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Conserved domains on  [gi|446610905|ref|WP_000688251|]
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aminodeoxychorismate/anthranilate synthase component II [Helicobacter pylori]

Protein Classification

aminodeoxychorismate/anthranilate synthase component II( domain architecture ID 10792604)

aminodeoxychorismate/anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA), and anthranilate, an intermediate in the biosynthesis of L-tryptophan, respectively

CATH:  3.40.50.880
EC:  4.1.3.27
Gene Ontology:  GO:0000162|GO:0046820|GO:0004049
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 2-191 6.17e-87

anthranilate synthase component II; Provisional


:

Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 253.90  E-value: 6.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   2 KIFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMglmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPIL 81
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEI----EALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE-HDNIPMAII 158
Cdd:PRK05670  77 GVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAWtDDGEIMGVR 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446610905 159 NEEDKILAYQFHPESIMTLQGRALLEQSVGFLR 191
Cdd:PRK05670 157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 2-191 6.17e-87

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 253.90  E-value: 6.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   2 KIFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMglmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPIL 81
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEI----EALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE-HDNIPMAII 158
Cdd:PRK05670  77 GVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAWtDDGEIMGVR 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446610905 159 NEEDKILAYQFHPESIMTLQGRALLEQSVGFLR 191
Cdd:PRK05670 157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 3-191 1.57e-79

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: 234.93  E-value: 1.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQND-IDPSYLmglmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPIL 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDeITLEEI-----EALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMAS--GLPKNLEVIAE-HDNIPMAII 158
Cdd:COG0512   76 GVCLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDreTLPDELEVTAWtEDGEIMGIR 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446610905 159 NEEDKILAYQFHPESIMTLQGRALLEQsvgFLR 191
Cdd:COG0512  156 HRELPIEGVQFHPESILTEHGHQLLAN---FLE 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 3-187 1.85e-73

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: 219.33  E-value: 1.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMGLMNEEsktpLLFISPGPGNPSSSGNLLKIIAMAKKKFPILG 82
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPD----AIVISPGPGHPEDAGISLEIIRALAGKVPILG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  83 VCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMAS--GLPKNLEVIA-EHDNIPMAIIN 159
Cdd:cd01743   77 VCLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDpdPLPDLLEVTAsTEDGVIMALRH 156

                        170       180
                 ....*....|....*....|....*...
gi 446610905 160 EEDKILAYQFHPESIMTLQGRALLEQSV 187
Cdd:cd01743  157 RDLPIYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
6-187 1.13e-53

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 169.34  E-value: 1.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905    6 IDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMglmneESKTPLLFISPGPGNPSSSGNLLKIIAMA-KKKFPILGVC 84
Cdd:pfam00117   3 IDNGDSFTYNLARALRELGVEVTVVPNDTPAEEIL-----EENPDGIILSGGPGSPGAAGGAIEAIREArELKIPILGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   85 LGLQALAQSYGAKIIRSKEIV-HGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAEHDNI--PMAIIN 159
Cdd:pfam00117  78 LGHQLLALAFGGKVVKAKKFGhHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVdpDTLPDGLEVTATSENDgtIMGIRH 157

                         170       180
                  ....*....|....*....|....*...
gi 446610905  160 EEDKILAYQFHPESIMTLQGRALLEQSV 187
Cdd:pfam00117 158 KKLPIFGVQFHPESILTPHGPEILFNFF 185
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-183 1.36e-46

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: 151.48  E-value: 1.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905    3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDidPSYLMGLmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPILG 82
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRND--SLTLQEI--EALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   83 VCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLM--ASGLPKNLEVIA--EHDNIPMAII 158
Cdd:TIGR00566  78 VCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVvePETLPTCFPVTAweEENIEIMAIR 157

                         170       180
                  ....*....|....*....|....*
gi 446610905  159 NEEDKILAYQFHPESIMTLQGRALL 183
Cdd:TIGR00566 158 HRDLPLEGVQFHPESILSEQGHQLL 182
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-193 4.49e-40

