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Conserved domains on  [gi|1595861189|ref|WP_133319969|]
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MULTISPECIES: imidazole glycerol phosphate synthase subunit HisH [Campylobacter]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10785031)

type 1 glutamine amidotransferase subunit (HisH) of imidazole glycerol phosphate synthase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-196 4.40e-97

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: 280.00  E-value: 4.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGIC 80
Cdd:COG0118     2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAV-AGGKPVLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKFDLSKEKLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVE-CLESVET 159
Cdd:COG0118    81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIA-KDHPLFAGIPDGEYFYFVHSYYVPpDDPEDVV 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLE 196
Cdd:COG0118   160 ATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
 
Name Accession Description Interval E-value
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-196 4.40e-97

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: 280.00  E-value: 4.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGIC 80
Cdd:COG0118     2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAV-AGGKPVLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKFDLSKEKLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVE-CLESVET 159
Cdd:COG0118    81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIA-KDHPLFAGIPDGEYFYFVHSYYVPpDDPEDVV 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLE 196
Cdd:COG0118   160 ATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-201 1.27e-94

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 274.02  E-value: 1.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVLKDKKPILGIC 80
Cdd:PRK13152    1 MIALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVLVQKKPILGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKFDLSKE-KLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVECLESVET 159
Cdd:PRK13152   81 LGMQLFLERGYEGGVCEGLGFIEGEVVKFEEDLNlKIPHMGWNELEIL-KQSPLYQGIPEKSDFYFVHSFYVKCKDEFVS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFANL 201
Cdd:PRK13152  160 AKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-198 3.34e-94

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: 272.83  E-value: 3.34e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGICL 81
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAI-ASGKPFLGICL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  82 GMQLFASKGYEGGECEGLDFIKAKVLKFDLSKE-KLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVECLESVET- 159
Cdd:cd01748    80 GMQLLFESSEEGGGTKGLGLIPGKVVRFPASEGlKVPHMGWNQLEIT-KESPLFKGIPDGSYFYFVHSYYAPPDDPDYIl 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENF 198
Cdd:cd01748   159 ATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-201 1.73e-80

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: 237.99  E-value: 1.73e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDeLLKECVLKDKKPILGICL 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLD-LFVELVVRLGKPVLGICL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  82 GMQLFASKGYEGGECEGLDFIKAKVLKFDLskEKLLHSGWDDLqFSDKKSKLFDGILEKSDFYFVHSYYVECLESVETSF 161
Cdd:TIGR01855  80 GMQLLFERSEEGGGVPGLGLIKGNVVKLEA--RKVPHMGWNEV-HPVKESPLLNGIDEGAYFYFVHSYYAVCEEEAVLAY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1595861189 162 CEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFANL 201
Cdd:TIGR01855 157 ADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase pfam00117
Glutamine amidotransferase class-I;
4-198 1.57e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 84.60  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   4 IVDYHLGNFKSVLKAFEKLNQEVII----SSKKEDIKNASKLVL--PGVGSFK--QGMENLKKLALDEllkecvlkdKKP 75
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVvpndTPAEEILEENPDGIIlsGGPGSPGaaGGAIEAIREAREL---------KIP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  76 ILGICLGMQLFAskgyeggECEGLDFIKAKvlkfdlskeKLLHSGWdDLQFSDKKSKLFDGILEKSDFYFVHSYYV---- 151
Cdd:pfam00117  73 ILGICLGHQLLA-------LAFGGKVVKAK---------KFGHHGK-NSPVGDDGCGLFYGLPNVFIVRRYHSYAVdpdt 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595861189 152 --ECLEsvETSFCEYEKPFCASFEKDN-IFAVQFHPEKSQNV-GLKLLENF 198
Cdd:pfam00117 136 lpDGLE--VTATSENDGTIMGIRHKKLpIFGVQFHPESILTPhGPEILFNF 184
 
Name Accession Description Interval E-value
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-196 4.40e-97

