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Conserved domains on  [gi|489336581|ref|WP_003243797|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [Bacillus]

Protein Classification

aminodeoxychorismate/anthranilate synthase component II( domain architecture ID 10792969)

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
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-194 6.45e-148

aminodeoxychorismate/anthranilate synthase component II;


:

Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 408.04  E-value: 6.45e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489336581 161 PIEGVQFHPESIMTSFGKEMLRNFIETYRKEVIA 194
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVTS 194
 
Name Accession Description Interval E-value
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-194 6.45e-148

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 408.04  E-value: 6.45e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489336581 161 PIEGVQFHPESIMTSFGKEMLRNFIETYRKEVIA 194
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVTS 194
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-190 3.61e-138

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: 383.23  E-value: 3.61e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDLP 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*....
gi 489336581 162 IEGVQFHPESIMTSFGKEMLRNFIETYRK 190
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLELAGE 189
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 8.27e-124

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: 347.16  E-value: 8.27e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581    1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEG-EIMAIRHND 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 489336581  160 LPIEGVQFHPESIMTSFGKEMLRNFIET 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 6.20e-115

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: 324.49  E-value: 6.20e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDLP 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 489336581 162 IEGVQFHPESIMTSFGKEMLRNFI 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
3-184 9.27e-77

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 227.89  E-value: 9.27e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581    3 LMIDNYDSFTYNLVQYLGELGEELVVKRNDSiTIDEIEELSPDFLMISPGPCSPDEAGISLEAIKH-FAGKIPIFGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   82 HQSIAQVFGGDVVRAERL-MHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGE-IMAIRHND 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*
gi 489336581  160 LPIEGVQFHPESIMTSFGKEMLRNF 184
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNF 184
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 3.92e-67

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 203.72  E-value: 3.92e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   5 IDNYDSFTYNLVQYLGELGE--ELVVKRNdSITIDEIEELSPDFLMISPGPCSPD---EAGISLEAIKHFAGKIPIFGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  80 LGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVkpETLPSCFTVTAQTK-EGE--IMAIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDhDGEelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489336581 157 HNDLPIEGVQFHPESIMTSFGKEMLRNFIET 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
 
Name Accession Description Interval E-value
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-194 6.45e-148

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 408.04  E-value: 6.45e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489336581 161 PIEGVQFHPESIMTSFGKEMLRNFIETYRKEVIA 194
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVTS 194
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-190 3.61e-138

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: 383.23  E-value: 3.61e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDLP 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*....
gi 489336581 162 IEGVQFHPESIMTSFGKEMLRNFIETYRK 190
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLELAGE 189
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 9.26e-133

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 369.46  E-value: 9.26e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 489336581 161 PIEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 8.27e-124

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: 347.16  E-value: 8.27e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581    1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEG-EIMAIRHND 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 489336581  160 LPIEGVQFHPESIMTSFGKEMLRNFIET 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 6.20e-115

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: 324.49  E-value: 6.20e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDLP 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 489336581 162 IEGVQFHPESIMTSFGKEMLRNFI 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-193 1.59e-106

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 315.50  E-value: 1.59e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELG-EELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGpEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  80 LGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHND 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489336581 160 LPIEGVQFHPESIMTSFGKEMLRNFIEtYRKEVI 193
Cdd:PRK14607 161 HPIFGVQFHPESILTEEGKRILKNFLN-YQREEI 193
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-185 1.60e-100

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 288.31  E-value: 1.60e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTK--EG---EIMAI 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGsmdEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 489336581 156 RHNDLPIEGVQFHPESIMTSFGKEMLRNFI 185
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 1.62e-99

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 285.66  E-value: 1.62e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 489336581 161 PIEGVQFHPESIMTSFGKEMLRNFIET 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-186 1.62e-97

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 280.59  E-value: 1.62e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEG----EIMAIR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGgemdEIMGIR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 489336581 157 HNDLPIEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:PRK06774 161 HRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
trpG CHL00101
anthranilate synthase component 2
 1-186 2.24e-90