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 134.77  E-value: 4.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   5 FIDNFDSFSYNLV-YELECLGY-EVAVYQN--------DIDPSYLMglmneesktpllfISPGPGNPSSS---GNLLKII 71
Cdd:NF041322   1 FVDNFDSFTYNLVeYVSEQREHaETTVLKNtaslaevrAVDPDAIV-------------ISPGPGHPKNDrdvGVTADVL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  72 AMAKKKFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIA--E 149
Cdd:NF041322  68 RELSPEVPTLGVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCFEVTAttD 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446610905 150 HD--NIPMAIINEEDKILAYQFHPESIMTLQGRALLEQsvgFLRGL 193
Cdd:NF041322 148 HDgeELVMGIRHREHPIECVQFHPESVLTGVGHDVIEN---FLAAA 190
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 2-191 6.17e-87

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 253.90  E-value: 6.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   2 KIFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMglmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPIL 81
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEI----EALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE-HDNIPMAII 158
Cdd:PRK05670  77 GVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAWtDDGEIMGVR 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446610905 159 NEEDKILAYQFHPESIMTLQGRALLEQSVGFLR 191
Cdd:PRK05670 157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 3-191 1.57e-79

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: 234.93  E-value: 1.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQND-IDPSYLmglmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPIL 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDeITLEEI-----EALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMAS--GLPKNLEVIAE-HDNIPMAII 158
Cdd:COG0512   76 GVCLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDreTLPDELEVTAWtEDGEIMGIR 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446610905 159 NEEDKILAYQFHPESIMTLQGRALLEQsvgFLR 191
Cdd:COG0512  156 HRELPIEGVQFHPESILTEHGHQLLAN---FLE 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 3-187 1.85e-73

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: 219.33  E-value: 1.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMGLMNEEsktpLLFISPGPGNPSSSGNLLKIIAMAKKKFPILG 82
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPD----AIVISPGPGHPEDAGISLEIIRALAGKVPILG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  83 VCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMAS--GLPKNLEVIA-EHDNIPMAIIN 159
Cdd:cd01743   77 VCLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDpdPLPDLLEVTAsTEDGVIMALRH 156

                        170       180
                 ....*....|....*....|....*...
gi 446610905 160 EEDKILAYQFHPESIMTLQGRALLEQSV 187
Cdd:cd01743  157 RDLPIYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
6-187 1.13e-53

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 169.34  E-value: 1.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905    6 IDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMglmneESKTPLLFISPGPGNPSSSGNLLKIIAMA-KKKFPILGVC 84
Cdd:pfam00117   3 IDNGDSFTYNLARALRELGVEVTVVPNDTPAEEIL-----EENPDGIILSGGPGSPGAAGGAIEAIREArELKIPILGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   85 LGLQALAQSYGAKIIRSKEIV-HGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAEHDNI--PMAIIN 159
Cdd:pfam00117  78 LGHQLLALAFGGKVVKAKKFGhHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVdpDTLPDGLEVTATSENDgtIMGIRH 157

                         170       180
                  ....*....|....*....|....*...
gi 446610905  160 EEDKILAYQFHPESIMTLQGRALLEQSV 187
Cdd:pfam00117 158 KKLPIFGVQFHPESILTPHGPEILFNFF 185
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 3-189 5.23e-53

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 177.14  E-value: 5.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMGLMnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPILG 82
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERL-ATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  83 VCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMAIINEED 162
Cdd:PRK09522  83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHDAD 162

                        170       180
                 ....*....|....*....|....*..
gi 446610905 163 KILAYQFHPESIMTLQGRALLEQSVGF 189
Cdd:PRK09522 163 RVCGFQFHPESILTTQGARLLEQTLAW 189
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-183 1.36e-46

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: 151.48  E-value: 1.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905    3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDidPSYLMGLmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPILG 82
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRND--SLTLQEI--EALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   83 VCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLM--ASGLPKNLEVIA--EHDNIPMAII 158
Cdd:TIGR00566  78 VCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVvePETLPTCFPVTAweEENIEIMAIR 157

