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Conserved domains on  [gi|296031690|gb|ADG82458|]
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glutamine amidotransferase of anthranilate synthase [Thermincola potens JR]

Protein Classification

anthranilate synthase component II( domain architecture ID 11423509)

anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan

CATH:  3.40.50.880|3.60.120.10|3.40.50.880
EC:  4.1.3.27
Gene Ontology:  GO:0004049|GO:0000162
PubMed:  10387030|7495530|35816663
SCOP:  3001405|4002317|4003747

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 ...
 2-187 1.41e-148

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: 409.43  E-value: 1.41e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHMA 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*.
gi 296031690 162 VEGVQFHPESILTEAGKTLLKNFLAL 187
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLEL 186
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-187 1.41e-148

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: 409.43  E-value: 1.41e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHMA 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*.
gi 296031690 162 VEGVQFHPESILTEAGKTLLKNFLAL 187
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLEL 186
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-188 1.12e-142

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 394.50  E-value: 1.12e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*...
gi 296031690 161 AVEGVQFHPESILTEAGKTLLKNFLALS 188
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLELA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 3.59e-121

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: 339.90  E-value: 3.59e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHMA 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 296031690 162 VEGVQFHPESILTEAGKTLLKNFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-185 2.54e-108

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: 307.87  E-value: 2.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690    1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQN-EIMGIRHKH 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 296031690  160 MAVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFL 186
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 3.55e-82

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 241.76  E-value: 3.55e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690    3 LMIDNYDSFTYNLVQYLGELGAEITVYRNDkITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKY-FAGKIPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   82 HQAIGQAFGGKVIRAENL-MHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNE-IMGIRHKH 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 296031690  160 MAVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-186 4.77e-71

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 213.35  E-value: 4.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   5 IDNYDSFTYNLVQYLGE--LGAEITVYRNdKITLPEIEELNPDHIIISPGPCTP-NE--AGISLDLIKYFAGKIPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkNDrdVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  80 LGHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVerETLPDCLEITAWTDQNE---IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGeelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 296031690 157 HKHMAVEGVQFHPESILTEAGKTLLKNFLA 186
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLA 188
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-187 1.41e-148

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: 409.43  E-value: 1.41e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHMA 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*.
gi 296031690 162 VEGVQFHPESILTEAGKTLLKNFLAL 187
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLEL 186
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-188 1.12e-142

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 394.50  E-value: 1.12e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*...
gi 296031690 161 AVEGVQFHPESILTEAGKTLLKNFLALS 188
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLELA 188
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-185 2.95e-124

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 348.33  E-value: 2.95e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180
                 ....*....|....*....|....*
gi 296031690 161 AVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFI 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 3.59e-121

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: 339.90  E-value: 3.59e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHMA 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 296031690 162 VEGVQFHPESILTEAGKTLLKNFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-185 1.32e-117

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 343.62  E-value: 1.32e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAE-ITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  80 LGHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKH 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180
                 ....*....|....*....|....*.
gi 296031690 160 MAVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:PRK14607 161 HPIFGVQFHPESILTEEGKRILKNFL 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-185 2.54e-108

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: 307.87  E-value: 2.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690    1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQN-EIMGIRHKH 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 296031690  160 MAVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFL 186
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-186 3.56e-105

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 299.87  E-value: 3.56e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWT-----DQNEIMGI 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTeledgSMDEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 296031690 156 RHKHMAVEGVQFHPESILTEAGKTLLKNFLA 186
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLA 191
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 6.48e-104

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 296.77  E-value: 6.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQN----EIMGIR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGgemdEIMGIR 160

                        170       180
                 ....*....|....*....|....*....
gi 296031690 157 HKHMAVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:PRK06774 161 HRTLPLEGVQFHPESILSEQGHQLLDNFL 189
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-185 8.06e-104

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 296.44  E-value: 8.06e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*
gi 296031690 161 AVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFL 185
trpG CHL00101
anthranilate synthase component 2
 1-188 1.18e-101