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 262.75  E-value: 2.24e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*..
gi 489336581 161 P-IEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:CHL00101 161 KmLRGIQFHPESLLTTHGQQILRNFLS 187
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-186 2.32e-90

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 263.45  E-value: 2.32e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDF--LMISPGPCSPDEAGISLEAIKHFAG-KIPIFGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFdgVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  79 CLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHN 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|....*...
gi 489336581 159 DLPIEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:PRK07765 163 ELPIHGVQFHPESVLTEGGHRMLANWLT 190
PLN02335 PLN02335
anthranilate synthase
 2-185 2.24e-80

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 238.54  E-value: 2.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDVVRAER-LMHGKTSDIEHDGK---TIFEGLKNPLVATRYHSLIVKPETLPS-CFTVTAQTKEGEIMAIR 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDEKgeeGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 489336581 157 HNDLP-IEGVQFHPESIMTSFGKEMLRNFI 185
Cdd:PLN02335 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
GATase pfam00117
Glutamine amidotransferase class-I;
3-184 9.27e-77

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 227.89  E-value: 9.27e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581    3 LMIDNYDSFTYNLVQYLGELGEELVVKRNDSiTIDEIEELSPDFLMISPGPCSPDEAGISLEAIKH-FAGKIPIFGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   82 HQSIAQVFGGDVVRAERL-MHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGE-IMAIRHND 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*
gi 489336581  160 LPIEGVQFHPESIMTSFGKEMLRNF 184
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNF 184
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 3.92e-67

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 203.72  E-value: 3.92e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   5 IDNYDSFTYNLVQYLGELGE--ELVVKRNdSITIDEIEELSPDFLMISPGPCSPD---EAGISLEAIKHFAGKIPIFGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  80 LGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVkpETLPSCFTVTAQTK-EGE--IMAIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDhDGEelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489336581 157 HNDLPIEGVQFHPESIMTSFGKEMLRNFIET 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
PRK13566 PRK13566
anthranilate synthase component I;
2-190 4.53e-56

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 188.20  E-value: 4.53e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDsITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLG 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDVVRAERLMHGKTSDIE-HDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:PRK13566 608 LQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKTL 687

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489336581 161 PIEGVQFHPESIMT---SFGKEMLRNFIETYRK 190
Cdd:PRK13566 688 PVAAVQFHPESIMTlggDVGLRIIENVVRLLAG 720
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-181 2.77e-55

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 182.92  E-value: 2.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRND---SITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  79 CLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIvkPETLPSCFTVTAQTkEGEIMAIRHN 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINAHF-NGMVMAVRHD 160

                        170       180
                 ....*....|....*....|...
gi 489336581 159 DLPIEGVQFHPESIMTSFGKEML 181
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLL 183
PRK06895 PRK06895
anthranilate synthase component II;
1-186 3.23e-45

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 147.96  E-value: 3.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSpdFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKT-IFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHND 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*..
gi 489336581 160 LPIEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:PRK06895 161 LPIYGVQFHPESYISEFGEQILRNWLA 187
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-190 1.96e-42

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: 150.81  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581    2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNdSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRH-SHAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   82 HQSIAQVFGGDVVRAERLMHGKTSDIE-HDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDL 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRvLGPDALFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489336581  161 PIEGVQFHPESIMT---SFGKEMLRNFIETYRK 190
Cdd:TIGR01815 678 PLAAVQFHPESIMTldgGAGLAMIGNVVDRLAA 710
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-186 2.49e-39

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 142.68  E-value: 2.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   3 LMIDNYDSFTYNLVQYLGEL-GEELVVKRNDSITIDEI-----EELSPDFLMISPGPCSP---DEAGISLEAIKHfAGKI 73
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLLLE-CRDI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  74 PIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFE----GLKNPLVATRYHSLIVKPETLP----------- 138
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDdipsGRNSGFKVVRYHSLVIDAESLPkelvpiawtss 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581 139 ---------------------------SCFTVTAQTKEGE---------------IMAIRHNDLPIEGVQFHPESIMTSF 176
Cdd:PLN02889 244 sdtlsflesqksglvpdayesqigqsgSSDPFSSKLKNGTswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIATCY 323

