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Conserved domains on  [gi|2065533849|dbj|BCR04071|]
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glutamine amidotransferase [Desulfuromonas versatilis]

Protein Classification

aminodeoxychorismate/anthranilate synthase component II( domain architecture ID 11423509)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-188 1.70e-139

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: 386.32  E-value: 1.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHRELP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 162 LWGVQFHPESILTVEGKRLLQNFLEMT 188
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELA 187
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-188 1.70e-139

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: 386.32  E-value: 1.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHRELP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 162 LWGVQFHPESILTVEGKRLLQNFLEMT 188
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELA 187
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-188 3.52e-138

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 382.94  E-value: 3.52e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHREL 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*...
gi 2065533849 161 PLWGVQFHPESILTVEGKRLLQNFLEMT 188
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLELA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 1.27e-113

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: 320.64  E-value: 1.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHRELP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 2065533849 162 LWGVQFHPESILTVEGKRLLQNFL 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 1.23e-94

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: 273.20  E-value: 1.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGC-IMGLEHRE 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 160 LPLWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLH 187
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 1.39e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 227.12  E-value: 1.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   3 LMLDNYDSFTYNLVQYLQELGEEVEVHRNDkITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAG-QIPMLGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGEL-MHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGC-IMGLEHRE 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 2065533849 160 LPLWGVQFHPESILTVEGKRLLQNFL 185
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
6-187 1.28e-69

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 209.89  E-value: 1.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   6 DNYDSFTYNLVQYLQELGE--EVEVHRNdKITVEQIAARRPRRLVISPGPCSPA---EAGISVEVLQRLAGQIPMLGVCL 80
Cdd:NF041322    3 DNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVCL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVErpSLPECLRVSAWTEDGC---IMGLEH 157
Cdd:NF041322   82 GLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIRH 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 2065533849 158 RELPLWGVQFHPESILTVEGKRLLQNFLEM 187
Cdd:NF041322  160 REHPIECVQFHPESVLTGVGHDVIENFLAA 189
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-188 1.70e-139

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: 386.32  E-value: 1.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHRELP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 162 LWGVQFHPESILTVEGKRLLQNFLEMT 188
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELA 187
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-188 3.52e-138

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 382.94  E-value: 3.52e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHREL 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*...
gi 2065533849 161 PLWGVQFHPESILTVEGKRLLQNFLEMT 188
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLELA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 1.27e-113

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: 320.64  E-value: 1.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHRELP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 2065533849 162 LWGVQFHPESILTVEGKRLLQNFL 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-185 3.44e-110

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 324.75  E-value: 3.44e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELG-EEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVC 79
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGpEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  80 LGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHRE 159
Cdd:PRK14607   81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                         170       180
                  ....*....|....*....|....*.
gi 2065533849 160 LPLWGVQFHPESILTVEGKRLLQNFL 185
Cdd:PRK14607  161 HPIFGVQFHPESILTEEGKRILKNFL 186
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-186 1.80e-107

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 305.57  E-value: 1.80e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHREL 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                         170       180
                  ....*....|....*....|....*.
gi 2065533849 161 PLWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:PRK07649  161 PIEGVQFHPESIMTSHGKELLQNFIR 186
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-185 5.54e-97

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 279.11  E-value: 5.54e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:PRK08007    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHREL 160
Cdd:PRK08007   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                         170       180
                  ....*....|....*....|....*
gi 2065533849 161 PLWGVQFHPESILTVEGKRLLQNFL 185
Cdd:PRK08007  161 DLEGVQFHPESILSEQGHQLLANFL 185
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 1.23e-94

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: 273.20  E-value: 1.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGC-IMGLEHRE 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 160 LPLWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLH 187
trpG CHL00101
anthranilate synthase component 2
 1-186 2.82e-93

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 269.68  E-value: 2.82e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:CHL00101    1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHREL 160
Cdd:CHL00101   81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 161 P-LWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:CHL00101  161 KmLRGIQFHPESLLTTHGQQILRNFLS 187
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-188 8.46e-93

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 268.67  E-value: 8.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:PRK08857    1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTE--DGC---IMGL 155
Cdd:PRK08857   81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGSmdeIMGF 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2065533849 156 EHRELPLWGVQFHPESILTVEGKRLLQNFLEMT 188
Cdd:PRK08857  161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLART 193
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-186 1.79e-91

