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  79 CLGMQLLFEKSEELKDCSGLSLLPGVIRKLKVP---YKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYA--DCPKG 153
Cdd:PRK13146  84 CVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDgpaLKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVHSYYAqpANPAD 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446482785 154 IVyGASEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:PRK13146 164 VV-AWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNF 204
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-199 4.72e-86

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 252.48  E-value: 4.72e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEekKLVFVLKEIGNLGKPFLGICL 80
Cdd:PRK13143   2 MIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLS--PLRDVILEAARSGKPFLGICL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEELKDCSGLSLLPGVIRKLKVPYKIPHMGWNELKKEGEIPLWNGIeDGSFVYYVHSYYADC-PKGIVYGAS 159
Cdd:PRK13143  80 GMQLLFESSEEGGGVRGLGLFPGRVVRFPAGVKVPHMGWNTVKVVKDCPLFEGI-DGEYVYFVHSYYAYPdDEDYVVATT 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446482785 160 EYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNFKGVV 199
Cdd:PRK13143 159 DYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVELI 198
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-198 7.45e-85

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 249.55  E-value: 7.45e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785    2 IAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   82 MQLLFEKSEELKDCSGLSLLPGVIRKLKVPyKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADCPKGIVYGASEY 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR-KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEAVLAYADY 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446482785  162 GVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNFKGV 198
Cdd:TIGR01855 160 GEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-195 7.09e-70

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 211.25  E-value: 7.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKeigNLGKPFLGICL 80
Cdd:PRK13170   2 NVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIK---ACTQPVLGICL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEELKDCSGLSLLPGVIRKLKVP-YKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYAD-CPKGIVYga 158
Cdd:PRK13170  79 GMQLLGERSEESGGVDCLGIIDGPVKKMTDFgLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPvNEYTIAQ-- 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446482785 159 SEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:PRK13170 157 CNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNF 193
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-193 5.96e-64

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 196.20  E-value: 5.96e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNlgKPFLGICL 80
Cdd:PRK13142   1 MIVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTD--KKMIGICL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEElKDCSGLSLLPGVIRKLKVPYKIPHMGWNELKKEGeiPLWNgiedgSFVYYVHSYYADCPKGIVyGASE 160
Cdd:PRK13142  79 GMQLMYEHSDE-GDASGLGFIPGNISRIQTEYPVPHLGWNNLVSKH--PMLN-----QDVYFVHSYQAPMSENVI-AYAQ 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446482785 161 YGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILK 193
Cdd:PRK13142 150 YGADIPAIVQFNNYIGIQFHPEKSGTYGLQILR 182
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-201 1.31e-61

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 200.32  E-value: 1.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICLG 81
Cdd:PLN02617   9 VTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLGICLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  82 MQLLFEKSEELKDCSGLSLLPGVIRKLKV--PYKIPHMGWNELKKEGEIPLWNGIeDGSFVYYVHSYYA---DCPKGIVY 156
Cdd:PLN02617  89 LQLLFESSEENGPVEGLGVIPGVVGRFDSsnGLRVPHIGWNALQITKDSELLDGV-GGRHVYFVHSYRAtpsDENKDWVL 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446482785 157 GASEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNFKGVVEA 201
Cdd:PLN02617 168 ATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFLEPKSS 212
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-195 2.69e-55

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 174.64  E-value: 2.69e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKE-IGNLGKPFLGIC 79
Cdd:PRK13152   1 MIALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEqVLVQKKPILGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  80 LGMQLLFEKSEELKDCSGLSLLPG-VIR-KLKVPYKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADCPKGIVYG 157
Cdd:PRK13152  81 LGMQLFLERGYEGGVCEGLGFIEGeVVKfEEDLNLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFYVKCKDEFVSA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446482785 158 ASEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:PRK13152 161 KAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENF 198
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 2-195 1.62e-52