                        250
                 ....*....|
gi 489336581 177 GKEMLRNFIE 186
Cdd:PLN02889 324 GRQIFKNFRE 333
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-186 8.51e-36

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: 123.58  E-value: 8.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581    2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDSiTIDEIEELSPDFLMISPGPCSpDEAGISLEAIKH-FAGKIPIFGVCL 80
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSS-VYAENAPRADEKiFELGVPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   81 GHQSIAQVFGGDVVRAERLMHGKTS-DIEHDGKtIFEGLKNPLVATRYHSLIVKpeTLPSCFTVTAQTKEGEIMAIRHND 159
Cdd:TIGR00888  79 GMQLMAKQLGGEVGRAEKREYGKAElEILDEDD-LFRGLPDESTVWMSHGDKVK--ELPEGFKVLATSDNCPVAAMAHEE 155

                         170       180
                  ....*....|....*....|....*..
gi 489336581  160 LPIEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:TIGR00888 156 KPIYGVQFHPEVTHTEYGNELLENFVY 182
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-186 2.22e-35

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 122.65  E-value: 2.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMIDNYDSFTYNLVQYLGELGEELVVKRNDsITIDEIEELsPDFLMISPGPcSPDEAGISLEAIKHFagKIPIFGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  81 GHQSIAQVFGGDVVRAERLMHGKT--SDIEHDgkTIFEGLKNPLVATRYHSLIVKpeTLPSCFTVTAQTKEGEIMAIRHN 158
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALVevEILDED--DILKGLPPEIRVWASHADEVK--ELPDGFEILARSDICEVEAMKHK 151

                        170       180
                 ....*....|....*....|....*...
gi 489336581 159 DLPIEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:PRK00758 152 EKPIYGVQFHPEVAHTEYGEEIFKNFLE 179
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 2-185 7.74e-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: 7.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNDsITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:cd01742    1 ILILDFGSQYTHLIARRVRELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVkpETLPSCFTVTAQTKEGEIMAIRHNDLP 161
Cdd:cd01742   80 MQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEV--VKLPEGFKVIASSDNCPVAAIANEEKK 157

                        170       180
                 ....*....|....*....|....
gi 489336581 162 IEGVQFHPESIMTSFGKEMLRNFI 185
Cdd:cd01742  158 IYGVQFHPEVTHTEKGKEILKNFL 181
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-186 6.61e-31

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 111.86  E-value: 6.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFTYNLVQYLGELGEELVVKRNdSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  82 HQSIAQVFGGDvVRA-------------------ERLMHGKTSDIEHDGKTiFEGLKNPLvaTRYHSL--IVKPETLPSC 140
Cdd:PRK05637  83 FQALLEHHGGK-VEPcgpvhgttdnmiltdagvqSPVFAGLATDVEPDHPE-IPGRKVPI--ARYHSLgcVVAPDGMESL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489336581 141 FTVTAQTKEgEIMAIRHNDLPIEGVQFHPESIMTSFGKEMLRNFIE 186
Cdd:PRK05637 159 GTCSSEIGP-VIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVE 203
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-186 1.60e-30

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: 117.31  E-value: 1.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581    2 ILMIDNYDSFTYNLVQYLGELGEELV-VKRNDSITID-EIEELSPDF--LMISPGPCSPDEA---GIsLEAIKHFAG--K 72
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLEQQTDISVhVTTVHSDTFQdQLLELLPLFdaIVVGPGPGNPNNAqdmGI-ISELWELANldE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   73 IPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNpLVATRYHSLIVKPETLPSCFT-VTAQTKEGE 151
Cdd:TIGR01823  87 VPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGIDTLLPlCLTEDEEGI 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489336581  152 I-MAIRHNDLPIEGVQFHPESIMTSFGK-EMLRNFIE 186
Cdd:TIGR01823 166 IlMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLK 202
guaA PRK00074
GMP synthase; Reviewed
 33-185 4.22e-26