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 265.19  E-value: 1.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCL 80
Cdd:PRK06774    1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTE-DGC---IMGLE 156
Cdd:PRK06774   81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSErGGEmdeIMGIR 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2065533849 157 HRELPLWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:PRK06774  161 HRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-186 5.69e-88

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 256.90  E-value: 5.69e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITV--EQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAG-QIPMLGV 78
Cdd:PRK07765    3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLadEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  79 CLGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHR 158
Cdd:PRK07765   83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                         170       180
                  ....*....|....*....|....*...
gi 2065533849 159 ELPLWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:PRK07765  163 ELPIHGVQFHPESVLTEGGHRMLANWLT 190
PLN02335 PLN02335
anthranilate synthase
 2-187 6.67e-87

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 254.72  E-value: 6.67e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:PLN02335   21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGE-LMHGKTSPIFHD---GSGVFRGLSNPFVATRYHSLIVERPSLPE-CLRVSAWTEDGCIMGLE 156
Cdd:PLN02335  101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2065533849 157 HRELP-LWGVQFHPESILTVEGKRLLQNFLEM 187
Cdd:PLN02335  181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIKI 212
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 1.39e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 227.12  E-value: 1.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   3 LMLDNYDSFTYNLVQYLQELGEEVEVHRNDkITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAG-QIPMLGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGEL-MHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGC-IMGLEHRE 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 2065533849 160 LPLWGVQFHPESILTVEGKRLLQNFL 185
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
6-187 1.28e-69

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 209.89  E-value: 1.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   6 DNYDSFTYNLVQYLQELGE--EVEVHRNdKITVEQIAARRPRRLVISPGPCSPA---EAGISVEVLQRLAGQIPMLGVCL 80
Cdd:NF041322    3 DNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVCL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVErpSLPECLRVSAWTEDGC---IMGLEH 157
Cdd:NF041322   82 GLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIRH 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 2065533849 158 RELPLWGVQFHPESILTVEGKRLLQNFLEM 187
Cdd:NF041322  160 REHPIECVQFHPESVLTGVGHDVIENFLAA 189
PRK13566 PRK13566
anthranilate synthase component I;
2-187 5.25e-56

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 187.82  E-value: 5.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKiTVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:PRK13566  529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGF-AEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLG 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGELMHGKTSPIF-HDGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHREL 160
Cdd:PRK13566  608 LQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKTL 687

                         170       180       190
                  ....*....|....*....|....*....|
gi 2065533849 161 PLWGVQFHPESILTVEGK---RLLQNFLEM 187
Cdd:PRK13566  688 PVAAVQFHPESIMTLGGDvglRIIENVVRL 717
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-185 5.65e-56

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 184.84  E-value: 5.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRND---KITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGV 78
Cdd:PRK09522    4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  79 CLGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIveRPSLPECLRVSAwTEDGCIMGLEHR 158
Cdd:PRK09522   84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 159 ELPLWGVQFHPESILTVEGKRLLQNFL 185
Cdd:PRK09522  161 ADRVCGFQFHPESILTTQGARLLEQTL 187
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-186 2.87e-43

anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of anthranilate synthases from alpha proteobacteria and Nostoc (a cyanobacterium). This enzyme is the first step in the pathway for the biosynthesis of tryprophan from chorismate. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130874 [Multi-domain]  Cd Length: 717  Bit Score: 152.73  E-value: 2.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNdKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRH-SHAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGV-FRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHREL 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRVLGPDAlFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180
                  ....*....|....*....|....*....
gi 2065533849 161 PLWGVQFHPESILTVEGK---RLLQNFLE 186
Cdd:TIGR01815 678 PLAAVQFHPESIMTLDGGaglAMIGNVVD 706
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-188 1.42e-41

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 148.84  E-value: 1.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   3 LMLDNYDSFTYNLVQYLQEL-GEEVEVHRNDKITVEQI-----AARRPRRLVISPGPCSP---AEAGISVEVLqRLAGQI 73
Cdd:PLN02889   85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLL-LECRDI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  74 PMLGVCLGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVF----RGLSNPFVATRYHSLIVERPSLPECLRVSAWT-- 147
Cdd:PLN02889  164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKELVPIAWTss 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849 148 --------------------------------------------------EDGCI-MGLEHRELPLWGVQFHPESILTVE 176
Cdd:PLN02889  244 sdtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermQNGKIlMGIMHSTRPHYGLQFHPESIATCY 323