                         170       180
                  ....*....|....*....|....*
gi 446610905  159 NEEDKILAYQFHPESIMTLQGRALL 183
Cdd:TIGR00566 158 HRDLPLEGVQFHPESILSEQGHQLL 182
PRK13566 PRK13566
anthranilate synthase component I;
1-181 2.03e-46

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 162.01  E-value: 2.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   1 MKIFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLmglmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPI 80
Cdd:PRK13566 527 KRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAEEML-----DRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPI 601

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  81 LGVCLGLQALAQSYGAKIIRSKEIVHGKATTIA-LKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE-HDNIPMA 156
Cdd:PRK13566 602 FGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFAdpETLPDELLVTAEtEDGVIMA 681

                        170       180
                 ....*....|....*....|....*
gi 446610905 157 IINEEDKILAYQFHPESIMTLQGRA 181
Cdd:PRK13566 682 IEHKTLPVAAVQFHPESIMTLGGDV 706
trpG CHL00101
anthranilate synthase component 2
 3-183 7.66e-46

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 149.50  E-value: 7.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQND-IDPSYLMGLmNEESktplLFISPGPGNPSSSGNLLKIIAMAKKKFPIL 81
Cdd:CHL00101   2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDeIDLSKIKNL-NIRH----IIISPGPGHPRDSGISLDVISSYAPYIPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIA-EHDNIPMAII 158
Cdd:CHL00101  77 GVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIdpLNLPSPLEITAwTEDGLIMACR 156

                        170       180
                 ....*....|....*....|....*.
gi 446610905 159 NEEDKIL-AYQFHPESIMTLQGRALL 183
Cdd:CHL00101 157 HKKYKMLrGIQFHPESLLTTHGQQIL 182
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
3-191 2.30e-44

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 145.77  E-value: 2.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLvYELEC-LGYEVAVYQNDidpsyLMGLMNEESKTPL-LFISPGPGNPSSSGNLLKIIAMAKKKFPI 80
Cdd:PRK06774   2 LLLIDNYDSFTYNL-YQYFCeLGTEVMVKRND-----ELQLTDIEQLAPShLVISPGPCTPNEAGISLAVIRHFADKLPI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  81 LGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLM--ASGLPKNLEVIA--EHDNIP-- 154
Cdd:PRK06774  76 LGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLViaADSLPGCFELTAwsERGGEMde 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446610905 155 -MAIINEEDKILAYQFHPESIMTLQGRALLEQsvgFLR 191
Cdd:PRK06774 156 iMGIRHRTLPLEGVQFHPESILSEQGHQLLDN---FLK 190
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
2-183 1.39e-43

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 152.18  E-value: 1.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   2 KIFFIDNFDSFSYNLVYELECLGYE-VAVYQND---------IDPSYLMglmneesktpllfISPGPGNPSSSGNLLKII 71
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDeitieeieaLNPSHIV-------------ISPGPGRPEEAGISVEVI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  72 AMAKKKFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLM--ASGLPKNLEVIAE 149
Cdd:PRK14607  68 RHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVveEASLPECLEVTAK 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446610905 150 -HDNIPMAIINEEDKILAYQFHPESIMTLQGRALL 183
Cdd:PRK14607 148 sDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRIL 182
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
1-183 9.26e-42

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 139.80  E-value: 9.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   1 MKIFFIDNFDSFSYNLVYELECLGYEVAVYQNDiDPSylmglMNEESKTPLLF----ISPGPGNPSSSGNLLKII-AMAK 75
Cdd:PRK07765   1 MRILVVDNYDSFVFNLVQYLGQLGVEAEVWRND-DPR-----LADEAAVAAQFdgvlLSPGPGTPERAGASIDMVrACAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  76 KKFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE-HDN 152
Cdd:PRK07765  75 AGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTIlpETLPAELEVTARtDSG 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446610905 153 IPMAIINEEDKILAYQFHPESIMTLQGRALL 183
Cdd:PRK07765 155 VIMAVRHRELPIHGVQFHPESVLTEGGHRML 185
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
3-183 1.08e-41