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 167.75  E-value: 1.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICLG 81
Cdd:CHL00188   4 IGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEGNPFIGICLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  82 MQLLFEKSEELKDcSGLSLLPGVIRKLKVP--YKIPHMGWNELK------KEGEIPLWNGIEDGSFVYYVHSYYADcPKG 153
Cdd:CHL00188  84 LHLLFETSEEGKE-EGLGIYKGQVKRLKHSpvKVIPHMGWNRLEcqnsecQNSEWVNWKAWPLNPWAYFVHSYGVM-PKS 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446482785 154 --IVYGASEYG-VQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:CHL00188 162 qaCATTTTFYGkQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREF 206
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-195 1.61e-49

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 160.07  E-value: 1.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGMGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:PRK14004   1 MIAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVESGKPLFGICI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  81 GMQLLFEKSEEL------KDCSGLSLLPGVIRKLK-VPYKIPHMGWNEL--KKEGEIPLWNGIEDGSFVYYVHSYYADCP 151
Cdd:PRK14004  81 GFQILFESSEETnqgtkkEQIEGLGYIKGKIKKFEgKDFKVPHIGWNRLqiRRKDKSKLLKGIGDQSFFYFIHSYRPTGA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446482785 152 KG--IVYGASEYGVQVPGFVAKGNVFGAQFHPEKSGEVGIQILKNF 195
Cdd:PRK14004 161 EGnaITGLCDYYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENF 206
GATase pfam00117
Glutamine amidotransferase class-I;
3-195 7.69e-26

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 98.46  E-value: 7.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785    3 AIVDYGMGNICSVEQALKYIGAEYIV---TDDREEILRS--DGVIL-PGVGAfPKAMDVLEEkklvfVLKEIGNLGKPFL 76
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpnDTPAEEILEEnpDGIILsGGPGS-PGAAGGAIE-----AIREARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   77 GICLGMQLLFEKSEelkdcsglsllpGVIRKLKvpyKIPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYAD---CPKG 153
Cdd:pfam00117  75 GICLGHQLLALAFG------------GKVVKAK---KFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDpdtLPDG 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446482785  154 I-VYGASEYGVQVPGFVAKGN-VFGAQFHPEK-SGEVGIQILKNF 195
Cdd:pfam00117 140 LeVTATSENDGTIMGIRHKKLpIFGVQFHPESiLTPHGPEILFNF 184
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-86 1.11e-10

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: 56.84  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNIC---SVEQALKYIGAEYIVTDDREEILRS-------DGVILPGVGAFPKAMDVLEEkkLVFVLKEIGNL 71
Cdd:cd01653    1 VAVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVESdvdlddyDGLILPGGPGTPDDLARDEA--LLALLREAAAA 78

                         90
                 ....*....|....*
gi 446482785  72 GKPFLGICLGMQLLF 86
Cdd:cd01653   79 GKPILGICLGAQLLV 93
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 17-195 1.53e-10

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 57.93  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  17 QALKYIGAEYIV------TDDREEILRSDGVIL-PGVGAfPKamdvlEEKKLVFVLKEIGNLgKPFLGICLGMQLLFEks 89
Cdd:cd01743   16 QYLRELGAEVVVvrndeiTLEELELLNPDAIVIsPGPGH-PE-----DAGISLEIIRALAGK-VPILGVCLGHQAIAE-- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  90 eelkdCSGlsllpGVIRKLKVPY-----KIPHMGWNELKkegeiplwnGIEDGSFVYYVHSYYADC---PKGIVYGASEY 161
Cdd:cd01743   87 -----AFG-----GKVVRAPEPMhgktsEIHHDGSGLFK---------GLPQPFTVGRYHSLVVDPdplPDLLEVTASTE 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446482785 162 -----GVQVPGFvakgNVFGAQFHPEkS--GEVGIQILKNF 195
Cdd:cd01743  148 dgvimALRHRDL----PIYGVQFHPE-SilTEYGLRLLENF 183
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 15-182 2.30e-10