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 103.97  E-value: 4.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  33 SITIDEIEELSPDFLMISPGPCSPDEAGISL--EAIkhFAGKIPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTsDIEHD 110
Cdd:PRK00074  36 DISAEEIRAFNPKGIILSGGPASVYEEGAPRadPEI--FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRA-ELEVD 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489336581 111 GKT-IFEGLKNPLVATRYHSLIVkpETLPSCFTVTAQTKEGEIMAIRHNDLPIEGVQFHPESIMTSFGKEMLRNFI 185
Cdd:PRK00074 113 NDSpLFKGLPEEQDVWMSHGDKV--TELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFV 186
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-191 2.03e-24

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: 95.40  E-value: 2.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMID---NYDSFTYNLVQYLGELGEELVVKR--NDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKH-----FAG 71
Cdd:COG0518    2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPAlireaFEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  72 KIPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTsDIE-HDGKTIFEGLKNPLVATRYHSLIVkpETLPSCFTVTAQTKEG 150
Cdd:COG0518   82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTVWMSHGDTV--TELPEGAEVLASSDNC 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489336581 151 EIMAIRHNDlPIEGVQFHPEsimtsFGKEMLRNFIETYRKE 191
Cdd:COG0518  159 PNQAFRYGR-RVYGVQFHPE-----VTHTMMEAWLEERADE 193
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 9.89e-22

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: 87.17  E-value: 9.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  13 YNLVQYLGELGEELVVKRNDSiTIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGK-IPIFGVCLGHQSIAQVFGG 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  92 DVVRaerlM----HGktSD---IEHDGKTIFeglknplVATRYHSLIVKPETLPSCFTVT-----AQTKEGeimaIRHND 159
Cdd:cd01744   89 KTYK----MkfghRG--SNhpvKDLITGRVY-------ITSQNHGYAVDPDSLPGGLEVThvnlnDGTVEG----IRHKD 151

                        170
                 ....*....|..
gi 489336581 160 LPIEGVQFHPES 171
Cdd:cd01744  152 LPVFSVQFHPEA 163
PLN02347 PLN02347
GMP synthetase
 36-185 9.62e-20

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 85.89  E-value: 9.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  36 IDEIEELSPDFLMISPGPCSPDEAG---ISLEAIKHFAGK-IPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDG 111
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPHSVHVEGaptVPEGFFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489336581 112 KTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDLPIEGVQFHPESIMTSFGKEMLRNFI 185
Cdd:PLN02347 126 SQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
35-171 9.45e-19

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 82.43  E-value: 9.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  35 TIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAG-KIPIFGVCLGHQSIAQVFGGDVVRaerlM----HG------- 102
Cdd:PRK12564 210 TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEkKIPIFGICLGHQLLALALGAKTYK----MkfghRGanhpvkd 285

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489336581 103 -KTSDIEhdgktifeglknplVATRYHSLIVKPETLPSCFTVTA-----QTKEGeimaIRHNDLPIEGVQFHPES 171
Cdd:PRK12564 286 lETGKVE--------------ITSQNHGFAVDEDSLPANLEVTHvnlndGTVEG----LRHKDLPAFSVQYHPEA 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 35-171 9.77e-18

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: 79.68  E-value: 9.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  35 TIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGK-IPIFGVCLGHQSIAQVFGGDVVRaerlM----HG-----Kt 104
Cdd:COG0505  209 SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYK----LkfghRGanhpvK- 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489336581 105 sDIEhDGKTifeglknpLVATRYHSLIVKPETLP-SCFTVTA-----QTKEGeimaIRHNDLPIEGVQFHPES 171
Cdd:COG0505  284 -DLE-TGRV--------EITSQNHGFAVDEDSLPaTDLEVTHvnlndGTVEG----LRHKDLPAFSVQYHPEA 342
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 35-170 1.90e-16

