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Conserved domains on  [gi|1586385892|gb|TBX59962|]
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aminodeoxychorismate/anthranilate synthase component II [Bacillus toyonensis]

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;
1-195 2.24e-148

aminodeoxychorismate/anthranilate synthase component II;


:

Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 409.58  E-value: 2.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1586385892 161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVASC 195
Cdd:PRK07649  161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVTSC 195
 
Name Accession Description Interval E-value
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-195 2.24e-148

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 409.58  E-value: 2.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1586385892 161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVASC 195
Cdd:PRK07649  161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVTSC 195
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-186 1.59e-139

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 386.70  E-value: 1.59e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTLP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*
gi 1586385892 162 IEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLE 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 5.24e-116

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: 327.18  E-value: 5.24e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTLP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 1586385892 162 IEGVQFHPESIMTSHGKELLQNFI 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 1.24e-109

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: 311.34  E-value: 1.24e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEG-EIMALRHTT 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 1586385892 160 LPIEGVQFHPESIMTSHGKELLQNFIRK 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 4.55e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 226.35  E-value: 4.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   3 LMIDNYDSFTFNLVQFLGELGQELVIKRNDEvTIADIENMKPDFLMISPGPCSPNEAGISMEAIKY-FAGKLPIFGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERL-MHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGE-IMALRHTT 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 1586385892 160 LPIEGVQFHPESIMTSHGKELLQNFIRK 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-186 7.21e-63

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 192.94  E-value: 7.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   5 IDNYDSFTFNLVQFLGELGQ--ELVIKRNdEVTIADIENMKPDFLMISPGPCSP-NE--AGISMEAIKYFAGKLPIFGVC 79
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkNDrdVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  80 LGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVkkETLPDCLEVTSWTE-EGE--IMALR 156
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDhDGEelVMGIR 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1586385892 157 HTTLPIEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:NF041322  159 HREHPIECVQFHPESVLTGVGHDVIENFLA 188
 
Name Accession Description Interval E-value
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-195 2.24e-148

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 409.58  E-value: 2.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1586385892 161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVASC 195
Cdd:PRK07649  161 PIEGVQFHPESIMTSHGKELLQNFIRKYSPSVTSC 195
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-186 1.59e-139

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 386.70  E-value: 1.59e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTLP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*
gi 1586385892 162 IEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLE 185
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 1.38e-135

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 376.78  E-value: 1.38e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*.
gi 1586385892 161 PIEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLE 186
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 5.24e-116

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: 327.18  E-value: 5.24e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTLP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 1586385892 162 IEGVQFHPESIMTSHGKELLQNFI 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 1.24e-109

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: 311.34  E-value: 1.24e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEG-EIMALRHTT 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 1586385892 160 LPIEGVQFHPESIMTSHGKELLQNFIRK 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-185 2.19e-108

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 320.51  E-value: 2.19e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELV-IKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVC 79
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGPEEIeVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  80 LGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTT 159
Cdd:PRK14607   81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                         170       180
                  ....*....|....*....|....*.
gi 1586385892 160 LPIEGVQFHPESIMTSHGKELLQNFI 185
Cdd:PRK14607  161 HPIFGVQFHPESILTEEGKRILKNFL 186
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-187 5.39e-103

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 294.86  E-value: 5.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK08857    1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTE--EG---EIMAL 155
Cdd:PRK08857   81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGsmdEIMGF 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1586385892 156 RHTTLPIEGVQFHPESIMTSHGKELLQNFIRK 187
Cdd:PRK08857  161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-186 2.29e-99

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 285.60  E-value: 2.29e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK06774    1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEG----EIMALR 156
Cdd:PRK06774   81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGgemdEIMGIR 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1586385892 157 HTTLPIEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:PRK06774  161 HRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 1.27e-97

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 281.04  E-value: 1.27e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK08007    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:PRK08007   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                         170       180
                  ....*....|....*....|....*..
gi 1586385892 161 PIEGVQFHPESIMTSHGKELLQNFIRK 187
Cdd:PRK08007  161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-185 3.17e-96