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: 280.00  E-value: 4.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGIC 80
Cdd:COG0118     2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAV-AGGKPVLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKFDLSKEKLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVE-CLESVET 159
Cdd:COG0118    81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIA-KDHPLFAGIPDGEYFYFVHSYYVPpDDPEDVV 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLE 196
Cdd:COG0118   160 ATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-201 1.27e-94

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 274.02  E-value: 1.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVLKDKKPILGIC 80
Cdd:PRK13152    1 MIALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVLVQKKPILGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKFDLSKE-KLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVECLESVET 159
Cdd:PRK13152   81 LGMQLFLERGYEGGVCEGLGFIEGEVVKFEEDLNlKIPHMGWNELEIL-KQSPLYQGIPEKSDFYFVHSFYVKCKDEFVS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFANL 201
Cdd:PRK13152  160 AKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-198 3.34e-94

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: 272.83  E-value: 3.34e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGICL 81
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAI-ASGKPFLGICL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  82 GMQLFASKGYEGGECEGLDFIKAKVLKFDLSKE-KLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVECLESVET- 159
Cdd:cd01748    80 GMQLLFESSEEGGGTKGLGLIPGKVVRFPASEGlKVPHMGWNQLEIT-KESPLFKGIPDGSYFYFVHSYYAPPDDPDYIl 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENF 198
Cdd:cd01748   159 ATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-203 1.34e-93

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 271.62  E-value: 1.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGIC 80
Cdd:PRK13141    1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAV-ASGKPLLGIC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKF-DLSKEKLLHSGWDDLQFsDKKSKLFDGILEKSDFYFVHSYYVE-CLESVE 158
Cdd:PRK13141   80 LGMQLLFESSEEFGETEGLGLLPGRVRRFpPEEGLKVPHMGWNQLEL-KKESPLLKGIPDGAYVYFVHSYYADpCDEEYV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1595861189 159 TSFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFANLKA 203
Cdd:PRK13141  159 AATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVE 203
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-201 8.71e-91

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 264.42  E-value: 8.71e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGIC 80
Cdd:PRK13181    1 MIAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHV-EKKQPVLGIC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGeCEGLDFIKAKVLKFDLSKEKLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVECLESVET- 159
Cdd:PRK13181   80 LGMQLLFESSEEGN-VKGLGLIPGDVKRFRSEPLKVPQMGWNSVKPL-KESPLFKGIEEGSYFYFVHSYYVPCEDPEDVl 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFANL 201
Cdd:PRK13181  158 ATTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL 199
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-201 1.73e-80

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: 237.99  E-value: 1.73e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDeLLKECVLKDKKPILGICL 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLD-LFVELVVRLGKPVLGICL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  82 GMQLFASKGYEGGECEGLDFIKAKVLKFDLskEKLLHSGWDDLqFSDKKSKLFDGILEKSDFYFVHSYYVECLESVETSF 161
Cdd:TIGR01855  80 GMQLLFERSEEGGGVPGLGLIKGNVVKLEA--RKVPHMGWNEV-HPVKESPLLNGIDEGAYFYFVHSYYAVCEEEAVLAY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1595861189 162 CEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFANL 201
Cdd:TIGR01855 157 ADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-201 1.88e-75

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 225.52  E-value: 1.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLAldELLKECVlKDKKPILGIC 80
Cdd:PRK13143    2 MIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSPLR--DVILEAA-RSGKPFLGIC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKFDlSKEKLLHSGWDDLqFSDKKSKLFDGIlEKSDFYFVHSYYVECLE-SVET 159
Cdd:PRK13143   79 LGMQLLFESSEEGGGVRGLGLFPGRVVRFP-AGVKVPHMGWNTV-KVVKDCPLFEGI-DGEYVYFVHSYYAYPDDeDYVV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1595861189 160 SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFANL 201
Cdd:PRK13143  156 ATTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVEL 197
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-200 1.30e-70