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 138.86  E-value: 1.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLvYELEC-LGYEVAVYQND-IDpsyLMGLmneESKTPL-LFISPGPGNPSSSGNLLKIIAMAKKKFP 79
Cdd:PRK08857   2 LLMIDNYDSFTYNL-YQYFCeLGAQVKVVRNDeID---IDGI---EALNPThLVISPGPCTPNEAGISLQAIEHFAGKLP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  80 ILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLM--ASGLPKNLEVIA-------EH 150
Cdd:PRK08857  75 ILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVvkNDTLPECFELTAwteledgSM 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446610905 151 DNIpMAIINEEDKILAYQFHPESIMTLQGRALL 183
Cdd:PRK08857 155 DEI-MGFQHKTLPIEAVQFHPESIKTEQGHQLL 186
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
3-184 1.44e-41

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 138.51  E-value: 1.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLvYELEC-LGYEVAVYQNDIdpsylMGLMNEESKTPL-LFISPGPGNPSSSGNLLKIIAMAKKKFPI 80
Cdd:PRK08007   2 ILLIDNYDSFTWNL-YQYFCeLGADVLVKRNDA-----LTLADIDALKPQkIVISPGPCTPDEAGISLDVIRHYAGRLPI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  81 LGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAEHDNIP-MAI 157
Cdd:PRK08007  76 LGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVepDSLPACFEVTAWSETREiMGI 155

                        170       180
                 ....*....|....*....|....*..
gi 446610905 158 INEEDKILAYQFHPESIMTLQGRALLE 184
Cdd:PRK08007 156 RHRQWDLEGVQFHPESILSEQGHQLLA 182
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
3-185 1.78e-41

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 138.40  E-value: 1.78e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQND-IDPSYLmglmnEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPIL 81
Cdd:PRK07649   2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDeVTISDI-----ENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLM--ASGLPKNLEVIA--EHDNIpMAI 157
Cdd:PRK07649  77 GVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIvkKETLPDCLEVTSwtEEGEI-MAI 155

                        170       180
                 ....*....|....*....|....*...
gi 446610905 158 INEEDKILAYQFHPESIMTLQGRALLEQ 185
Cdd:PRK07649 156 RHKTLPIEGVQFHPESIMTSHGKELLQN 183
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-193 4.49e-40

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 134.77  E-value: 4.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   5 FIDNFDSFSYNLV-YELECLGY-EVAVYQN--------DIDPSYLMglmneesktpllfISPGPGNPSSS---GNLLKII 71
Cdd:NF041322   1 FVDNFDSFTYNLVeYVSEQREHaETTVLKNtaslaevrAVDPDAIV-------------ISPGPGHPKNDrdvGVTADVL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  72 AMAKKKFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIA--E 149
Cdd:NF041322  68 RELSPEVPTLGVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCFEVTAttD 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446610905 150 HD--NIPMAIINEEDKILAYQFHPESIMTLQGRALLEQsvgFLRGL 193
Cdd:NF041322 148 HDgeELVMGIRHREHPIECVQFHPESVLTGVGHDVIEN---FLAAA 190
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 3-187 3.31e-35

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 123.03  E-value: 3.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMGLmneesKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPILG 82
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILAA-----NPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  83 VCLGLQALAQSYGAKiIRSKEIVHGKATTIALK----KHAVFKGL------------GESMVVGRYHSLMASGLPKNLEV 146
Cdd:PRK05637  79 ICLGFQALLEHHGGK-VEPCGPVHGTTDNMILTdagvQSPVFAGLatdvepdhpeipGRKVPIARYHSLGCVVAPDGMES 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446610905 147 IAEHDN----IPMAIINEEDKILAYQFHPESIMTLQGRALLEQSV 187
Cdd:PRK05637 158 LGTCSSeigpVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCV 202
PLN02335 PLN02335
anthranilate synthase
 3-190 2.78e-34