                         250
                  ....*....|..
gi 2065533849 177 GKRLLQNFLEMT 188
Cdd:PLN02889  324 GRQIFKNFREIT 335
PRK06895 PRK06895
anthranilate synthase component II;
1-186 2.94e-41

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 137.56  E-value: 2.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVhrndkITVEQI---AARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLG 77
Cdd:PRK06895    3 KLLIINNHDSFTFNLVDLIRKLGVPMQV-----VNVEDLdldEVENFSHILISPGPDVPRAYPQLFAMLERYHQHKSILG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  78 VCLGHQAIGHAFGGRVIRAGELMHGKTSPIFH-DGSGVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLE 156
Cdd:PRK06895   78 VCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVrSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQ 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 2065533849 157 HRELPLWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:PRK06895  158 HKTLPIYGVQFHPESYISEFGEQILRNWLA 187
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-185 3.05e-33

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: 116.87  E-value: 3.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   3 LMLDNYDSFTYNLVQYLQELGEEVEVHRNDkITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLGH 82
Cdd:cd01742     2 LILDFGSQYTHLIARRVRELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  83 QAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERpsLPECLRVSAWTEDGCIMGLEHRELPL 162
Cdd:cd01742    81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDNCPVAAIANEEKKI 158

                         170       180
                  ....*....|....*....|...
gi 2065533849 163 WGVQFHPESILTVEGKRLLQNFL 185
Cdd:cd01742   159 YGVQFHPEVTHTEKGKEILKNFL 181
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-186 6.03e-33

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: 116.26  E-value: 6.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNDkITVEQIAARRPRRLVISPGPCSpAEAGISVEVLQRL--AGqIPMLGVC 79
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSS-VYAENAPRADEKIfeLG-VPVLGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  80 LGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERpsLPECLRVSAWTEDGCIMGLEHRE 159
Cdd:TIGR00888  78 YGMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDNCPVAAMAHEE 155

                         170       180
                  ....*....|....*....|....*..
gi 2065533849 160 LPLWGVQFHPESILTVEGKRLLQNFLE 186
Cdd:TIGR00888 156 KPIYGVQFHPEVTHTEYGNELLENFVY 182
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-182 1.18e-31

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 113.40  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHRNdKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLG 81
Cdd:PRK05637    4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  82 HQAIGHAFGGRViRAGELMHGKTSPIFHDGSG----VFRGLS------NP-FVAT-----RYHSL-IVERP----SLPEC 140
Cdd:PRK05637   83 FQALLEHHGGKV-EPCGPVHGTTDNMILTDAGvqspVFAGLAtdvepdHPeIPGRkvpiaRYHSLgCVVAPdgmeSLGTC 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2065533849 141 LrvsawTEDG-CIMGLEHRELPLWGVQFHPESILTVEGKRLLQ 182
Cdd:PRK05637  162 S-----SEIGpVIMAAETTDGKAIGLQFHPESVLSPTGPIILS 199
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-187 1.42e-29

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 107.25  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   1 MLLMLDNYDSFTYNLVQYLQELGEEVEVHRNDKiTVEQIAARrPRRLVISPGPcSPAEAGISVEVLQRLagQIPMLGVCL 80
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTT-PVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  81 GHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSliVERPSLPECLRVSAwTEDGC-IMGLEHRE 159
Cdd:PRK00758   76 GHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHA--DEVKELPDGFEILA-RSDICeVEAMKHKE 152

                         170       180
                  ....*....|....*....|....*...
gi 2065533849 160 LPLWGVQFHPESILTVEGKRLLQNFLEM 187
Cdd:PRK00758  153 KPIYGVQFHPEVAHTEYGEEIFKNFLEI 180
guaA PRK00074
GMP synthase; Reviewed
 17-185 4.78e-27

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 106.28  E-value: 4.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  17 QYLQ-------ELGEEVEVHRNDkITVEQIAARRPRRLVISPGPCSPAEAG---ISVEVLQrlAGqIPMLGVCLGHQAIG 86
Cdd:PRK00074   14 QYTQliarrvrELGVYSEIVPYD-ISAEEIRAFNPKGIILSGGPASVYEEGaprADPEIFE--LG-VPVLGICYGMQLMA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  87 HAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNPFVATRYHSLIVERpsLPECLRVSAWTEDGCIMGLEHRELPLWGVQ 166
Cdd:PRK00074   90 HQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFKVIASTENCPIAAIANEERKFYGVQ 167