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 290.86  E-value: 1.18e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*....
gi 296031690 161 -AVEGVQFHPESILTEAGKTLLKNFLALS 188
Cdd:CHL00101 161 kMLRGIQFHPESLLTTHGQQILRNFLSLS 189
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-186 1.33e-98

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 284.25  E-value: 1.33e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNP--DHIIISPGPCTPNEAGISLDLIKYFAG-KIPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAqfDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  79 CLGHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHK 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|....*...
gi 296031690 159 HMAVEGVQFHPESILTEAGKTLLKNFLA 186
Cdd:PRK07765 163 ELPIHGVQFHPESVLTEGGHRMLANWLT 190
PLN02335 PLN02335
anthranilate synthase
 2-192 4.91e-91

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 265.51  E-value: 4.91e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKVIRAEN-LMHGKTSRIYHD---GRTIFQGIPSPFTATRYHSLIVERETLP-DCLEITAWTDQNEIMGIR 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTEDGLIMAAR 180

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 296031690 157 H-KHMAVEGVQFHPESILTEAGKTLLKNFLALSVRQE 192
Cdd:PLN02335 181 HrKYKHIQGVQFHPESIITTEGKTIVRNFIKIIEKKE 217
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 3.55e-82

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 241.76  E-value: 3.55e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690    3 LMIDNYDSFTYNLVQYLGELGAEITVYRNDkITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKY-FAGKIPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   82 HQAIGQAFGGKVIRAENL-MHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNE-IMGIRHKH 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 296031690  160 MAVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-186 4.77e-71

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 213.35  E-value: 4.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   5 IDNYDSFTYNLVQYLGE--LGAEITVYRNdKITLPEIEELNPDHIIISPGPCTP-NE--AGISLDLIKYFAGKIPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkNDrdVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  80 LGHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVerETLPDCLEITAWTDQNE---IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGeelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 296031690 157 HKHMAVEGVQFHPESILTEAGKTLLKNFLA 186
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLA 188
PRK13566 PRK13566
anthranilate synthase component I;
2-187 3.50e-62

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 204.38  E-value: 3.50e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDKiTLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGF-AEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLG 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKVIRAENLMHGKTSRIY-HDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:PRK13566 608 LQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKTL 687

                        170       180       190
                 ....*....|....*....|....*....|
gi 296031690 161 AVEGVQFHPESILT---EAGKTLLKNFLAL 187
Cdd:PRK13566 688 PVAAVQFHPESIMTlggDVGLRIIENVVRL 717
PRK06895 PRK06895
anthranilate synthase component II;
1-188 6.61e-52

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 164.91  E-value: 6.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKITLPEIEelNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVE--NFSHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRT-IFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKH 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*....
gi 296031690 160 MAVEGVQFHPESILTEAGKTLLKNFLALS 188
Cdd:PRK06895 161 LPIYGVQFHPESYISEFGEQILRNWLAIS 189
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-191 1.49e-51

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 173.29  E-value: 1.49e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRND---KITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  79 CLGHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIveRETLPDCLEITAwTDQNEIMGIRHK 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 296031690 159 HMAVEGVQFHPESILTEAGKTLLKNFLALSVRQ 191
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTLAWAQQK 193
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 8.20e-44

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 155.39  E-value: 8.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   3 LMIDNYDSFTYNLVQYLGEL-GAEITVYRNDKITLPEI-----EELNPDHIIISPGPCTPNEA---GISLDLIKYfAGKI 73
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPTCPadiGICLRLLLE-CRDI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  74 PILGVCLGHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIP----SPFTATRYHSLIVERETLPDCLEITAWT-- 147
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAESLPKELVPIAWTss 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690 148 ---------------------------------------------------DQNEIMGIRHKHMAVEGVQFHPESILTEA 176
Cdd:PLN02889 244 sdtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermqNGKILMGIMHSTRPHYGLQFHPESIATCY 323