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 58.03  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  15 VEQALKYIGAEYIVTD-DREEILRS-------DGVILPGvGAfpkaMDVLEEKKLVF----VLKEIGNLGKPFLGICLGM 82
Cdd:COG0518   18 IARRLREAGIELDVLRvYAGEILPYdpdledpDGLILSG-GP----MSVYDEDPWLEdepaLIREAFELGKPVLGICYGA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  83 QLLfekSEELkdcsGlsllpGVIRKLKVpykiPHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYADC-PKG-IVYGASE 160
Cdd:COG0518   93 QLL---AHAL----G-----GKVEPGPG----REIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTElPEGaEVLASSD 156

                        170       180
                 ....*....|....*....|...
gi 446482785 161 -YGVQvpGFVAKGNVFGAQFHPE 182
Cdd:COG0518  157 nCPNQ--AFRYGRRVYGVQFHPE 177
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 1.62e-09

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: 52.97  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNIC---SVEQALKYIGAEYIVTDDREEILRS-------DGVILPGVGAFPKAMDVLEEkkLVFVLKEIGNL 71
Cdd:cd03128    1 VAVLLFGGSEELelaSPLDALREAGAEVDVVSPDGGPVESdvdlddyDGLILPGGPGTPDDLAWDEA--LLALLREAAAA 78

                         90
                 ....*....|....
gi 446482785  72 GKPFLGICLGMQLL 85
Cdd:cd03128   79 GKPVLGICLGAQLL 92
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 2-102 2.66e-09

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: 54.56  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYG-MGNICSVEQALKYIGAEYIVTDDREEILRSDGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLGKPFLGICL 80
Cdd:cd01750    1 IAVIRYPdISNFTDLDPLAREPGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGICG 80

                         90       100
                 ....*....|....*....|....*...
gi 446482785  81 GMQLLFEK------SEELKDCSGLSLLP 102
Cdd:cd01750   81 GYQMLGKYivdpegVEGPGEIEGLGLLD 108
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-195 2.06e-07

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 49.24  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785    2 IAIVDYGMGNICSVEQALKYIG--AEYIVTDDREEILRS---DGVILPGVGAFPKAMDVLEekklvfVLKEIGNLGKPFL 76
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGvySELVPNTTPLEEIREknpKGIILSGGPSSVYAENAPR------ADEKIFELGVPVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   77 GICLGMQLL-------FEKSEElkdcsglsllpgvirklkvpykiPHMGWNELKKEGEIPLWNGIEDGSFVYYVH-SYYA 148
Cdd:TIGR00888  75 GICYGMQLMakqlggeVGRAEK-----------------------REYGKAELEILDEDDLFRGLPDESTVWMSHgDKVK 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446482785  149 DCPKGIVYGASEYGVQVPGFVAKGN-VFGAQFHPE-KSGEVGIQILKNF 195
Cdd:TIGR00888 132 ELPEGFKVLATSDNCPVAAMAHEEKpIYGVQFHPEvTHTEYGNELLENF 180
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 66-195 2.21e-07

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 49.07  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  66 KEIGNLGKPFLGICLGMQLLFEkseelkdcsglsLLPGVIRKLKVPYkiphMGWNELKKEGEIPLWNGIEDGSFVYYVHs 145
Cdd:cd01742   64 PEIFELGVPVLGICYGMQLIAK------------ALGGKVERGDKRE----YGKAEIEIDDSSPLFEGLPDEQTVWMSH- 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446482785 146 yyAD----CPKGIVYGASEYGVQVPGFVAKG-NVFGAQFHPE-KSGEVGIQILKNF 195
Cdd:cd01742  127 --GDevvkLPEGFKVIASSDNCPVAAIANEEkKIYGVQFHPEvTHTEKGKEILKNF 180
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 1-195 6.46e-07