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 121.06  E-value: 2.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDidpsylmGLMNEE--SKTPL-LFISPGPGNPSSSGNLLKIIAMAKKKFP 79
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRND-------ELTVEElkRKNPRgVLISPGPGTPQDSGISLQTVLELGPLVP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  80 ILGVCLGLQALAQSYGAKIIRSKE-IVHGKATTIALKK---HAVFKGLGESMVVGRYHSLMAS--GLPKN-LEVIA-EHD 151
Cdd:PLN02335  94 LFGVCMGLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDEkgeEGLFSGLPNPFTAGRYHSLVIEkdTFPSDeLEVTAwTED 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446610905 152 NIPMAIINEEDK-ILAYQFHPESIMTLQGRALLEQSVGFL 190
Cdd:PLN02335 174 GLIMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKII 213
PRK06895 PRK06895
anthranilate synthase component II;
1-183 3.07e-26

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 99.04  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   1 MKIFFIDNFDSFSYNLVYELECLGYEVAVYQ-NDIDpsylmglMNEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFP 79
Cdd:PRK06895   2 TKLLIINNHDSFTFNLVDLIRKLGVPMQVVNvEDLD-------LDEVENFSHILISPGPDVPRAYPQLFAMLERYHQHKS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  80 ILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALK-KHAVFKGLGESMVVGRYHSLMAS--GLPKNLEVIAE-HDNIPM 155
Cdd:PRK06895  75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRsNSPLFDGLPEEFNIGLYHSWAVSeeNFPTPLEITAVcDENVVM 154

                        170       180
                 ....*....|....*....|....*...
gi 446610905 156 AIINEEDKILAYQFHPESIMTLQGRALL 183
Cdd:PRK06895 155 AMQHKTLPIYGVQFHPESYISEFGEQIL 182
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 1-183 3.41e-23

aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate.


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 96.13  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905    1 MKIFFIDNFDSFSYNLVYELEcLGYEVAVYQNDIDPSYLMGLMNEESktpLLF----ISPGPGNPSS---SGNLLKIIAM 73
Cdd:TIGR01823   6 LHVLFIDSYDSFTYNVVRLLE-QQTDISVHVTTVHSDTFQDQLLELL---PLFdaivVGPGPGNPNNaqdMGIISELWEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   74 AK-KKFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLgESMVVGRYHSLMASGLPKN---LEVIAE 149
Cdd:TIGR01823  82 ANlDEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLYANPEGIDtllPLCLTE 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446610905  150 --HDNIPMAIINEEDKILAYQFHPESIMTLQGRALL 183
Cdd:TIGR01823 161 deEGIILMSAQTKKKPWFGVQYHPESCCSELGSGKL 196
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 77-184 8.84e-20

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: 82.20  E-value: 8.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  77 KFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMA 156
Cdd:cd01742   70 GVPVLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVA 149

                         90       100
                 ....*....|....*....|....*....
gi 446610905 157 II-NEEDKILAYQFHPESIMTLQGRALLE 184
Cdd:cd01742  150 AIaNEEKKIYGVQFHPEVTHTEKGKEILK 178
guaA PRK00074
GMP synthase; Reviewed
 79-184 3.68e-19

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 84.33  E-value: 3.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  79 PILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMAII 158
Cdd:PRK00074  77 PVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAI 156

                         90       100
                 ....*....|....*....|....*..
gi 446610905 159 -NEEDKILAYQFHPESIMTLQGRALLE 184
Cdd:PRK00074 157 aNEERKFYGVQFHPEVTHTPQGKKLLE 183
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 6-184 7.22e-19

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 83.74  E-value: 7.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   6 IDNFDSFSYNLVYELECLG--YEVAVYQNDIDPSYLMGLMNEESKTPLLFISPGPGNPSSSGNL---LKIIaMAKKKFPI 80
Cdd:PLN02889  87 IDNYDSYTYNIYQELSIVNgvPPVVVRNDEWTWEEVYHYLYEEKAFDNIVISPGPGSPTCPADIgicLRLL-LECRDIPI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  81 LGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVF----KGLGESMVVGRYHSLM--ASGLPKNLEVIA------ 148
Cdd:PLN02889 166 LGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVidAESLPKELVPIAwtsssd 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905 149 ------------------------------------------EHDN------IPMAIINEEDKILAYQFHPESIMTLQGR 180
Cdd:PLN02889 246 tlsflesqksglvpdayesqigqsgssdpfssklkngtswpsSHSErmqngkILMGIMHSTRPHYGLQFHPESIATCYGR 325