                 ....*...
gi 296031690 177 GKTLLKNF 184
Cdd:PLN02889 324 GRQIFKNF 331
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-186 1.58e-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: 153.89  E-value: 1.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690    2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNdKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRH-SHAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   82 HQAIGQAFGGKVIRAENLMHGKTSRIY-HDGRTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRvLGPDALFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180
                  ....*....|....*....|....*....
gi 296031690  161 AVEGVQFHPESILT---EAGKTLLKNFLA 186
Cdd:TIGR01815 678 PLAAVQFHPESIMTldgGAGLAMIGNVVD 706
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-185 8.35e-34

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: 118.41  E-value: 8.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   3 LMIDNYDSFTYNLVQYLGELGAEITVYRNDkITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLGH 82
Cdd:cd01742    2 LILDFGSQYTHLIARRVRELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  83 QAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERetLPDCLEITAWTDQNEIMGIRHKHMAV 162
Cdd:cd01742   81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDNCPVAAIANEEKKI 158

                        170       180
                 ....*....|....*....|...
gi 296031690 163 EGVQFHPESILTEAGKTLLKNFL 185
Cdd:cd01742  159 YGVQFHPEVTHTEKGKEILKNFL 181
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-187 2.00e-33

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 117.26  E-value: 2.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   1 MLLMIDNYDSFTYNLVQYLGELGAEITVYRNDKiTLPEIEElNPDHIIISPGPcTPNEAGISLDLIKYFagKIPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTT-PVEEIKA-FEDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  81 GHQAIGQAFGGKVIRAENLMHGKTsRIY---HDgrTIFQGIPSPFTATRYHSliVERETLPDCLEITAWTDQNEIMGIRH 157
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALV-EVEildED--DILKGLPPEIRVWASHA--DEVKELPDGFEILARSDICEVEAMKH 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 296031690 158 KHMAVEGVQFHPESILTEAGKTLLKNFLAL 187
Cdd:PRK00758 151 KEKPIYGVQFHPEVAHTEYGEEIFKNFLEI 180
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-181 6.19e-33

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 116.87  E-value: 6.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNdKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  82 HQAIGQAFGGKViRAENLMHGKT-----------SRIYHD-------GRTIFQGIPSPFtaTRYHSL-IVEretLPDCLE 142
Cdd:PRK05637  83 FQALLEHHGGKV-EPCGPVHGTTdnmiltdagvqSPVFAGlatdvepDHPEIPGRKVPI--ARYHSLgCVV---APDGME 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296031690 143 ITAWTDQ---NEIMGIR-HKHMAVeGVQFHPESILTEAGKTLL 181
Cdd:PRK05637 157 SLGTCSSeigPVIMAAEtTDGKAI-GLQFHPESVLSPTGPIIL 198
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-185 8.32e-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: 115.87  E-value: 8.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690    2 LLMIDNYDSFTYNLVQYLGELGAEITVYRNDkITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   82 HQAIGQAFGGKVIRAENLMHGKTS-RIYHDGrTIFQGIPSPFTATRYHSLIVERetLPDCLEITAWTDQNEIMGIRHKHM 160
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAElEILDED-DLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDNCPVAAMAHEEK 156

                         170       180
                  ....*....|....*....|....*
gi 296031690  161 AVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:TIGR00888 157 PIYGVQFHPEVTHTEYGNELLENFV 181
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-188 1.45e-31

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: 120.01  E-value: 1.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690    2 LLMIDNYDSFTYNLVQYL---GELGAEITVYRNDKITlPEIEELNP--DHIIISPGPCTPNEA---GISLDLIKY-FAGK 72
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQ-DQLLELLPlfDAIVVGPGPGNPNNAqdmGIISELWELaNLDE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   73 IPILGVCLGHQAIGQAFGGKVIRAENLMHGKTSRIYHDGRTIFQGIpSPFTATRYHSLIVERETlPDCL--EITAWTDQN 150
Cdd:TIGR01823  87 VPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLYANPEG-IDTLlpLCLTEDEEG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 296031690  151 EI-MGIRHKHMAVEGVQFHPESILTEAGK-TLLKNFLALS 188
Cdd:TIGR01823 165 IIlMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKLA 204
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-187 8.11e-28