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: 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. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 47.63  E-value: 6.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIV----DYGMGNICSVEQALKYIGAEYIVTD-DREEILRS----DGVILPGvGAfpkaMDVLEE-----KKLVFVLK 66
Cdd:cd01741    1 RILILqhdtPEGPGLFEDLLREAGAETIEIDVVDvYAGELLPDlddyDGLVILG-GP----MSVDEDdypwlKKLKELIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  67 EIGNLGKPFLGICLGMQLLfekseelkdcsGLSLLPGVIRKlkvPYKIPhMGW--NELKKEG-EIPLWNGIEDGSFVYYV 143
Cdd:cd01741   76 QALAAGKPVLGICLGHQLL-----------ARALGGKVGRN---PKGWE-IGWfpVTLTEAGkADPLFAGLPDEFPVFHW 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446482785 144 HSyyaDC----PKG-IVYGASE-YGVQvpGFVAKGNVFGAQFHPEKsgevgiQILKNF 195
Cdd:cd01741  141 HG---DTvvelPPGaVLLASSEaCPNQ--AFRYGDRALGLQFHPEE------RLLRNF 187
guaA PRK00074
GMP synthase; Reviewed
 66-195 6.78e-07

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 48.89  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  66 KEIGNLGKPFLGICLGMQLLFEkseelkdcsglsLLPGVIRKLKVP-YkiphmGWNELKKEGEIPLWNGIEDGSFVYYVH 144
Cdd:PRK00074  69 PEIFELGVPVLGICYGMQLMAH------------QLGGKVERAGKReY-----GRAELEVDNDSPLFKGLPEEQDVWMSH 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446482785 145 SyyaDC----PKGIVYGASEYGVQVPGF-VAKGNVFGAQFHPeksgEV-----GIQILKNF 195
Cdd:PRK00074 132 G---DKvtelPEGFKVIASTENCPIAAIaNEERKFYGVQFHP----EVthtpqGKKLLENF 185
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 63-182 2.18e-06

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 46.88  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  63 FVLKEIGNLG------KPFLGICLGMQLLfekseelkdcsglsllpgvIRKL--KVPykiPH------MGWNELK--KEG 126
Cdd:PRK06490  71 FIRREIDWISvplkenKPFLGICLGAQML-------------------ARHLgaRVA---PHpdgrveIGYYPLRptEAG 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446482785 127 -EIPLWNgiedgSFVYYVHSYYADCPKGIVYGASEYGVQVPGFVAKGNVFGAQFHPE 182
Cdd:PRK06490 129 rALMHWP-----EMVYHWHREGFDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPE 180
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-198 2.78e-06

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 46.00  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   1 MIAIVDYGmGNICSVEQ-ALKYIGAEY-IV--TDDREEIL-RSDGVILPGvGAfpkAMDvleekKLVFVLKEIGNLGKPF 75
Cdd:PRK00758   1 KIVVVDNG-GQYNHLIHrTLRYLGVDAkIIpnTTPVEEIKaFEDGLILSG-GP---DIE-----RAGNCPEYLKELDVPI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  76 LGICLGMQLLFEKseelkdcsglslLPGVIRKLKVP-YkiphmGWNELKKEGEIPLWNGIEDGSFVYYVHsyyAD----C 150
Cdd:PRK00758  71 LGICLGHQLIAKA------------FGGEVGRGEYGeY-----ALVEVEILDEDDILKGLPPEIRVWASH---ADevkeL 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446482785 151 PKGIVYGASEYGVQVPGFVAKGN-VFGAQFHPE-KSGEVGIQILKNFKGV 198
Cdd:PRK00758 131 PDGFEILARSDICEVEAMKHKEKpIYGVQFHPEvAHTEYGEEIFKNFLEI 180
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 17-195 2.23e-05

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 43.49  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  17 QALKYIGAEYIV----TDDREEI--LRSDGVIL-PGVGAfPKAMDVLEEkklvfVLKEIGNlGKPFLGICLGMQLLFEks 89
Cdd:COG0512   16 QYLGELGAEVVVvrndEITLEEIeaLAPDGIVLsPGPGT-PEEAGISLE-----VIRAFAG-KIPILGVCLGHQAIGE-- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  90 eelkdCSGlsllpGVIRKLKVPY-----KIPHmgwnelkkEGEiPLWNGIEDGSFV--YyvHSYYAD---CPKG-IVYGA 158
Cdd:COG0512   87 -----AFG-----GKVVRAPEPMhgktsPITH--------DGS-GLFAGLPNPFTAtrY--HSLVVDretLPDElEVTAW 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446482785 159 SEYGVqVPGFVAKG-NVFGAQFHPEkS--GEVGIQILKNF 195
Cdd:COG0512  146 TEDGE-IMGIRHRElPIEGVQFHPE-SilTEHGHQLLANF 183
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 2-85 1.58e-04