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 75.70  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  35 TIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLGHQSIAQVFGGDVvraERLMHGktsdieHDG--- 111
Cdd:PRK12838 200 SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADT---EKLPFG------HRGanh 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489336581 112 -------KTIFEGLKNplvatryHSLIVKPETL-PSCFTVTA-QTKEGEIMAIRHNDLPIEGVQFHPE 170
Cdd:PRK12838 271 pvidlttGRVWMTSQN-------HGYVVDEDSLdGTPLSVRFfNVNDGSIEGLRHKKKPVLSVQFHPE 331
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 38-171 4.73e-15

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 72.32  E-value: 4.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  38 EIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEg 117
Cdd:PLN02771 276 EALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVE- 354

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489336581 118 lknplVATRYHSLIVKPETLPSCFTVT-AQTKEGEIMAIRHNDLPIEGVQFHPES 171
Cdd:PLN02771 355 -----ISAQNHNYAVDPASLPEGVEVThVNLNDGSCAGLAFPALNVMSLQYHPEA 404
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 45-185 1.84e-13

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: 65.34  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  45 DFLMISPGPCSPDEAGIS-LEAIKHF-----AGKIPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIE--HDGKT--I 114
Cdd:cd01741   48 DGLVILGGPMSVDEDDYPwLKKLKELirqalAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTltEAGKAdpL 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489336581 115 FEGLKNPLVATRYHSLIVkpETLPSCFTVTAQTKEGEIMAIRHNDLPIeGVQFHPEsimtsfgKEMLRNFI 185
Cdd:cd01741  128 FAGLPDEFPVFHWHGDTV--VELPPGAVLLASSEACPNQAFRYGDRAL-GLQFHPE-------ERLLRNFL 188
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-171 5.74e-12

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 63.28  E-value: 5.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  13 YNLVQYLGELGEELVVKrNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAG-KIPIFGVCLGHQSIAQVFGG 91
Cdd:CHL00197 204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEA 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  92 DVVraeRLMHGktsdieHDGKTIFEGLKNPL-VATRYHSLIVKPETL-PSCFTVTA-QTKEGEIMAIRHNDLPIEGVQFH 168
Cdd:CHL00197 283 KTF---KLKFG------HRGLNHPSGLNQQVeITSQNHGFAVNLESLaKNKFYITHfNLNDGTVAGISHSPKPYFSVQYH 353


                 ...
gi 489336581 169 PES 171
Cdd:CHL00197 354 PEA 356
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 1.51e-10

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 56.07  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFT---YNLVQYLGELGEELVVKRNDSITIDEIEELS-PDFLMISPGPCSPDEAGISLEAI----KHFAGKI 73
Cdd:cd01653    1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDdYDGLILPGGPGTPDDLARDEALLallrEAAAAGK 80

                         90
                 ....*....|..
gi 489336581  74 PIFGVCLGHQSI 85
Cdd:cd01653   81 PILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 4.55e-10

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: 54.13  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   2 ILMIDNYDSFT---YNLVQYLGELGEELVVKRNDSITIDEIEELS-PDFLMISPGPCSPDEAGISLEAI----KHFAGKI 73
Cdd:cd03128    1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDdYDGLILPGGPGTPDDLAWDEALLallrEAAAAGK 80

                         90
                 ....*....|..
gi 489336581  74 PIFGVCLGHQSI 85
Cdd:cd03128   81 PVLGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-170 7.07e-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: 52.96  E-value: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  63 LEAIKHF-AGKIPIFGVCLGHQSIAQVFGGDVVRaerlmhgktsDIEhdgktifeglknplvATRYHSLIVKpeTLPSCF 141
Cdd:cd01745   90 LALLRAAlERGKPILGICRGMQLLNVALGGTLYQ----------DIR---------------VNSLHHQAIK--RLADGL 142