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 213.49  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGNFKSVLKAFEKL--NQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVLKDKKPILGI 79
Cdd:PRK13146    4 VAIIDYGSGNLRSAAKALERAgaGADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAVLAAGRPFLGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  80 CLGMQLFASKGYEGGECEGLDFIKAKVLKFDLSKE--KLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVECLESV 157
Cdd:PRK13146   84 CVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDGPalKVPHMGWNTVDQT-RDHPLFAGIPDGARFYFVHSYYAQPANPA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1595861189 158 ET-SFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENFAN 200
Cdd:PRK13146  163 DVvAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLA 206
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-198 1.46e-64

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 197.77  E-value: 1.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECvlkdKKPILGIC 80
Cdd:PRK13170    2 NVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKAC----TQPVLGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEGGECEGLDFIKAKVLKFDLSKEKLLHSGWDDLQFSdKKSKLFDGILEKSDFYFVHSYYVEcLESVETS 160
Cdd:PRK13170   78 LGMQLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQ-AGHPLFQGIEDGSYFYFVHSYAMP-VNEYTIA 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1595861189 161 FCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENF 198
Cdd:PRK13170  156 QCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNF 193
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 4-198 1.91e-51

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 173.36  E-value: 1.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   4 IVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVLKDkKPILGICLGM 83
Cdd:PLN02617   11 LLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQND-RPFLGICLGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  84 QLFASKGYEGGECEGLDFIKAKVLKFDLSKE-KLLHSGWDDLQFSdKKSKLFDGIlEKSDFYFVHSYYVecLESVE---- 158
Cdd:PLN02617   90 QLLFESSEENGPVEGLGVIPGVVGRFDSSNGlRVPHIGWNALQIT-KDSELLDGV-GGRHVYFVHSYRA--TPSDEnkdw 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1595861189 159 -TSFCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENF 198
Cdd:PLN02617  166 vLATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRF 206
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-198 2.56e-48

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 156.99  E-value: 2.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGIC 80
Cdd:PRK14004    1 MIAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHV-ESGKPLFGIC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQ-LFAS-----KGYEGGECEGLDFIKAKVLKFDLSKEKLLHSGWDDLQF-SDKKSKLFDGILEKSDFYFVHSYYVEC 153
Cdd:PRK14004   80 IGFQiLFESseetnQGTKKEQIEGLGYIKGKIKKFEGKDFKVPHIGWNRLQIrRKDKSKLLKGIGDQSFFYFIHSYRPTG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1595861189 154 LESVE-TSFCE-YEKPFCASFEKDNIFAVQFHPEKSQNVGLKLLENF 198
Cdd:PRK14004  160 AEGNAiTGLCDyYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENF 206
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-195 6.31e-47

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 152.67  E-value: 6.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKEcvlKDKKPILGIC 80
Cdd:PRK13142    1 MIVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAK---NTDKKMIGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  81 LGMQLFASKGYEgGECEGLDFIKAKVLKFDlSKEKLLHSGWDDLqfsdkKSKlfdGILEKSDFYFVHSYYVECLESVeTS 160
Cdd:PRK13142   78 LGMQLMYEHSDE-GDASGLGFIPGNISRIQ-TEYPVPHLGWNNL-----VSK---HPMLNQDVYFVHSYQAPMSENV-IA 146

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1595861189 161 FCEYEKPFCASFEKDNIFAVQFHPEKSQNVGLKLL 195
Cdd:PRK13142  147 YAQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQIL 181
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 2-198 8.79e-46