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 40.94  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGMGNicSVEQALKYIGAEYIV----TDDRE-EILRSDGVIL---PGvgafpkamDVLEEKKLVFVLKEIGNLGK 73
Cdd:cd01744    1 VVVIDFGVKH--NILRELLKRGCEVTVvpynTDAEEiLKLDPDGIFLsngPG--------DPALLDEAIKTVRKLLGKKI 70

                         90
                 ....*....|..
gi 446482785  74 PFLGICLGMQLL 85
Cdd:cd01744   71 PIFGICLGHQLL 82
PRK13566 PRK13566
anthranilate synthase component I;
74-194 1.65e-04

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 41.83  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  74 PFLGICLGMQLLFEKseelkdcsglslLPGVIRKLKVPYkipHMGWNELKKEGEIPLWNGIEDGSFVYYVHSYYAD---C 150
Cdd:PRK13566 600 PIFGVCLGLQAIVEA------------FGGELGQLAYPM---HGKPSRIRVRGPGRLFSGLPEEFTVGRYHSLFADpetL 664

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446482785 151 PKG-IVYGASEYGVqVPGFVAKGN-VFGAQFHPEK----SGEVGIQILKN 194
Cdd:PRK13566 665 PDElLVTAETEDGV-IMAIEHKTLpVAAVQFHPESimtlGGDVGLRIIEN 713
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
2-85 1.73e-04

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 41.60  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   2 IAIVDYGM-GNICSveqALKYIGAEYIV---TDDREEILRS--DGVIL---PGVgafPKAMDVLEEkklvfVLKEIGNLG 72
Cdd:PRK12564 180 VVAIDFGVkRNILR---ELAERGCRVTVvpaTTTAEEILALnpDGVFLsngPGD---PAALDYAIE-----MIRELLEKK 248

                         90
                 ....*....|...
gi 446482785  73 KPFLGICLGMQLL 85
Cdd:PRK12564 249 IPIFGICLGHQLL 261
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
2-106 3.87e-04

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 39.92  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785    2 IAIVD------YGMGNIcsveQALKYIGAE--YIVTDDREEILRS-DGVILPGVGAFPKAMDVLEEKKLVFVLKEIGNLG 72
Cdd:pfam07685   2 IAVIRlprisnYTDDNL----DPLRYEPAVrvRFVPLPDESLGPDaDLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446482785   73 KPFLGICLGMQLLfekSEELKD-----CSGLSLLPGVIR 106
Cdd:pfam07685  78 GPVLGICGGYQML---GETIEDpegvrIEGLGLLDIETV 113
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 8-84 4.26e-04

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 40.38  E-value: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   8 GMGNICSVEqaLKYIGAEYIVTDDREEILRS-DGVILPG----------VGAFPKAMdvleEKKLvfvlkeignlgkPFL 76
Cdd:COG0504  316 GIANGVKVN--IKWIDSEDLEEENAEELLKGvDGILVPGgfgergiegkIAAIRYAR----ENKI------------PFL 377


                 ....*...
gi 446482785  77 GICLGMQL 84
Cdd:COG0504  378 GICLGMQL 385
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 33-85 4.53e-04