                 ....
gi 446610905 181 ALLE 184
Cdd:PLN02889 326 QIFK 329
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 79-172 1.76e-18

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: 79.60  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  79 PILGVCLGLQALAQSYGAKIIRS--KEIvhGKATTIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMA 156
Cdd:COG0518   84 PVLGICYGAQLLAHALGGKVEPGpgREI--GWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQ 161

                         90
                 ....*....|....*.
gi 446610905 157 IINEEDKILAYQFHPE 172
Cdd:COG0518  162 AFRYGRRVYGVQFHPE 177
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 67-175 4.57e-16

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: 72.28  E-value: 4.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  67 LLKIIAMA-KKKFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIAL----KKHAVFKGLGESMVVGRYHSLMASGLP 141
Cdd:cd01741   70 LKELIRQAlAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLteagKADPLFAGLPDEFPVFHWHGDTVVELP 149

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446610905 142 KNLEVIAEHDNIPMAIINEEDKILAYQFHPESIM 175
Cdd:cd01741  150 PGAVLLASSEACPNQAFRYGDRALGLQFHPEERL 183
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 52-173 1.02e-14

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: 68.68  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  52 LFISPGPGNPSSSGNLLK-IIAMAKKKFPILGVCLGLQALAQSYGAKIIR-----------SKEIVHGKA--TTialKKH 117
Cdd:cd01744   43 IFLSNGPGDPALLDEAIKtVRKLLGKKIPIFGICLGHQLLALALGAKTYKmkfghrgsnhpVKDLITGRVyiTS---QNH 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905 118 --AVFkglgesmvvgryhslmASGLPKNLEV--IAEHDNIPMAIINEEDKILAYQFHPES 173
Cdd:cd01744  120 gyAVD----------------PDSLPGGLEVthVNLNDGTVEGIRHKDLPVFSVQFHPEA 163
PRK00758 PRK00758
GMP synthase subunit A; Validated
 2-184 2.79e-14

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 67.57  E-value: 2.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   2 KIFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLmglmneESKTPLLFISPGPgNPSSSGNLLKIIAmaKKKFPIL 81
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEI------KAFEDGLILSGGP-DIERAGNCPEYLK--ELDVPIL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  82 GVCLGLQALAQSYGAKIIRSKeivHGK--ATTIALKKHA-VFKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPM-AI 157
Cdd:PRK00758  72 GICLGHQLIAKAFGGEVGRGE---YGEyaLVEVEILDEDdILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVeAM 148

                        170       180
                 ....*....|....*....|....*..
gi 446610905 158 INEEDKILAYQFHPESIMTLQGRALLE 184
Cdd:PRK00758 149 KHKEKPIYGVQFHPEVAHTEYGEEIFK 175
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 80-172 1.81e-11

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 60.75  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  80 ILGVCLGLQALAQSYGAKIIRS--KEIVHGKAT-TIALKKHAVFKGLGESMVVGRYHSLMaSGLPKNLEVIAEHDNIPMA 156
Cdd:PRK08250  87 VIGVCLGAQLIGEALGAKYEHSpeKEIGYFPITlTEAGLKDPLLSHFGSTLTVGHWHNDM-PGLTDQAKVLATSEGCPRQ 165

                         90
                 ....*....|....*.
gi 446610905 157 IINEEDKILAYQFHPE 172
Cdd:PRK08250 166 IVQYSNLVYGFQCHME 181
PLN02347 PLN02347
GMP synthetase
 58-183 9.93e-10

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 57.00  E-value: 9.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  58 PGNPSSSGNLLKIIAmaKKKFPILGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHAVFKGLGESM--VVGRYHSL 135
Cdd:PLN02347  69 EGAPTVPEGFFDYCR--ERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGEtqTVWMSHGD 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446610905 136 MASGLPKNLEVIAEHDNIPM-AIINEEDKILAYQFHPESIMTLQGRALL 183
Cdd:PLN02347 147 EAVKLPEGFEVVAKSVQGAVvAIENRERRIYGLQYHPEVTHSPKGMETL 195
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 52-97 3.79e-08