                         170
                  ....*....|....*....
gi 2065533849 167 FHPESILTVEGKRLLQNFL 185
Cdd:PRK00074  168 FHPEVTHTPQGKKLLENFV 186
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-187 2.63e-26

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: 104.99  E-value: 2.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELgEEVEVH----RNDKIT------VEQIAArrprrLVISPGPCSPAEA---GISVEVLQ- 67
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLEQQ-TDISVHvttvHSDTFQdqllelLPLFDA-----IVVGPGPGNPNNAqdmGIISELWEl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  68 RLAGQIPMLGVCLGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRGLSNpFVATRYHSLIVeRPSLPECLRVSAWT 147
Cdd:TIGR01823  82 ANLDEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYA-NPEGIDTLLPLCLT 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2065533849 148 EDG---CIMGLEHRELPLWGVQFHPESILTVEGK-RLLQNFLEM 187
Cdd:TIGR01823 160 EDEegiILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKL 203
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 1.10e-24

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: 94.49  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  13 YNLVQYLQELGEEVEVHRNDKiTVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQ-IPMLGVCLGHQAIGHAFGG 91
Cdd:cd01744    10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  92 RVIRageLMHGktspifHdgsgvfRGLSNP---------FVATRYHSLIVERPSLPECLRVSAWT-EDGCIMGLEHRELP 161
Cdd:cd01744    89 KTYK---MKFG------H------RGSNHPvkdlitgrvYITSQNHGYAVDPDSLPGGLEVTHVNlNDGTVEGIRHKDLP 153

                         170
                  ....*....|
gi 2065533849 162 LWGVQFHPES 171
Cdd:cd01744   154 VFSVQFHPEA 163
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-170 3.20e-23

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: 91.93  E-value: 3.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   2 LLMLDNYDSFTYNLVQYLQELGEEVEVHR--NDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRL-----AGQIP 74
Cdd:COG0518     5 LDHDPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALireafELGKP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  75 MLGVCLGHQAIGHAFGGRVIRAGELMHGKTsPI-FHDGSGVFRGLSNPFVATRYHSLIVERpsLPECLRVSAWTEDGCIM 153
Cdd:COG0518    85 VLGICYGAQLLAHALGGKVEPGPGREIGWA-PVeLTEADPLFAGLPDEFTVWMSHGDTVTE--LPEGAEVLASSDNCPNQ 161

                         170
                  ....*....|....*..
gi 2065533849 154 GLEHRElPLWGVQFHPE 170
Cdd:COG0518   162 AFRYGR-RVYGVQFHPE 177
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 13-171 1.74e-19

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: 84.30  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  13 YNLVQYLQELGEEVEVHRNDkITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQ-IPMLGVCLGHQAIGHAFGG 91
Cdd:COG0505   188 RNILRELAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  92 RVIRageLMHGktspifHdgsgvfRGLSNP---------FVATRYHSLIVERPSLPE-CLRVsawTE----DGCIMGLEH 157
Cdd:COG0505   267 KTYK---LKFG------H------RGANHPvkdletgrvEITSQNHGFAVDEDSLPAtDLEV---THvnlnDGTVEGLRH 328

                         170
                  ....*....|....
gi 2065533849 158 RELPLWGVQFHPES 171
Cdd:COG0505   329 KDLPAFSVQYHPEA 342
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
35-171 6.78e-19

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 82.43  E-value: 6.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  35 TVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQ-IPMLGVCLGHQAIGHAFGGRVIRageLMHGktspifHdgsg 113
Cdd:PRK12564  210 TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKkIPIFGICLGHQLLALALGAKTYK---MKFG------H---- 276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065533849 114 vfRGLSNP---------FVATRYHSLIVERPSLPECLRVSAW-TEDGCIMGLEHRELPLWGVQFHPES 171
Cdd:PRK12564  277 --RGANHPvkdletgkvEITSQNHGFAVDEDSLPANLEVTHVnLNDGTVEGLRHKDLPAFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 37-185 3.05e-17

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 78.57  E-value: 3.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  37 EQIAARRPRRLVISPGPCSPAEAG---ISVEVLQRLAGQ-IPMLGVCLGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGS 112
Cdd:PLN02347   47 DRIASLNPRVVILSGGPHSVHVEGaptVPEGFFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGS 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065533849 113 GVFRGLSNPFVATRYHSLIVERPSLPECLRVSAWTEDGCIMGLEHRELPLWGVQFHPESILTVEGKRLLQNFL 185
Cdd:PLN02347  127 QLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 43-171 1.26e-15