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 150.42  E-value: 8.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVLKDkKPILGICL 81
Cdd:CHL00188    4 IGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEG-NPFIGICL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  82 GMQLFASKGYEGGEcEGLDFIKAKVLKFDLSKEKLL-HSGWDDLQFS-----DKKSKLFDGILEKSDFYFVHSYYVE--- 152
Cdd:CHL00188   83 GLHLLFETSEEGKE-EGLGIYKGQVKRLKHSPVKVIpHMGWNRLECQnsecqNSEWVNWKAWPLNPWAYFVHSYGVMpks 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1595861189 153 CLESVETSFCEYEKpFCASFEKDNIFAVQFHPEKSQNVGLKLLENF 198
Cdd:CHL00188  162 QACATTTTFYGKQQ-MVAAIEYDNIFAMQFHPEKSGEFGLWLLREF 206
GATase pfam00117
Glutamine amidotransferase class-I;
4-198 1.57e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 84.60  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   4 IVDYHLGNFKSVLKAFEKLNQEVII----SSKKEDIKNASKLVL--PGVGSFK--QGMENLKKLALDEllkecvlkdKKP 75
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVvpndTPAEEILEENPDGIIlsGGPGSPGaaGGAIEAIREAREL---------KIP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  76 ILGICLGMQLFAskgyeggECEGLDFIKAKvlkfdlskeKLLHSGWdDLQFSDKKSKLFDGILEKSDFYFVHSYYV---- 151
Cdd:pfam00117  73 ILGICLGHQLLA-------LAFGGKVVKAK---------KFGHHGK-NSPVGDDGCGLFYGLPNVFIVRRYHSYAVdpdt 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595861189 152 --ECLEsvETSFCEYEKPFCASFEKDN-IFAVQFHPEKSQNV-GLKLLENF 198
Cdd:pfam00117 136 lpDGLE--VTATSENDGTIMGIRHKKLpIFGVQFHPESILTPhGPEILFNF 184
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 73-199 4.03e-10

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: 56.55  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  73 KKPILGICLGMQLFASkgYEGGECEgldfiKAKVLKFDLSKEKLlhsgwddlqfsDKKSKLFDGILEKSDFYFVHSYYVE 152
Cdd:TIGR00888  70 GVPVLGICYGMQLMAK--QLGGEVG-----RAEKREYGKAELEI-----------LDEDDLFRGLPDESTVWMSHGDKVK 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595861189 153 CLES-----VETSFCeyekPFCA-SFEKDNIFAVQFHPEKSQNV-GLKLLENFA 199
Cdd:TIGR00888 132 ELPEgfkvlATSDNC----PVAAmAHEEKPIYGVQFHPEVTHTEyGNELLENFV 181
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 59-199 6.07e-10

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: 56.10  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  59 LALDELLKECvLKDKKPILGICLGMQLFAskgyeggECEGldfikAKVLKFDLSKEkllhSGWDDLQFSD--KKSKLFDG 136
Cdd:cd01741    68 KKLKELIRQA-LAAGKPVLGICLGHQLLA-------RALG-----GKVGRNPKGWE----IGWFPVTLTEagKADPLFAG 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595861189 137 ILEKSDFYFVHSYYVECL--ESV---ETSFCEYEkpfcaSFE-KDNIFAVQFHPEKsqnvglKLLENFA 199
Cdd:cd01741   131 LPDEFPVFHWHGDTVVELppGAVllaSSEACPNQ-----AFRyGDRALGLQFHPEE------RLLRNFL 188
guaA PRK00074
GMP synthase; Reviewed
 69-199 6.26e-10

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 57.75  E-value: 6.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  69 VLKDKKPILGICLGMQLFASkgYEGGECEGLD---FIKAKVlkfdlskekllhsgwddlqFSDKKSKLFDGILEKSDFYF 145
Cdd:PRK00074   71 IFELGVPVLGICYGMQLMAH--QLGGKVERAGkreYGRAEL-------------------EVDNDSPLFKGLPEEQDVWM 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595861189 146 VHSYYVECL----ESV-ETSFCeyekPFCA-SFEKDNIFAVQFHPEksqnV-----GLKLLENFA 199
Cdd:PRK00074  130 SHGDKVTELpegfKVIaSTENC----PIAAiANEERKFYGVQFHPE----VthtpqGKKLLENFV 186
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 69-199 5.45e-09

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: 53.31  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  69 VLKDKKPILGICLGMQLFAsKGYEG--GECEGLDFIKAKVLkfdlskekllhsgwddlqfSDKKSKLFDGILEKSDFYFV 146
Cdd:cd01742    66 IFELGVPVLGICYGMQLIA-KALGGkvERGDKREYGKAEIE-------------------IDDSSPLFEGLPDEQTVWMS 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595861189 147 HSYYVECLES-----VETSFCEYekpfcASF--EKDNIFAVQFHPE--KSQNvGLKLLENFA 199
Cdd:cd01742   126 HGDEVVKLPEgfkviASSDNCPV-----AAIanEEKKIYGVQFHPEvtHTEK-GKEILKNFL 181
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 69-185 5.48e-09