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 278.47  E-value: 3.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDF--LMISPGPCSPNEAGISMEAIKYFAG-KLPIFGV 78
Cdd:PRK07765    3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFdgVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  79 CLGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHT 158
Cdd:PRK07765   83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                         170       180
                  ....*....|....*....|....*..
gi 1586385892 159 TLPIEGVQFHPESIMTSHGKELLQNFI 185
Cdd:PRK07765  163 ELPIHGVQFHPESVLTEGGHRMLANWL 189
trpG CHL00101
anthranilate synthase component 2
 1-185 3.66e-91

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 264.67  E-value: 3.66e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:CHL00101    1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:CHL00101   81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                         170       180
                  ....*....|....*....|....*.
gi 1586385892 161 P-IEGVQFHPESIMTSHGKELLQNFI 185
Cdd:CHL00101  161 KmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-186 7.27e-89

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 260.11  E-value: 7.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:PLN02335   21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAER-LMHGKTSPMHHDGK---TIFSDIPNPFTATRYHSLIVKKETLP-DCLEVTSWTEEGEIMALR 156
Cdd:PLN02335  101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDEKgeeGLFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTEDGLIMAAR 180

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1586385892 157 HTTLP-IEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:PLN02335  181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIK 211
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 4.55e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 226.35  E-value: 4.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   3 LMIDNYDSFTFNLVQFLGELGQELVIKRNDEvTIADIENMKPDFLMISPGPCSPNEAGISMEAIKY-FAGKLPIFGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERL-MHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGE-IMALRHTT 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 1586385892 160 LPIEGVQFHPESIMTSHGKELLQNFIRK 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-186 7.21e-63

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 192.94  E-value: 7.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   5 IDNYDSFTFNLVQFLGELGQ--ELVIKRNdEVTIADIENMKPDFLMISPGPCSP-NE--AGISMEAIKYFAGKLPIFGVC 79
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkNDrdVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  80 LGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVkkETLPDCLEVTSWTE-EGE--IMALR 156
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDhDGEelVMGIR 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1586385892 157 HTTLPIEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:NF041322  159 HREHPIECVQFHPESVLTGVGHDVIENFLA 188
PRK13566 PRK13566
anthranilate synthase component I;
2-190 2.29e-54

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 183.58  E-value: 2.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDeVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:PRK13566  529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLG 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPM-HHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:PRK13566  608 LQAIVEAFGGELGQLAYPMHGKPSRIrVRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKTL 687

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1586385892 161 PIEGVQFHPESIMT---SHGKELLQNFIRKYSP 190
Cdd:PRK13566  688 PVAAVQFHPESIMTlggDVGLRIIENVVRLLAG 720
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-182 2.15e-53

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 178.30  E-value: 2.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRND---EVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGV 78
Cdd:PRK09522    4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  79 CLGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIvkKETLPDCLEVTSwTEEGEIMALRHT 158
Cdd:PRK09522   84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160

                         170       180
                  ....*....|....*....|....
gi 1586385892 159 TLPIEGVQFHPESIMTSHGKELLQ 182
Cdd:PRK09522  161 ADRVCGFQFHPESILTTQGARLLE 184
PRK06895 PRK06895
anthranilate synthase component II;
1-185 6.15e-45

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 147.19  E-value: 6.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDEVTIADIENMKpdFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCL 80
Cdd:PRK06895    3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKT-IFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTT 159
Cdd:PRK06895   81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                         170       180
                  ....*....|....*....|....*.
gi 1586385892 160 LPIEGVQFHPESIMTSHGKELLQNFI 185
Cdd:PRK06895  161 LPIYGVQFHPESYISEFGEQILRNWL 186
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-194 2.74e-41