                         90       100       110
                 ....*....|....*....|....*....|
gi 489336581 142 TVTAQTKEGEIMAIRH-NDLPIEGVQFHPE 170
Cdd:cd01745  143 RVEARAPDGVIEAIESpDRPFVLGVQWHPE 172
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 58-186 1.99e-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: 51.94  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   58 EAGISLEAIKHFAGKIPIFGVCLGHQSIAQ------------VFGGDVVR--AERLMH-GKTSDIEHDGKTIFEGLKNPL 122
Cdd:TIGR01855  57 ENGLDLFVELVVRLGKPVLGICLGMQLLFErseegggvpglgLIKGNVVKleARKVPHmGWNEVHPVKESPLLNGIDEGA 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489336581  123 VATRYHSLIVKPETLpscfTVTAQTKEGEIMAIRHNDLPIEGVQFHPESIMTsFGKEMLRNFIE 186
Cdd:TIGR01855 137 YFYFVHSYYAVCEEE----AVLAYADYGEKFPAAVQKGNIFGTQFHPEKSGK-TGLKLLENFLE 195
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 63-170 6.41e-07

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: 47.86  E-value: 6.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  63 LEAIKHF-AGKIPIFGVCLGHQSIAQVFGG----DV--VRAERLMHGKTSDIEHDGKTI-------FEGL--KNPLVATR 126
Cdd:COG2071   86 LALIRAAlERGKPVLGICRGMQLLNVALGGtlyqDLpdQVPGALDHRQPAPRYAPRHTVeiepgsrLARIlgEEEIRVNS 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489336581 127 YHSLIVKpeTLPSCFTVTAQTKEGEIMAIRHNDLP-IEGVQFHPE 170
Cdd:COG2071  166 LHHQAVK--RLGPGLRVSARAPDGVIEAIESPGAPfVLGVQWHPE 208
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 72-170 6.58e-07

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: 47.64  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   72 KIPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFE-----------------GLKNPLVATRYHSLIvkp 134
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREHCQVAPYApshavnvepgsllasllGSEEFRVNSLHHQAI--- 181

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489336581  135 ETLPSCFTVTAQTKEGEIMAIRH--NDLPIEGVQFHPE 170
Cdd:pfam07722 182 DRLAPGLRVEAVAPDGTIEAIESpnAKGFALGVQWHPE 219
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-186 4.40e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 45.24  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581   1 MILMID----NYDSFtYNLVQYLGElgeELVVKrndsitiDEIEELSPDFLMISPGPCSPDEAGISL------EAIK-HF 69
Cdd:PRK13181   1 MIAIIDygagNLRSV-ANALKRLGV---EAVVS-------SDPEEIAGADKVILPGVGAFGQAMRSLresgldEALKeHV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  70 AGKIPIFGVCLGHQSIAQ-----------VFGGDVVR----AERLMHGKTSDIEHDGK-TIFEGLKNPlvaTRY---HSL 130
Cdd:PRK13181  70 EKKQPVLGICLGMQLLFEsseegnvkglgLIPGDVKRfrsePLKVPQMGWNSVKPLKEsPLFKGIEEG---SYFyfvHSY 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489336581 131 IVKPETLPScftVTAQTKEGEIM--AIRHNDlpIEGVQFHPE-SimTSFGKEMLRNFIE 186
Cdd:PRK13181 147 YVPCEDPED---VLATTEYGVPFcsAVAKDN--IYAVQFHPEkS--GKAGLKLLKNFAE 198
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 64-185 8.45e-06