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 73.86  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  43 RPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLGHQAIGHAFGGRVIRAGELMHGKTSPIFHDGSGVFRglsnpf 122
Cdd:PLN02771  281 KPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVE------ 354

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065533849 123 VATRYHSLIVERPSLPECLRVSAWT-EDGCIMGLEHRELPLWGVQFHPES 171
Cdd:PLN02771  355 ISAQNHNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVMSLQYHPEA 404
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 35-170 2.82e-15

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 72.23  E-value: 2.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  35 TVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQIPMLGVCLGHQAIGHAFGGRVIRageLMHGktspifhdgsgv 114
Cdd:PRK12838  200 SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEK---LPFG------------ 264

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065533849 115 FRGLSNP---------FVATRYHSLIVERPSLPECLRVSAWTE--DGCIMGLEHRELPLWGVQFHPE 170
Cdd:PRK12838  265 HRGANHPvidlttgrvWMTSQNHGYVVDEDSLDGTPLSVRFFNvnDGSIEGLRHKKKPVLSVQFHPE 331
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-171 6.39e-15

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 71.75  E-value: 6.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  13 YNLVQYLQELGEEVEVhRNDKITVEQIAARRPRRLVISPGPCSPAEAGISVEVLQRLAGQ-IPMLGVCLGHQAIGHAFGG 91
Cdd:CHL00197  204 YNILRRLKSFGCSITV-VPATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYnIPIFGICMGHQILSLALEA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  92 RVIRageLMHGktspifHdgsgvfRGLSNPF-------VATRYHSLIVERPSLPE-CLRVSAWT-EDGCIMGLEHRELPL 162
Cdd:CHL00197  283 KTFK---LKFG------H------RGLNHPSglnqqveITSQNHGFAVNLESLAKnKFYITHFNlNDGTVAGISHSPKPY 347


                  ....*....
gi 2065533849 163 WGVQFHPES 171
Cdd:CHL00197  348 FSVQYHPEA 356
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 67-185 1.72e-12

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: 62.65  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  67 QRLAGQIPMLGVCLGHQAIGHAFGGRVIRAGE-----------LMHGKTSPIfhdgsgvFRGLSNPFVATRYHSLIVERp 135
Cdd:cd01741    76 QALAAGKPVLGICLGHQLLARALGGKVGRNPKgweigwfpvtlTEAGKADPL-------FAGLPDEFPVFHWHGDTVVE- 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065533849 136 sLPECLRVSAWTEDGCIMGLEHRELpLWGVQFHPEsiltvegKRLLQNFL 185
Cdd:cd01741   148 -LPPGAVLLASSEACPNQAFRYGDR-ALGLQFHPE-------ERLLRNFL 188
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 69-170 5.46e-10

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: 56.33  E-value: 5.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  69 LAGQIPMLGVCLGHQAIGHAFGGRVI------RAGELMHGKTSPIF---HD-----GSGVFR--GLSNPFVATrYHSLIV 132
Cdd:COG2071    93 LERGKPVLGICRGMQLLNVALGGTLYqdlpdqVPGALDHRQPAPRYaprHTveiepGSRLARilGEEEIRVNS-LHHQAV 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2065533849 133 ERpsLPECLRVSAWTEDGCIMGLEHRELP-LWGVQFHPE 170
Cdd:COG2071   172 KR--LGPGLRVSARAPDGVIEAIESPGAPfVLGVQWHPE 208
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-103 1.22e-09

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: 53.37  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   3 LMLDNYDSFT---YNLVQYLQELGEEVEVHRNDKITVE-QIAARRPRRLVISPGPCSPAEAGISVEVLQRL----AGQIP 74
Cdd:cd01653     2 AVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLARDEALLALLreaaAAGKP 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2065533849  75 MLGVCLGHQAI-----GHAFGGRVIRAGELMHGK 103
Cdd:cd01653    82 ILGICLGAQLLvlgvqFHPEAIDGAEAGARLLVN 115
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 73-170 1.23e-09