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 52.24  E-value: 3.79e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446610905   52 LFISPGPGNPSSSGNLLKIIAMAKKKFPILGVCLGLQALAQSYGAK 97
Cdd:TIGR01368 217 IFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALAFGAK 262
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
52-98 2.37e-07

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 49.69  E-value: 2.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446610905  52 LFISPGPGNPSssgNLLKIIAMAKK----KFPILGVCLGLQALAQSYGAKI 98
Cdd:PRK12564 222 VFLSNGPGDPA---ALDYAIEMIREllekKIPIFGICLGHQLLALALGAKT 269
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 52-102 7.92e-07

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: 48.09  E-value: 7.92e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446610905  52 LFISPGPGNPSSSGNLLKII-AMAKKKFPILGVCLGLQALAQSYGAKIIRSK 102
Cdd:COG0505  221 VFLSNGPGDPAALDYAIETIrELLGKGIPIFGICLGHQLLALALGAKTYKLK 272
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-90 2.74e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 44.51  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMGLMneeSKTPLLFISPGPGNP----SSSGNLLKIIAMAKKKF 78
Cdd:cd01653    4 LLFPGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDL---DDYDGLILPGGPGTPddlaRDEALLALLREAAAAGK 80

                         90
                 ....*....|..
gi 446610905  79 PILGVCLGLQAL 90
Cdd:cd01653   81 PILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-90 3.74e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 43.73  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMGLMNEESktpLLFISPGPGNP----SSSGNLLKIIAMAKKKF 78
Cdd:cd03128    4 LLFGGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYD---GLILPGGPGTPddlaWDEALLALLREAAAAGK 80

                         90
                 ....*....|..
gi 446610905  79 PILGVCLGLQAL 90
Cdd:cd03128   81 PVLGICLGAQLL 92
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 52-172 7.46e-06

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 45.27  E-value: 7.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  52 LFISPGPGNPSSSGNLLKIIAMAKKKFPILGVCLGLQALAQSYGAKIIRSKEIVHG-KATTIALKKHAVF---------- 120
Cdd:PRK12838 212 IVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGaNHPVIDLTTGRVWmtsqnhgyvv 291

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446610905 121 --KGLGESMVVGRYHSLmasglpkNLEVIAehdnipmAIINEEDKILAYQFHPE 172
Cdd:PRK12838 292 deDSLDGTPLSVRFFNV-------NDGSIE-------GLRHKKKPVLSVQFHPE 331
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 63-192 7.61e-06

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: 44.62  E-value: 7.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   63 SSGNLLKIIAMAKKKfPILGVCLGLQALAQS------------YGAKIIRSKE--IVH-GKATTIALKKHAVFKGLGESM 127
Cdd:TIGR01855  58 NGLDLFVELVVRLGK-PVLGICLGMQLLFERseegggvpglglIKGNVVKLEArkVPHmGWNEVHPVKESPLLNGIDEGA 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446610905  128 VVGRYHSLMASglPKNLEVIAEHD---NIPMAIinEEDKILAYQFHPESIMTLqGRALLEQsvgFLRG 192
Cdd:TIGR01855 137 YFYFVHSYYAV--CEEEAVLAYADygeKFPAAV--QKGNIFGTQFHPEKSGKT-GLKLLEN---FLEL 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 70-172 1.07e-05

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: 44.03  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  70 IIAMAKKKFPILGVCLGLQALAQS------------YGAKIIR-----SKEIVH-GKATTIALKKHAVFKGLGEsmvvGR 131
Cdd:cd01748   64 LKEAIASGKPFLGICLGMQLLFESseegggtkglglIPGKVVRfpaseGLKVPHmGWNQLEITKESPLFKGIPD----GS 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446610905 132 Y----HSLMASglPKNLEVI---AEHDnIPMAIINEEDKILAYQFHPE 172
Cdd:cd01748  140 YfyfvHSYYAP--PDDPDYIlatTDYG-GKFPAAVEKDNIFGTQFHPE 184
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 2-173 1.30e-05