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 44.41  E-value: 8.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  64 EAIKHFAGK-IPIFGVCLGHQSIAQ------------VFGGDVVRAERLMHGK-------TSDIEHDGKTIFEGLKNPLV 123
Cdd:cd01748   62 EALKEAIASgKPFLGICLGMQLLFEsseegggtkglgLIPGKVVRFPASEGLKvphmgwnQLEITKESPLFKGIPDGSYF 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489336581 124 atrY--HSLIVKPEtlpSCFTVTAQTKEGEIM--AIRHNdlPIEGVQFHPE-SimTSFGKEMLRNFI 185
Cdd:cd01748  142 ---YfvHSYYAPPD---DPDYILATTDYGGKFpaAVEKD--NIFGTQFHPEkS--GKAGLKLLKNFL 198
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 72-186 2.96e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 42.93  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  72 KIPIFGVCLGHQSIAQ------------VFGGDVVR---AERLMH-G-KTSDIEHDGkTIFEGLKNPLVatrY--HSLIV 132
Cdd:PRK13143  71 GKPFLGICLGMQLLFEsseegggvrglgLFPGRVVRfpaGVKVPHmGwNTVKVVKDC-PLFEGIDGEYV---YfvHSYYA 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489336581 133 KPEtlpSCFTVTAQTKEGEIMAIRHNDLPIEGVQFHPE-SIMTsfGKEMLRNFIE 186
Cdd:PRK13143 147 YPD---DEDYVVATTDYGIEFPAAVCNDNVFGTQFHPEkSGET--GLKILENFVE 196
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 36-188 1.57e-04

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 41.02  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  36 IDEIEELSPDFLMISPGPCSPDEAGISLE------AIKHF-AGKIPIFGVCLGHQSIAQ-----------VFGGDVvraE 97
Cdd:CHL00188  31 INSESELAQVHALVLPGVGSFDLAMKKLEkkglitPIKKWiAEGNPFIGICLGLHLLFEtseegkeeglgIYKGQV---K 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  98 RLMHGKTSDIEHDG---------KTIFEGLKN----PLVATRY--HSLIVKPETlPSCFTVTAQTKEGEIMA-IRHNDlp 161
Cdd:CHL00188 108 RLKHSPVKVIPHMGwnrlecqnsECQNSEWVNwkawPLNPWAYfvHSYGVMPKS-QACATTTTFYGKQQMVAaIEYDN-- 184

                        170       180
                 ....*....|....*....|....*..
gi 489336581 162 IEGVQFHPESiMTSFGKEMLRNFIETY 188
Cdd:CHL00188 185 IFAMQFHPEK-SGEFGLWLLREFMKKA 210
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 64-187 2.83e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 40.15  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  64 EAIKHFA---GKiPIFGVCLGHQSIAQ------------VFGGDVVR----AERL----MHGKTSDIEHDGkTIFEGLkn 120
Cdd:PRK13146  67 EAVIEAVlaaGR-PFLGICVGMQLLFErglehgdtpglgLIPGEVVRfqpdGPALkvphMGWNTVDQTRDH-PLFAGI-- 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581 121 PLVATRY--HSLIVKPETLPSCFTVTaqTKEGEIMAIRHNDlPIEGVQFHPE-SimTSFGKEMLRNFIET 187
Cdd:PRK13146 143 PDGARFYfvHSYYAQPANPADVVAWT--DYGGPFTAAVARD-NLFATQFHPEkS--QDAGLALLRNFLAW 207
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 74-189 8.66e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 38.79  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336581  74 PIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIE-HDgktifEGLKNPLVAtryhslivkpeTLPSCF---TVTAQT-- 147
Cdd:PRK09065  90 PLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVElHP-----AAADDPLFA-----------GLPAQFpahLTHLQSvl 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489336581 148 --KEGEIM----------AIRHNDlPIEGVQFHPEsimtsFGKEMLRNFIETYR 189
Cdd:PRK09065 154 rlPPGAVVlarsaqdphqAFRYGP-HAWGVQFHPE-----FTAHIMRAYLRARA 201
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 35-93 2.86e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 37.25  E-value: 2.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489336581  35 TIDEIeelspDFLMISPGPCSPDE-----------AGISL--EAIKhfAGKIpIFGVCLGHQSIAQVFGGDV 93
Cdd:PRK08250  42 NADGF-----DLLIVMGGPQSPRTtreecpyfdskAEQRLinQAIK--AGKA-VIGVCLGAQLIGEALGAKY 105
 
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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