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: 55.34  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  73 IPMLGVCLGHQAIGHAFGGR--------VIRAGELMHGKTSPIF--HD-----GSGVFR--GLSNPFVATRYHSLIVErp 135
Cdd:pfam07722 106 KPILGICRGFQLLNVALGGTlyqdiqeqPGFTDHREHCQVAPYApsHAvnvepGSLLASllGSEEFRVNSLHHQAIDR-- 183

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2065533849 136 sLPECLRVSAWTEDGCIMGLEHRELP--LWGVQFHPE 170
Cdd:pfam07722 184 -LAPGLRVEAVAPDGTIEAIESPNAKgfALGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 69-170 2.06e-09

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: 54.50  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  69 LAGQIPMLGVCLGHQAIGHAFGGRVIRagELMhgktspifhdgsgvfrglsnpfvATRYHSLIVERpsLPECLRVSAWTE 148
Cdd:cd01745    97 LERGKPILGICRGMQLLNVALGGTLYQ--DIR-----------------------VNSLHHQAIKR--LADGLRVEARAP 149

                          90       100
                  ....*....|....*....|...
gi 2065533849 149 DGCIMGLEHRELPLW-GVQFHPE 170
Cdd:cd01745   150 DGVIEAIESPDRPFVlGVQWHPE 172
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 6.79e-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: 51.05  E-value: 6.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849   3 LMLDNYDSFT---YNLVQYLQELGEEVEVHRNDKITVE-QIAARRPRRLVISPGPCSPAEAGISVEVLQRL----AGQIP 74
Cdd:cd03128     2 AVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLAWDEALLALLreaaAAGKP 81

                          90
                  ....*....|.
gi 2065533849  75 MLGVCLGHQAI 85
Cdd:cd03128    82 VLGICLGAQLL 92
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 74-170 7.11e-08

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 50.73  E-value: 7.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  74 PMLGVCLGHQAIGHAFGGRVI-----RAGELMHGKTSPIFHDGSgVFRGLSNPFVATRYHSLIVERPslPECLRVSAWTE 148
Cdd:PRK09065   90 PLLGICYGHQLLAHALGGEVGynpagRESGTVTVELHPAAADDP-LFAGLPAQFPAHLTHLQSVLRL--PPGAVVLARSA 166

                          90       100
                  ....*....|....*....|...
gi 2065533849 149 -DGCIMgLEHRElPLWGVQFHPE 170
Cdd:PRK09065  167 qDPHQA-FRYGP-HAWGVQFHPE 187
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 19-187 2.02e-07

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: 48.86  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  19 LQELGEEVEVHRNDKItVEQIAArrprrlVISPGPCSPAEA-------GISVEVLQRLAGQIPMLGVCLGHQ-------- 83
Cdd:TIGR01855  18 LKRVGAEPVVVKDSKE-AELADK------LILPGVGAFGAAmarlrenGLDLFVELVVRLGKPVLGICLGMQllfersee 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  84 -----AIGHaFGGRVIRAgelmhgKTSPIFHDG---------SGVFRGLSNP----FVatryHSLIVErpslPECLRVSA 145
Cdd:TIGR01855  91 gggvpGLGL-IKGNVVKL------EARKVPHMGwnevhpvkeSPLLNGIDEGayfyFV----HSYYAV----CEEEAVLA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2065533849 146 WTEDG----CIMGLEHrelpLWGVQFHPESILTVeGKRLLQNFLEM 187
Cdd:TIGR01855 156 YADYGekfpAAVQKGN----IFGTQFHPEKSGKT-GLKLLENFLEL 196
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 63-188 7.90e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 44.35  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  63 VEVLQRLAGQ-IPMLGVCLGHQAI-------GHAFG-----GRVIRAGELMHGK------TSPIFHDGSGVFRGLSNP-- 121
Cdd:PRK13141   62 DEVIKEAVASgKPLLGICLGMQLLfesseefGETEGlgllpGRVRRFPPEEGLKvphmgwNQLELKKESPLLKGIPDGay 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065533849 122 --FVatryHSLIVErPSLPEclRVSAWTEDGcimglehRELP-------LWGVQFHPESILTVeGKRLLQNFLEMT 188
Cdd:PRK13141  142 vyFV----HSYYAD-PCDEE--YVAATTDYG-------VEFPaavgkdnVFGAQFHPEKSGDV-GLKILKNFVEMV 202
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 65-170 9.54e-06