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 44.58  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   2 KIFFIDNFD-SFSYNLVYELECLGYEVAVYqndidPSYLMGLMNEESKTPLLFISPGPGNPSSSGNLLKIIAMAKKKFPI 80
Cdd:PLN02771 239 ESYHVIAYDfGIKHNILRRLASYGCKITVV-----PSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPV 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  81 LGVCLGLQALAQSYGAKIIRSKEIVHGKATTIALKKHavfkGLGESMVVGRYHSLMASGLPKNLEV--IAEHDNIPMAII 158
Cdd:PLN02771 314 FGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRT----GRVEISAQNHNYAVDPASLPEGVEVthVNLNDGSCAGLA 389

                        170
                 ....*....|....*
gi 446610905 159 NEEDKILAYQFHPES 173
Cdd:PLN02771 390 FPALNVMSLQYHPEA 404
PRK05665 PRK05665
amidotransferase; Provisional
 67-184 9.61e-05

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 41.72  E-value: 9.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  67 LLKIIAMAKKkfpILGVCLGLQALA-----------QSYGAKIIRSKEIVHGKATTIALKKHAVFKGlgesmvvgryHSL 135
Cdd:PRK05665  84 LLKLYERGDK---LLGVCFGHQLLAlllggkaerasQGWGVGIHRYQLAAHAPWMSPAVTELTLLIS----------HQD 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446610905 136 MASGLPKNLEVIAEHDNIPMAIINEEDKILAYQFHPESIMTLQgRALLE 184
Cdd:PRK05665 151 QVTALPEGATVIASSDFCPFAAYHIGDQVLCFQGHPEFVHDYS-RALLD 198
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 52-102 5.55e-04

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 39.78  E-value: 5.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446610905  52 LFISPGPGNPSSSGNLLKIIA-MAKKKFPILGVCLGLQALAQSYGAKIIRSK 102
Cdd:CHL00197 237 ILLSNGPGDPSAIHYGIKTVKkLLKYNIPIFGICMGHQILSLALEAKTFKLK 288
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 78-172 1.59e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 38.00  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  78 FPILGVCLGLQALAQSYGAKIIRSkeivHGK---ATTIALKKHA----VFKGLGESMV--VGryHSLMASGLPKNLEVIA 148
Cdd:PRK07567  94 FPFLGACYGVGTLGHHQGGVVDRT----YGEpvgAVTVSLTDAGradpLLAGLPDTFTafVG--HKEAVSALPPGAVLLA 167

                         90       100
                 ....*....|....*....|....
gi 446610905 149 EHDNIPMAIINEEDKILAYQFHPE 172
Cdd:PRK07567 168 TSPTCPVQMFRVGENVYATQFHPE 191
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 70-172 1.93e-03

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 37.62  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905   70 IIAMAKKKFPILGVCLGLQ--------ALAQSYGAKIIRSKEIVH------GKATTIALKKHAVFKGLG--ESMVVGRYH 133
Cdd:pfam07722  98 IRAALARGKPILGICRGFQllnvalggTLYQDIQEQPGFTDHREHcqvapyAPSHAVNVEPGSLLASLLgsEEFRVNSLH 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446610905  134 SLMASGLPKNLEVIA-EHDNIPMAI--INEEDKILAYQFHPE 172
Cdd:pfam07722 178 HQAIDRLAPGLRVEAvAPDGTIEAIesPNAKGFALGVQWHPE 219
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 56-172 9.09e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 35.61  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610905  56 PGPGNPSSSGNLL-----KIIAMAKKKFPILGVCLGLQALAQS-------YGAKIIRSK--------EIVH-GKATTIAL 114
Cdd:PRK13143  45 PGVGAFGAAMENLsplrdVILEAARSGKPFLGICLGMQLLFESseegggvRGLGLFPGRvvrfpagvKVPHmGWNTVKVV 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446610905 115 KKHAVFKGLGESMVvgrY--HSLMAsgLPKNLEVIAEHDN--IPMAIINEEDKILAYQFHPE 172
Cdd:PRK13143 125 KDCPLFEGIDGEYV---YfvHSYYA--YPDDEDYVVATTDygIEFPAAVCNDNVFGTQFHPE 181
 
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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