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: 104.26  E-value: 8.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   2 LLMIDNYDSFTYNLVQYLGELGAEITVYR--NDKITLPEIEELNPDHIIISPGPCTPNEAGISL----DLIKY-FAGKIP 74
Cdd:COG0518    5 LDHDPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLedepALIREaFELGKP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  75 ILGVCLGHQAIGQAFGGKVIRAENLMHGKTsRIY-HDGRTIFQGIPSPFTATRYHSLIVERetLPDCLEITAWTDQNEIM 153
Cdd:COG0518   85 VLGICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTVWMSHGDTVTE--LPEGAEVLASSDNCPNQ 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296031690 154 GIRHKHMAVeGVQFHPE------------------------------SILTEAGKTLLKNFLAL 187
Cdd:COG0518  162 AFRYGRRVY-GVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 5.53e-27

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: 100.65  E-value: 5.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  13 YNLVQYLGELGAEITVYRNDKiTLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGK-IPILGVCLGHQAIGQAFGG 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  92 KVI------RAEN--LMHGKTSRIYhdgrtifqgipspfTATRYHSLIVERETLPDCLEITAWT-DQNEIMGIRHKHMAV 162
Cdd:cd01744   89 KTYkmkfghRGSNhpVKDLITGRVY--------------ITSQNHGYAVDPDSLPGGLEVTHVNlNDGTVEGIRHKDLPV 154


                 ....*....
gi 296031690 163 EGVQFHPES 171
Cdd:cd01744  155 FSVQFHPEA 163
guaA PRK00074
GMP synthase; Reviewed
 21-185 1.27e-25

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 102.43  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  21 ELG--AEITVYRndkITLPEIEELNPDHIIISPGPCTPNEAGiSLDLIKY-FAGKIPILGVCLGHQAIGQAFGGKVIRAE 97
Cdd:PRK00074  25 ELGvySEIVPYD---ISAEEIRAFNPKGIILSGGPASVYEEG-APRADPEiFELGVPVLGICYGMQLMAHQLGGKVERAG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  98 NLMHGKTSRIYHDGRTIFQGIPSPFTATRYHSLIVERetLPDCLEITAWTDQNEIMGIRHKHMAVEGVQFHPESILTEAG 177
Cdd:PRK00074 101 KREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQG 178


                 ....*...
gi 296031690 178 KTLLKNFL 185
Cdd:PRK00074 179 KKLLENFV 186
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
13-171 3.77e-20

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 86.28  E-value: 3.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  13 YNLVQYLGELGAEITVYRNDkITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAG-KIPILGVCLGHQAIGQAFGG 91
Cdd:PRK12564 189 RNILRELAERGCRVTVVPAT-TTAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEkKIPIFGICLGHQLLALALGA 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  92 KVIRaenlM----HG--------KTSRIYhdgrtifqgipspFTaTRYHSLIVERETLPDCLEITAWT--DqNEIMGIRH 157
Cdd:PRK12564 268 KTYK----MkfghRGanhpvkdlETGKVE-------------IT-SQNHGFAVDEDSLPANLEVTHVNlnD-GTVEGLRH 328

                        170
                 ....*....|....
gi 296031690 158 KHMAVEGVQFHPES 171
Cdd:PRK12564 329 KDLPAFSVQYHPEA 342
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 14-170 4.42e-20

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 85.71  E-value: 4.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  14 NLVQYLGELGAEITVYRNDKiTLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLGHQAIGQAFGGKV 93
Cdd:PRK12838 180 SILRSLSKRGCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADT 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  94 IRAENLMHG--------KTSRIYhdgrtifqgipspfTATRYHSLIVERETLPDCLEITAWTDQN--EIMGIRHKHMAVE 163
Cdd:PRK12838 259 EKLPFGHRGanhpvidlTTGRVW--------------MTSQNHGYVVDEDSLDGTPLSVRFFNVNdgSIEGLRHKKKPVL 324