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: 147.72  E-value: 2.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDeVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRHS-HAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPMH-HDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTL 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRvLGPDALFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1586385892 161 PIEGVQFHPESIMT---SHGKELLQNFIRKYSPSVAS 194
Cdd:TIGR01815 678 PLAAVQFHPESIMTldgGAGLAMIGNVVDRLAAGALT 714
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 1.19e-40

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 146.15  E-value: 1.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   3 LMIDNYDSFTFNLVQFLGEL-GQELVIKRNDEVTIADI-----ENMKPDFLMISPGPCSPNEA---GISMEAIKYfAGKL 73
Cdd:PLN02889   85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPTCPadiGICLRLLLE-CRDI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  74 PIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIP----NPFTATRYHSLIVKKETLPDCLEVTSWT-- 147
Cdd:PLN02889  164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAESLPKELVPIAWTss 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892 148 --------------------------------------------------EEGEI-MALRHTTLPIEGVQFHPESIMTSH 176
Cdd:PLN02889  244 sdtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermQNGKIlMGIMHSTRPHYGLQFHPESIATCY 323


                  ....*...
gi 1586385892 177 GKELLQNF 184
Cdd:PLN02889  324 GRQIFKNF 331
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-186 1.34e-34

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: 120.88  E-value: 1.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDeVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKetLPDCLEVTSWTEEGEIMALRHTTLP 161
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDNCPVAAMAHEEKP 157

                         170       180
                  ....*....|....*....|....*
gi 1586385892 162 IEGVQFHPESIMTSHGKELLQNFIR 186
Cdd:TIGR00888 158 IYGVQFHPEVTHTEYGNELLENFVY 182
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-185 1.24e-33

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 118.03  E-value: 1.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   1 MILMIDNYDSFTFNLVQFLGELGQELVIKRNDeVTIADIENMKpDFLMISPGPcSPNEAGISMEAIKYFagKLPIFGVCL 80
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAFE-DGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  81 GHQSIAQVFGGEVVRAERLMHGKT--SPMHHDgkTIFSDIPNPFTATRYHSLIVKKetLPDCLEVTSWTEEGEIMALRHT 158
Cdd:PRK00758   76 GHQLIAKAFGGEVGRGEYGEYALVevEILDED--DILKGLPPEIRVWASHADEVKE--LPDGFEILARSDICEVEAMKHK 151

                         170       180
                  ....*....|....*....|....*..
gi 1586385892 159 TLPIEGVQFHPESIMTSHGKELLQNFI 185
Cdd:PRK00758  152 EKPIYGVQFHPEVAHTEYGEEIFKNFL 178
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 2-185 5.28e-33

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 116.48  E-value: 5.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNDEvTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:cd01742     1 ILILDFGSQYTHLIARRVRELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNPFTATRYHSLIVKKetLPDCLEVTSWTEEGEIMALRHTTLP 161
Cdd:cd01742    80 MQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDNCPVAAIANEEKK 157

                         170       180
                  ....*....|....*....|....
gi 1586385892 162 IEGVQFHPESIMTSHGKELLQNFI 185
Cdd:cd01742   158 IYGVQFHPEVTHTEKGKEILKNFL 181
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-185 1.04e-29

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: 115.00  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVikrndEVTIADIENMKPDFL---------MISPGPCSPNEA---GIsMEAIKYF 69
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLEQQTDISV-----HVTTVHSDTFQDQLLellplfdaiVVGPGPGNPNNAqdmGI-ISELWEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  70 AG--KLPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGKTIFSDIPNpFTATRYHSLIVKKETlPDCLEVTSWT 147
Cdd:TIGR01823  82 ANldEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEG-IDTLLPLCLT 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1586385892 148 EEGE---IMALRHTTLPIEGVQFHPESIMTSHGK-ELLQNFI 185
Cdd:TIGR01823 160 EDEEgiiLMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFL 201
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-189 8.20e-29