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: 53.80  E-value: 5.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  69 VLKDKKPILGICLGMQLFASkgYEGGECEgldfiKAKVlkfdlsKEKllhsGWDDLQFSDkKSKLFDGILEKSDFYFVHS 148
Cdd:COG0518    78 AFELGKPVLGICYGAQLLAH--ALGGKVE-----PGPG------REI----GWAPVELTE-ADPLFAGLPDEFTVWMSHG 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1595861189 149 YYVECL--ESV---ETSFCEYekpfcASFE-KDNIFAVQFHPE 185
Cdd:COG0518   140 DTVTELpeGAEvlaSSDNCPN-----QAFRyGRRVYGVQFHPE 177
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 5.89e-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: 51.43  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGN---FKSVLKAFEKLNQEVIISSKKE-------DIKNASKLVLPGVGSFKQGMENLKKLAldELLKECVlK 71
Cdd:cd03128     1 VAVLLFGGSEeleLASPLDALREAGAEVDVVSPDGgpvesdvDLDDYDGLILPGGPGTPDDLAWDEALL--ALLREAA-A 77

                          90
                  ....*....|....
gi 1595861189  72 DKKPILGICLGMQL 85
Cdd:cd03128    78 AGKPVLGICLGAQL 91
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 69-198 1.57e-08

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: 52.15  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  69 VLKDKKPILGICLGMQLFAskgyeggECEGLDFIKAKVLKFDLSKEkLLHSGwddlqfsdkkSKLFDGIleKSDFYFV-- 146
Cdd:cd01743    67 ALAGKVPILGVCLGHQAIA-------EAFGGKVVRAPEPMHGKTSE-IHHDG----------SGLFKGL--PQPFTVGry 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595861189 147 HSYYVEcLESVETSFCEyekpfCASFE----------KDNIFAVQFHPE--KSQNvGLKLLENF 198
Cdd:cd01743   127 HSLVVD-PDPLPDLLEV-----TASTEdgvimalrhrDLPIYGVQFHPEsiLTEY-GLRLLENF 183
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 2.45e-08

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: 50.29  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDYHLGN---FKSVLKAFEKLNQEVIISSKKE-------DIKNASKLVLPGVGSFKQGMENLKKLAldELLKECVlK 71
Cdd:cd01653     1 VAVLLFPGFEeleLASPLDALREAGAEVDVVSPDGgpvesdvDLDDYDGLILPGGPGTPDDLARDEALL--ALLREAA-A 77

                          90
                  ....*....|....
gi 1595861189  72 DKKPILGICLGMQL 85
Cdd:cd01653    78 AGKPILGICLGAQL 91
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 63-201 6.40e-08

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: 50.42  E-value: 6.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  63 ELLKECvlKDKKPILGICLGMQLFaskgyegGECEGLDFIKAKVL---KfdlsKEKLLHSGwddlqfsdkkSKLFDGIle 139
Cdd:COG0512    63 EVIRAF--AGKIPILGVCLGHQAI-------GEAFGGKVVRAPEPmhgK----TSPITHDG----------SGLFAGL-- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189 140 KSDFYFV--HSYYVE------CLESveTSFCEY---------EKPfcasfekdnIFAVQFHPE--KSQNvGLKLLENFAN 200
Cdd:COG0512   118 PNPFTATryHSLVVDretlpdELEV--TAWTEDgeimgirhrELP---------IEGVQFHPEsiLTEH-GHQLLANFLE 185


                  .
gi 1595861189 201 L 201
Cdd:COG0512   186 L 186
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 2-99 8.75e-08

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: 50.32  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   2 ICIVDY-HLGNFkSVLKAFEKLNQ-EVIISSKKEDIKNASKLVLPGVGSFKQGMENLKKLALDELLKECVlKDKKPILGI 79
Cdd:cd01750     1 IAVIRYpDISNF-TDLDPLAREPGvDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYA-RAGGPVLGI 78