                 ....*..
gi 296031690 164 GVQFHPE 170
Cdd:PRK12838 325 SVQFHPE 331
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 13-171 6.08e-20

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: 85.46  E-value: 6.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  13 YNLVQYLGELGAEITVYRNDkITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAGK-IPILGVCLGHQAIGQAFGG 91
Cdd:COG0505  188 RNILRELAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGA 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  92 KVIRaenlM----HG--------KTSRIYhdgrtifqgipspFTAtRYHSLIVERETLPD-CLEITawtdQ-----NEIM 153
Cdd:COG0505  267 KTYK----LkfghRGanhpvkdlETGRVE-------------ITS-QNHGFAVDEDSLPAtDLEVT----HvnlndGTVE 324

                        170
                 ....*....|....*...
gi 296031690 154 GIRHKHMAVEGVQFHPES 171
Cdd:COG0505  325 GLRHKDLPAFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 36-185 7.57e-19

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 83.20  E-value: 7.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  36 LPEIEELNPDHIIISPGPCTPNEAG---ISLDLIKYFAGK-IPILGVCLGHQAIGQAFGGKVIRAENLMHGKTSRIYHDG 111
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPHSVHVEGaptVPEGFFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296031690 112 RTIFQGIPSPFTATRYHSLIVERETLPDCLEITAWTDQNEIMGIRHKHMAVEGVQFHPESILTEAGKTLLKNFL 185
Cdd:PLN02347 126 SQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 8-171 2.98e-18

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 81.18  E-value: 2.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   8 YD-SFTYNLVQYLGELGAEITVYRNdkiTLPEIE--ELNPDHIIISPGPCTPNEAGISLDLIKYFAGKIPILGVCLGHQA 84
Cdd:PLN02771 246 YDfGIKHNILRRLASYGCKITVVPS---TWPASEalKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQL 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  85 IGQAFGGKVIRAENLMHGKTsriyHDGRTIFQGIPSpfTATRYHSLIVERETLPDCLEITAWT-DQNEIMGIRHKHMAVE 163
Cdd:PLN02771 323 LGQALGGKTFKMKFGHHGGN----HPVRNNRTGRVE--ISAQNHNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVM 396


                 ....*...
gi 296031690 164 GVQFHPES 171
Cdd:PLN02771 397 SLQYHPEA 404
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 19-185 7.13e-17

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: 74.59  E-value: 7.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  19 LGELGAEITVYRNDKITLPEiEELNPDHIIISPGPCTPNEAGIS-----LDLIKY-FAGKIPILGVCLGHQAIGQAFGGK 92
Cdd:cd01741   23 AGAETIEIDVVDVYAGELLP-DLDDYDGLVILGGPMSVDEDDYPwlkklKELIRQaLAAGKPVLGICLGHQLLARALGGK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  93 VIRAENLMHGKTSRIY--HDGRT--IFQGIPSPFTATRYHSLIVERetLPDCLEITAWTDQNEIMGIRhKHMAVEGVQFH 168
Cdd:cd01741  102 VGRNPKGWEIGWFPVTltEAGKAdpLFAGLPDEFPVFHWHGDTVVE--LPPGAVLLASSEACPNQAFR-YGDRALGLQFH 178

                        170
                 ....*....|....*..
gi 296031690 169 PEsilteagKTLLKNFL 185
Cdd:cd01741  179 PE-------ERLLRNFL 188
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-171 6.70e-13

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 65.97  E-value: 6.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  13 YNLVQYLGELGAEITVYrNDKITLPEIEELNPDHIIISPGPCTPNEAGISLDLIKYFAG-KIPILGVCLGHQAIGQAFGG 91
Cdd:CHL00197 204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEA 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  92 KVIRaenLMHGktsriyHDGRTIFQGIPSPFTAT-RYHSLIVERETL-PDCLEITAWT-DQNEIMGIRHKHMAVEGVQFH 168
Cdd:CHL00197 283 KTFK---LKFG------HRGLNHPSGLNQQVEITsQNHGFAVNLESLaKNKFYITHFNlNDGTVAGISHSPKPYFSVQYH 353