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 106.47  E-value: 8.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTFNLVQFLGELGQELVIKRNdEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLG 81
Cdd:PRK05637    4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  82 HQSIAQVFGGEvVRAERLMHGKTSPM------------HHDGKTIFSDIPNP----FTATRYHSLIVKKetLPDCLEV-- 143
Cdd:PRK05637   83 FQALLEHHGGK-VEPCGPVHGTTDNMiltdagvqspvfAGLATDVEPDHPEIpgrkVPIARYHSLGCVV--APDGMESlg 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1586385892 144 TSWTEEGE-IMALRHTTLPIEGVQFHPESIMTSHGKELLQNFIRKYS 189
Cdd:PRK05637  160 TCSSEIGPvIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQLL 206
guaA PRK00074
GMP synthase; Reviewed
 33-187 3.99e-24

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 98.20  E-value: 3.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  33 EVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSPMHHDGK 112
Cdd:PRK00074   36 DISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDS 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586385892 113 TIFSDIPNPFTATRYHSLIVKKetLPDCLEVTSWTEEGEIMALRHTTLPIEGVQFHPESIMTSHGKELLQNFIRK 187
Cdd:PRK00074  116 PLFKGLPEEQDVWMSHGDKVTE--LPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVFD 188
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-187 1.15e-22

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: 90.78  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFTF---NLVQFLGELGQELVIKR--NDEVTIADIENMKPDFLMISPGPCSPNEAGISMEA----IKY-FAG 71
Cdd:COG0518     2 ILILDHDPFGGQypgLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDepalIREaFEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  72 KLPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTsPMH-HDGKTIFSDIPNPFTATRYHSLIVkkETLPDCLEVTSWTEEG 150
Cdd:COG0518    82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTVWMSHGDTV--TELPEGAEVLASSDNC 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586385892 151 EIMALRHTTlPIEGVQFHPE------------------------------SIMTSHGKELLQNFIRK 187
Cdd:COG0518   159 PNQAFRYGR-RVYGVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 35-171 6.24e-21

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: 84.86  E-value: 6.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  35 TIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGK-LPIFGVCLGHQSIAQVFGGEVVRaerlM----HGKTSPM-H 108
Cdd:cd01744    31 DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGAKTYK----MkfghRGSNHPVkD 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586385892 109 HDGKTIfsdipnpFTATRYHSLIVKKETLPDCLEVTSW-----TEEGeimaLRHTTLPIEGVQFHPES 171
Cdd:cd01744   107 LITGRV-------YITSQNHGYAVDPDSLPGGLEVTHVnlndgTVEG----IRHKDLPVFSVQFHPEA 163
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
35-171 7.78e-20

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 85.51  E-value: 7.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  35 TIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAG-KLPIFGVCLGHQSIAQVFGGEVVraeRLMHGktspmHH---- 109
Cdd:PRK12564  210 TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEkKIPIFGICLGHQLLALALGAKTY---KMKFG-----HRganh 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892 110 ---DGKTIFSDIpnpftATRYHSLIVKKETLPDCLEVTSW-----TEEGeimaLRHTTLPIEGVQFHPES 171
Cdd:PRK12564  282 pvkDLETGKVEI-----TSQNHGFAVDEDSLPANLEVTHVnlndgTVEG----LRHKDLPAFSVQYHPEA 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 35-171 7.30e-19

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 82.76  E-value: 7.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  35 TIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGK-LPIFGVCLGHQSIAQVFGGEVVraeRLMHGktspmHH---- 109
Cdd:COG0505   209 SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTY---KLKFG-----HRganh 280

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586385892 110 ------DGKT-IFSDipNpftatryHSLIVKKETLPD-CLEVT-----SWTEEGeimaLRHTTLPIEGVQFHPES 171
Cdd:COG0505   281 pvkdleTGRVeITSQ--N-------HGFAVDEDSLPAtDLEVThvnlnDGTVEG----LRHKDLPAFSVQYHPEA 342
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 24-170 1.44e-18