                          90       100
                  ....*....|....*....|....*.
gi 1595861189  80 CLGMQLFASK-----GYEG-GECEGL 99
Cdd:cd01750    79 CGGYQMLGKYivdpeGVEGpGEIEGL 104
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 10-185 2.29e-07

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: 48.68  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  10 GNFKSVLKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGmENLKKLALDELLKEcVLKDKKPILGICLGMQLFASK 89
Cdd:cd01749     8 GDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIG-KLLRRTGLLDPLRE-FIRAGKPVFGTCAGLILLAKE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  90 GYEGGECEGLDFIKAKVLKfdLSKEKLLHSGWDDLQFSDKKSKLFDGIleksdfyFVHSYYVECLESVETSFCEYEKPFC 169
Cdd:cd01749    86 VEDQGGQPLLGLLDITVRR--NAFGRQVDSFEADLDIPGLGLGPFPAV-------FIRAPVIEEVGPGVEVLAEYDGKIV 156

                         170
                  ....*....|....*.
gi 1595861189 170 ASfEKDNIFAVQFHPE 185
Cdd:cd01749   157 AV-RQGNVLATSFHPE 171
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-202 3.69e-07

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 49.71  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   1 MICIVDyhlgNFKS----VLKAFEKLNQEVI-------ISSKKEDIKNASKLVL-PGVGSFKQG---MENLKKLAldell 65
Cdd:PRK14607    1 MIILID----NYDSftynIYQYIGELGPEEIevvrndeITIEEIEALNPSHIVIsPGPGRPEEAgisVEVIRHFS----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  66 kecvlkDKKPILGICLGMQLFaskgyegGECEGLDFIKAKVLKFDLSkEKLLHSGWDdlqfsdkkskLFDGILEKSDFYF 145
Cdd:PRK14607   72 ------GKVPILGVCLGHQAI-------GYAFGGKIVHAKRILHGKT-SPIDHNGKG----------LFRGIPNPTVATR 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595861189 146 VHSYYV------ECLESveTSFCEYEKPFCASFEKDNIFAVQFHPEK-SQNVGLKLLENFANLK 202
Cdd:PRK14607  128 YHSLVVeeaslpECLEV--TAKSDDGEIMGIRHKEHPIFGVQFHPESiLTEEGKRILKNFLNYQ 189
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 4-201 6.54e-06

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 44.74  E-value: 6.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189   4 IVDY--HLG-------NFKSVLKAFEKLNQEVIISSkkediknasklvlPGVGSFKQ-G-MEnlkklaldELLKEcvLKD 72
Cdd:PRK05670   15 LVQYlgELGaevvvyrNDEITLEEIEALNPDAIVLS-------------PGPGTPAEaGiSL--------ELIRE--FAG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  73 KKPILGICLGMQLFaskgyegGECEGLDFIKAKvlkfdlskeKLLHsGWDDLQFSDKKSkLFDGIleKSDF----YfvHS 148
Cdd:PRK05670   72 KVPILGVCLGHQAI-------GEAFGGKVVRAK---------EIMH-GKTSPIEHDGSG-IFAGL--PNPFtvtrY--HS 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595861189 149 YYV------ECLESveTSFCEYEKPFCASFEKDNIFAVQFHPEkS--QNVGLKLLENFANL 201
Cdd:PRK05670  130 LVVdreslpDCLEV--TAWTDDGEIMGVRHKELPIYGVQFHPE-SilTEHGHKLLENFLEL 187
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 17-89 1.86e-04

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 40.64  E-value: 1.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595861189  17 KAFEKLNQ--EVIISSKKEDIKNASKLVLPGVGSFKQGMEnLKKLALDELLKECVlKDKKPILGICLGMQLFASK 89
Cdd:PRK13527   21 RALDELGIdgEVVEVRRPGDLPDCDALIIPGGESTTIGRL-MKREGILDEIKEKI-EEGLPILGTCAGLILLAKE 93
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
63-87 2.09e-04