                 ...
gi 296031690 169 PES 171
Cdd:CHL00197 354 PEA 356
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 7.61e-13

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: 62.23  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   3 LMIDNYDSFT---YNLVQYLGELGAEITVYRNDKITLPEIEEL-NPDHIIISPGPCTPNEAGISLDLI----KYFAGKIP 74
Cdd:cd01653    2 AVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLARDEALLallrEAAAAGKP 81

                         90
                 ....*....|.
gi 296031690  75 ILGVCLGHQAI 85
Cdd:cd01653   82 ILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 8.46e-13

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: 61.45  E-value: 8.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   3 LMIDNYDSFT---YNLVQYLGELGAEITVYRNDKITLPEIEEL-NPDHIIISPGPCTPNEAGISLDLI----KYFAGKIP 74
Cdd:cd03128    2 AVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLAWDEALLallrEAAAAGKP 81

                         90
                 ....*....|.
gi 296031690  75 ILGVCLGHQAI 85
Cdd:cd03128   82 VLGICLGAQLL 92
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 74-170 2.15e-09

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 54.97  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  74 PILGVCLGHQAIGQAFGGKVI-----RAENLMHGKTSRIYHDGRtIFQGIPSPFTATRYHSLIVERetLPDCLEITAWTD 148
Cdd:PRK09065  90 PLLGICYGHQLLAHALGGEVGynpagRESGTVTVELHPAAADDP-LFAGLPAQFPAHLTHLQSVLR--LPPGAVVLARSA 166

                         90       100
                 ....*....|....*....|..
gi 296031690 149 QNEIMGIRHKHMAVeGVQFHPE 170
Cdd:PRK09065 167 QDPHQAFRYGPHAW-GVQFHPE 187
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 65-170 1.84e-08

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: 51.81  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  65 LIKYF-AGKIPILGVCLGHQAIGQAFGGkviraenlmhgktsriyhdgrTIFQGIpspfTATRYHSLIVERetLPDCLEI 143
Cdd:cd01745   92 LLRAAlERGKPILGICRGMQLLNVALGG---------------------TLYQDI----RVNSLHHQAIKR--LADGLRV 144

                         90       100
                 ....*....|....*....|....*...
gi 296031690 144 TAWTDQNEIMGIRHKHMA-VEGVQFHPE 170
Cdd:cd01745  145 EARAPDGVIEAIESPDRPfVLGVQWHPE 172
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 57-187 3.53e-08

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: 51.17  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   57 NEAGISLDLIKYFAGKIPILGVCLGHQAIGQA------------FGGKVIRAEnlmhgkTSRIYHDG---------RTIF 115
Cdd:TIGR01855  56 RENGLDLFVELVVRLGKPVLGICLGMQLLFERseegggvpglglIKGNVVKLE------ARKVPHMGwnevhpvkeSPLL 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296031690  116 QGIPSPFTATRYHSLIVERETlpdcLEITAWTDQNEIM--GIRHKHMAveGVQFHPE-SilTEAGKTLLKNFLAL 187
Cdd:TIGR01855 130 NGIDEGAYFYFVHSYYAVCEE----EAVLAYADYGEKFpaAVQKGNIF--GTQFHPEkS--GKTGLKLLENFLEL 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 22-185 1.41e-07

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: 49.42  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  22 LGAEITVYRNDKitlpEIeeLNPDHIIIsPG-----PCTPN--EAGISLDLIKYFAGKIPILGVCLGHQAIGQA------ 88
Cdd:cd01748   21 LGAEVIITSDPE----EI--LSADKLIL-PGvgafgDAMANlrERGLIEALKEAIASGKPFLGICLGMQLLFESseeggg 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  89 ------FGGKVIRaenLMHGKTSRIYHDG---------RTIFQGIPSPftaTRY---HSLIVEretLPDCLEITAWTDQN 150
Cdd:cd01748   94 tkglglIPGKVVR---FPASEGLKVPHMGwnqleitkeSPLFKGIPDG---SYFyfvHSYYAP---PDDPDYILATTDYG 164