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: 44.26  E-value: 9.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  65 VLQRLAGQIPMLGVCLGHQAI--------GHA----FGGRVIRagelMHGKTSPI---------FHDGSGVFRGLSNP-- 121
Cdd:COG0118    66 IREAVAGGKPVLGICLGMQLLferseengDTEglglIPGEVVR----FPASDLKVphmgwntveIAKDHPLFAGIPDGey 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2065533849 122 --FVatryHSLIVErPSLPEClrVSAWTEDG----CIMGLEhrelPLWGVQFHPE 170
Cdd:COG0118   142 fyFV----HSYYVP-PDDPED--VVATTDYGvpftAAVERG----NVFGTQFHPE 185
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 36-93 3.53e-05

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 43.01  E-value: 3.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065533849  36 VEQIAARRPRRLVISPGPCSPAEAG----ISVE---VLQRLAGQIPMLGVCLGHQAIGHAFGGRV 93
Cdd:PRK07053   40 LETLDALEPDLLVVLGGPIGVYDDElypfLAPEialLRQRLAAGLPTLGICLGAQLIARALGARV 104
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 14-187 7.15e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 41.77  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  14 NL--VQY-LQELGEEVEVHRN-DKItveqIAARRprrlVISPGpCSPAEAGIS-------VEVLQRLAgQiPMLGVCLGH 82
Cdd:PRK13170   12 NLssVKFaIERLGYEPVVSRDpDVI----LAADK----LFLPG-VGTAQAAMDqlrerelIDLIKACT-Q-PVLGICLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  83 QAIGHAF--GGRVIRAG------ELMHGKTSPIFH---------DGSGVFRGLSNP----FVatryHSLIVErpslpecl 141
Cdd:PRK13170   81 QLLGERSeeSGGVDCLGiidgpvKKMTDFGLPLPHmgwnqvtpqAGHPLFQGIEDGsyfyFV----HSYAMP-------- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2065533849 142 rVSAWTedgcIMGLEHREL--------PLWGVQFHPESILTVeGKRLLQNFLEM 187
Cdd:PRK13170  149 -VNEYT----IAQCNYGEPfsaaiqkdNFFGVQFHPERSGAA-GAQLLKNFLEM 196
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 67-186 1.31e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 40.92  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  67 QRLAGQIPMLGVCLGHQAI---GHAFG---------GRVIR---AGE-----------LMHGKTSPIFH---DGSGVFrg 117
Cdd:PRK13146   72 AVLAAGRPFLGICVGMQLLferGLEHGdtpglglipGEVVRfqpDGPalkvphmgwntVDQTRDHPLFAgipDGARFY-- 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065533849 118 lsnpFVatryHSLIVeRPSLPEclRVSAWTEDG----CIMGlehRElPLWGVQFHPESILTVeGKRLLQNFLE 186
Cdd:PRK13146  150 ----FV----HSYYA-QPANPA--DVVAWTDYGgpftAAVA---RD-NLFATQFHPEKSQDA-GLALLRNFLA 206
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 73-187 2.98e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 39.85  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  73 IPMLGVCLGHQ--------AIGH----AFGGRVIR--AGE-LMH-G-------KTSPIFH--DGSGVFrglsnpFVatry 127
Cdd:PRK13143   72 KPFLGICLGMQllfesseeGGGVrglgLFPGRVVRfpAGVkVPHmGwntvkvvKDCPLFEgiDGEYVY------FV---- 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065533849 128 HSLIVErPSLPEClrVSAWTEDGcimglehRELP-------LWGVQFHPE-SILTveGKRLLQNFLEM 187
Cdd:PRK13143  142 HSYYAY-PDDEDY--VVATTDYG-------IEFPaavcndnVFGTQFHPEkSGET--GLKILENFVEL 197
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 64-187 8.37e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 35.59  E-value: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065533849  64 EVLQR--LAGQIPMLGVCLGHQAI---GHAFG---------GRVIRAGELMHGKtspIFHDG---------SGVFRGLSN 120
Cdd:PRK13152   63 EALKEqvLVQKKPILGICLGMQLFlerGYEGGvceglgfieGEVVKFEEDLNLK---IPHMGwneleilkqSPLYQGIPE 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065533849 121 PFVATRYHSLIVErpslpeCLR--VSAWTEDGCIMGLEHRELPLWGVQFHPESILTVeGKRLLQNFLEM 187
Cdd:PRK13152  140 KSDFYFVHSFYVK------CKDefVSAKAQYGHKFVASLQKDNIFATQFHPEKSQNL-GLKLLENFARL 201
 
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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