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 41.21  E-value: 2.09e-04
                          10        20
                  ....*....|....*....|....*
gi 1595861189  63 ELLKEcVLKDKKPILGICLGMQLFA 87
Cdd:PRK12564  239 EMIRE-LLEKKIPIFGICLGHQLLA 262
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 63-87 3.12e-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: 40.77  E-value: 3.12e-04
                          10        20
                  ....*....|....*....|....*
gi 1595861189  63 ELLKEcVLKDKKPILGICLGMQLFA 87
Cdd:COG0505   238 ETIRE-LLGKGIPIFGICLGHQLLA 261
PRK00758 PRK00758
GMP synthase subunit A; Validated
 66-199 3.63e-04

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 39.84  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  66 KECVLKDKKPILGICLGMQLFAsKGYeGGECEgldfiKAKVLKFDLSKEKLLHSgwDDlqfsdkkskLFDGILEKSDFYF 145
Cdd:PRK00758   60 PEYLKELDVPILGICLGHQLIA-KAF-GGEVG-----RGEYGEYALVEVEILDE--DD---------ILKGLPPEIRVWA 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189 146 VHSYYV----ECLESVETS-FCEYEkpfCASFEKDNIFAVQFHPEKSQNV-GLKLLENFA 199
Cdd:PRK00758  122 SHADEVkelpDGFEILARSdICEVE---AMKHKEKPIYGVQFHPEVAHTEyGEEIFKNFL 178
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 73-201 7.32e-04

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 39.00  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  73 KKPILGICLGMQLFaskgyegGECEGLDFIKAkvlkfdlskEKLLHSGWDDLQFSDKksKLFDGILE--KSDFYfvHSYY 150
Cdd:TIGR00566  72 KLPILGVCLGHQAM-------GQAFGGDVVRA---------NTVMHGKTSEIEHNGA--GIFRGLFNplTATRY--HSLV 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595861189 151 VEClESVETSFceyekPFCASFEKDN-----------IFAVQFHPEK--SQNvGLKLLENFANL 201
Cdd:TIGR00566 132 VEP-ETLPTCF-----PVTAWEEENIeimairhrdlpLEGVQFHPESilSEQ-GHQLLANFLHR 188
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 13-85 1.02e-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: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  13 KSVLKAFE--------KLNQEVIISSKKEDIKNASKL-------VLPGVGSFkqGMENlKKLALdellKECvLKDKKPIL 77
Cdd:cd01746    17 LSVLEALKhagialgvKLEIKWIDSEDLEEENAEEALkgadgilVPGGFGIR--GVEG-KILAI----KYA-RENNIPFL 88


                  ....*...
gi 1595861189  78 GICLGMQL 85
Cdd:cd01746    89 GICLGMQL 96
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 63-85 1.08e-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: 38.61  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|...
gi 1595861189  63 ELLKECvLKDKKPILGICLGMQL 85
Cdd:COG2071    87 ALIRAA-LERGKPVLGICRGMQL 108
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
16-106 1.67e-03

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 37.83  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595861189  16 LKAFEKLNQEVIISSKKEDIKNASKLVLPGVGSFKQGMEnLKKLALDELLKECVlKDKKPILGICLGMQLFAsKGYEGGE 95
Cdd:PRK13525   17 LAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKL-LRDFGLLEPLREFI-ASGLPVFGTCAGMILLA-KEIEGYE 93

                          90
                  ....*....|.
gi 1595861189  96 CEGLDFIKAKV 106
Cdd:PRK13525   94 QEHLGLLDITV 104
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 60-87 2.96e-03

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: 37.09  E-value: 2.96e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1595861189  60 ALDELLKEC--VLKDKKPILGICLGMQLFA 87
Cdd:cd01744    54 LLDEAIKTVrkLLGKKIPIFGICLGHQLLA 83
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-85 6.31e-03

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: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 36.01  E-value: 6.31e-03
                          10        20
                  ....*....|....*....|...
gi 1595861189  63 ELLKECvLKDKKPILGICLGMQL 85
Cdd:cd01745    91 ALLRAA-LERGKPILGICRGMQL 112
 
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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