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296031690 151 EIM--GIRHKHMAveGVQFHPE-SilTEAGKTLLKNFL 185
Cdd:cd01748  165 GKFpaAVEKDNIF--GTQFHPEkS--GKAGLKLLKNFL 198
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 22-187 2.84e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 45.62  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  22 LGAEITVYRN-DKItlpeieeLNPDHIIIsPGPCTPNEAGISL------DLIKyfAGKIPILGVCLGHQAIGQAFG-GKV 93
Cdd:PRK13170  23 LGYEPVVSRDpDVI-------LAADKLFL-PGVGTAQAAMDQLrereliDLIK--ACTQPVLGICLGMQLLGERSEeSGG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  94 IRAENLMHGKTSRI----------------YHDGRTIFQGIPSpfTATRY--HSLIVE--RETLPDC---LEITAWTDQN 150
Cdd:PRK13170  93 VDCLGIIDGPVKKMtdfglplphmgwnqvtPQAGHPLFQGIED--GSYFYfvHSYAMPvnEYTIAQCnygEPFSAAIQKD 170

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 296031690 151 EIMGirhkhmavegVQFHPE-SilTEAGKTLLKNFLAL 187
Cdd:PRK13170 171 NFFG----------VQFHPErS--GAAGAQLLKNFLEM 196
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 72-170 1.34e-05

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: 44.17  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690   72 KIPILGVCLGHQAIGQAFGG--------KVIRAENLMH--GKTSRIYHD-----GRTIFQGIPSPFTATR-YHSLIVERe 135
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGtlyqdiqeQPGFTDHREHcqVAPYAPSHAvnvepGSLLASLLGSEEFRVNsLHHQAIDR- 183

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 296031690  136 tLPDCLEITAWTDQNEIMGIRHK--HMAVEGVQFHPE 170
Cdd:pfam07722 184 -LAPGLRVEAVAPDGTIEAIESPnaKGFALGVQWHPE 219
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 70-186 3.23e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 42.85  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  70 AGKiPILGVCLGHQ-------------AIGQaFGGKVIRAENlmHGKTSRIYHDG---------RTIFQGIPspfTATRY 127
Cdd:PRK13146  76 AGR-PFLGICVGMQllferglehgdtpGLGL-IPGEVVRFQP--DGPALKVPHMGwntvdqtrdHPLFAGIP---DGARF 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296031690 128 ---HSLIVERETLPDCLeitAWTDqneimgirhkH-----MAVE-----GVQFHPE-SilTEAGKTLLKNFLA 186
Cdd:PRK13146 149 yfvHSYYAQPANPADVV---AWTD----------YggpftAAVArdnlfATQFHPEkS--QDAGLALLRNFLA 206
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 28-93 1.01e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 38.79  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  28 VYRNDKitLPEieelNPDHI---IISPGPCTPNEagiSLDLIKYF--------------AGKIpILGVCLGHQAIGQAFG 90
Cdd:PRK08250  33 VYAGEA--LPE----NADGFdllIVMGGPQSPRT---TREECPYFdskaeqrlinqaikAGKA-VIGVCLGAQLIGEALG 102


                 ...
gi 296031690  91 GKV 93
Cdd:PRK08250 103 AKY 105
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 72-187 2.17e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 37.51  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296031690  72 KIPILGVCLGHQAI---GQAFG---------GKVIRAE-----NLMHGKTSRIYHDGRT-IFQGIPSPFTATRYHSLIVE 133
Cdd:PRK13152  73 KKPILGICLGMQLFlerGYEGGvceglgfieGEVVKFEedlnlKIPHMGWNELEILKQSpLYQGIPEKSDFYFVHSFYVK 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296031690 134 retlpdCLE--ITAWTDQNEIMGIRHKHMAVEGVQFHPESIlTEAGKTLLKNFLAL 187
Cdd:PRK13152 153 ------CKDefVSAKAQYGHKFVASLQKDNIFATQFHPEKS-QNLGLKLLENFARL 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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