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 81.86  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  24 QELViKRNDEVTI-------ADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLGHQSIAQVFGGEVVRA 96
Cdd:PRK12838  183 RSLS-KRGCKVTVlpydtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKL 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586385892  97 ERLMHGKTSPM--HHDGKTifsdipnpFTATRYHSLIVKKETLPDCLEVTSWTE--EGEIMALRHTTLPIEGVQFHPE 170
Cdd:PRK12838  262 PFGHRGANHPVidLTTGRV--------WMTSQNHGYVVDEDSLDGTPLSVRFFNvnDGSIEGLRHKKKPVLSVQFHPE 331
PLN02347 PLN02347
GMP synthetase
 34-185 3.04e-18

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 81.65  E-value: 3.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  34 VTIADIENMKPDFLMISPGPCSPNEAG---ISMEAIKYFAGK-LPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSPMHH 109
Cdd:PLN02347   44 ASLDRIASLNPRVVILSGGPHSVHVEGaptVPEGFFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586385892 110 DGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMALRHTTLPIEGVQFHPESIMTSHGKELLQNFI 185
Cdd:PLN02347  124 CGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 42-171 7.29e-16

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 74.63  E-value: 7.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  42 MKPDFLMISPGPCSPNEAGISMEAIKYFAGKLPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSPMHHDgKTIFSDIpnp 121
Cdd:PLN02771  280 MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNN-RTGRVEI--- 355

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1586385892 122 ftATRYHSLIVKKETLPDCLEVTSWT-EEGEIMALRHTTLPIEGVQFHPES 171
Cdd:PLN02771  356 --SAQNHNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVMSLQYHPEA 404
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 45-185 3.23e-12

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 62.26  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  45 DFLMISPGPCSPNEAGIS-----MEAIKY-FAGKLPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSPMH--HDGKT--I 114
Cdd:cd01741    48 DGLVILGGPMSVDEDDYPwlkklKELIRQaLAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTltEAGKAdpL 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586385892 115 FSDIPNPFTATRYHSLIVkkETLPDCLEVTSWTEEGEIMALRhttlpIE----GVQFHPEsimtshgKELLQNFI 185
Cdd:cd01741   128 FAGLPDEFPVFHWHGDTV--VELPPGAVLLASSEACPNQAFR-----YGdralGLQFHPE-------ERLLRNFL 188
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-186 4.41e-10

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 57.88  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  13 FNLVQFLGELGQELVIKrNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAIKYFAG-KLPIFGVCLGHQSIAQVFGG 91
Cdd:CHL00197  204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  92 EVVraeRLMHGKTSPMHHDGKTIFSDIpnpftATRYHSLIVKKETL-PDCLEVTSWT-EEGEIMALRHTTLPIEGVQFHP 169
Cdd:CHL00197  283 KTF---KLKFGHRGLNHPSGLNQQVEI-----TSQNHGFAVNLESLaKNKFYITHFNlNDGTVAGISHSPKPYFSVQYHP 354

                         170
                  ....*....|....*...
gi 1586385892 170 ESIMTSHGKE-LLQNFIR 186
Cdd:CHL00197  355 EASPGPHDADyLFEYFIE 372
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-170 1.04e-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: 55.27  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  63 MEAIKYF-AGKLPIFGVCLGHQSIAQVFGGevvraerlmhgktspmhhdgkTIFSDIpnpfTATRYHSLIVKKetLPDCL 141
Cdd:cd01745    90 LALLRAAlERGKPILGICRGMQLLNVALGG---------------------TLYQDI----RVNSLHHQAIKR--LADGL 142

                          90       100       110
                  ....*....|....*....|....*....|
gi 1586385892 142 EVTSWTEEGEIMALRHTTLP-IEGVQFHPE 170
Cdd:cd01745   143 RVEARAPDGVIEAIESPDRPfVLGVQWHPE 172
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-92 1.08e-09