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 40.39  E-value: 4.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446482785  33 EEILRS--DGVIL---PGVgafPKAMDVLEEkklvfVLKEIGNLGKPFLGICLGMQLL 85
Cdd:COG0505  211 EEILALnpDGVFLsngPGD---PAALDYAIE-----TIRELLGKGIPIFGICLGHQLL 260
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 18-84 1.04e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 38.69  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446482785  18 ALKYIGAEYIVTDDREEILRS-DGVILPGvgAFPKaMDVleEKKLVFVLKEIGNlGKPFLGICLGMQL 84
Cdd:cd01746   35 EIKWIDSEDLEEENAEEALKGaDGILVPG--GFGI-RGV--EGKILAIKYAREN-NIPFLGICLGMQL 96
pyrG PRK05380
CTP synthetase; Validated
 8-84 1.38e-03

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 38.85  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785   8 GMGNICSVEqaLKYIGAEYIVTDDREEILRS-DGVILPG----------VGAFPKAMdvleEKKlvfvlkeignlgKPFL 76
Cdd:PRK05380 315 GIANDVKVN--IKWIDSEDLEEENVAELLKGvDGILVPGgfgergiegkILAIRYAR----ENN------------IPFL 376


                 ....*...
gi 446482785  77 GICLGMQL 84
Cdd:PRK05380 377 GICLGMQL 384
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 30-85 2.86e-03

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 37.46  E-value: 2.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446482785  30 DDREEILRS-DGVILPG----------------VGAFPKAMDVLEekklVFVLKEIGNLGKPFLGICLGMQLL 85
Cdd:COG2071   41 EDLDELLDRlDGLVLTGgadvdpalygeephpeLGPIDPERDAFE----LALIRAALERGKPVLGICRGMQLL 109
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 18-182 3.16e-03

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 37.38  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  18 ALKYIGAEYIVTDDREEILRSDGVILPGvgAFPKAMDVLEEKKLVF-VLKEIGNLGKPFLGICLGMQLLFEKSEELKDcS 96
Cdd:PLN02832  19 ALRRLGVEAVEVRKPEQLEGVSGLIIPG--GESTTMAKLAERHNLFpALREFVKSGKPVWGTCAGLIFLAERAVGQKE-G 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  97 GLSLLPGV------------IRKLKVPYKIPHMGwnelKKEGEIPLWNGI--------EDGSFVYYVhsyyADCP----- 151
Cdd:PLN02832  96 GQELLGGLdctvhrnffgsqINSFETELPVPELA----ASEGGPETFRAVfirapailSVGPGVEVL----AEYPlpsek 167

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446482785 152 KGIVYGASEYGV-QVPGFVAKGNVFGAQFHPE 182
Cdd:PLN02832 168 ALYSSSTDAEGRdKVIVAVKQGNLLATAFHPE 199
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 18-101 5.41e-03

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: 36.35  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785  18 ALKYIGAEYIVTDDREEILRSDGVILPG-----VGAFPKAMDVLEEkklvfvLKEIGNLGKPFLGICLGMQLLFEKSEEL 92
Cdd:cd01749   16 ALERLGVEVIEVRTPEDLEGIDGLIIPGgesttIGKLLRRTGLLDP------LREFIRAGKPVFGTCAGLILLAKEVEDQ 89


                 ....*....
gi 446482785  93 KDCSGLSLL 101
Cdd:cd01749   90 GGQPLLGLL 98
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
39-104 5.84e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 36.63  E-value: 5.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446482785  39 DGVILPG---------VGAFPKAMDVLEEkklvfvLKEIGNLGKPFLGICLGMQLLFEkseelkdcSGlsLLPGV 104
Cdd:PRK03619  43 DAVVLPGgfsygdylrCGAIAAFSPIMKA------VKEFAEKGKPVLGICNGFQILTE--------AG--LLPGA 101
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 3-84 5.91e-03

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 36.92  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446482785    3 AIVDYGMGNICSVEqaLKYIGAEYIVTDDREEILRSDGVILPG------VGAFPKAMDVLEEKKLvfvlkeignlgkPFL 76
Cdd:TIGR00337 311 ALKHAGAKLDTKVN--IKWIDSEDLEEEGVEFLKGLDGILVPGgfgergVEGKILAIKYARENNI------------PFL 376


                  ....*...
gi 446482785   77 GICLGMQL 84
Cdd:TIGR00337 377 GICLGMQL 384
 
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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