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 53.76  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFT---FNLVQFLGELGQELVIKRNDEVTI-ADIENMKPDFLMISPGPCSPNEAGISMEAI----KYFAGKL 73
Cdd:cd01653     1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVeSDVDLDDYDGLILPGGPGTPDDLARDEALLallrEAAAAGK 80

                          90
                  ....*....|....*....
gi 1586385892  74 PIFGVCLGHQSIaqVFGGE 92
Cdd:cd01653    81 PILGICLGAQLL--VLGVQ 97
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 2.61e-09

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 52.20  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892   2 ILMIDNYDSFT---FNLVQFLGELGQEL-VIKRNDEVTIADIENMKPDFLMISPGPCSPNEAGISMEAI----KYFAGKL 73
Cdd:cd03128     1 VAVLLFGGSEElelASPLDALREAGAEVdVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLallrEAAAAGK 80

                          90
                  ....*....|..
gi 1586385892  74 PIFGVCLGHQSI 85
Cdd:cd03128    81 PVLGICLGAQLL 92
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 72-186 2.95e-08

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: 51.71  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  72 KLPIFGVCLGHQSIAQVFGG------EVVRAERLMHGKTSPMHHDGKTI-------FSDI--PNPFTATRYHSLIVKKet 136
Cdd:COG2071    96 GKPVLGICRGMQLLNVALGGtlyqdlPDQVPGALDHRQPAPRYAPRHTVeiepgsrLARIlgEEEIRVNSLHHQAVKR-- 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1586385892 137 LPDCLEVTSWTEEGEIMALRHTTLP-IEGVQFHPESiMTSHGKE---LLQNFIR 186
Cdd:COG2071   174 LGPGLRVSARAPDGVIEAIESPGAPfVLGVQWHPEW-LAASDPLsrrLFEAFVE 226
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 73-176 1.20e-07

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 49.96  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  73 LPIFGVCLGHQSIAQVFGGEV-----------VRAERLMHGKTSPMhhdgktiFSDIPNPFTATRYHSLIVKkeTLPDCL 141
Cdd:PRK09065   89 MPLLGICYGHQLLAHALGGEVgynpagresgtVTVELHPAAADDPL-------FAGLPAQFPAHLTHLQSVL--RLPPGA 159

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1586385892 142 EVTSWTEEGEIMALRHTTlPIEGVQFHPE---SIMTSH 176
Cdd:PRK09065  160 VVLARSAQDPHQAFRYGP-HAWGVQFHPEftaHIMRAY 196
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 64-170 8.59e-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: 8.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  64 EAIKyfAGKlPIFGVCLGHQSIAQVFGG--------EVVRAERLMH------GKTSPMHHDGKTIFSDIP--NPFTATRY 127
Cdd:pfam07722 100 AALA--RGK-PILGICRGFQLLNVALGGtlyqdiqeQPGFTDHREHcqvapyAPSHAVNVEPGSLLASLLgsEEFRVNSL 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1586385892 128 HSLIVKKetLPDCLEVTSWTEEGEIMALRHTTLP--IEGVQFHPE 170
Cdd:pfam07722 177 HHQAIDR--LAPGLRVEAVAPDGTIEAIESPNAKgfALGVQWHPE 219
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 72-186 8.94e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 35.59  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385892  72 KLPIFGVCLGHQSIAQV---FG---------GEVVRAE-----RLMH-GKTSPMHHDGKTIFSDIPNPFTATRYHSLIVK 133
Cdd:PRK13152   73 KKPILGICLGMQLFLERgyeGGvceglgfieGEVVKFEedlnlKIPHmGWNELEILKQSPLYQGIPEKSDFYFVHSFYVK 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1586385892 134 ketlpdCLE--VTSWTEEGEIMALRHTTLPIEGVQFHPESiMTSHGKELLQNFIR 186
Cdd:PRK13152  153 ------CKDefVSAKAQYGHKFVASLQKDNIFATQFHPEK-SQNLGLKLLENFAR 200
 
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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