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Conserved domains on  [gi|446524507|ref|WP_000601853|]
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MULTISPECIES: aminodeoxychorismate synthase component 2 [Enterobacteriaceae]

Protein Classification

aminodeoxychorismate synthase component II( domain architecture ID 10792999)

aminodeoxychorismate synthase component II is part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 1.72e-148

aminodeoxychorismate synthase component 2;


:

Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 408.92  E-value: 1.72e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 446524507 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 1.72e-148

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 408.92  E-value: 1.72e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 446524507 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-185 3.20e-143

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: 395.56  E-value: 3.20e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQWD 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....
gi 446524507 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 3.54e-129

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: 360.26  E-value: 3.54e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETR-EIMGIRHRQ 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 446524507  160 WDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 4.52e-118

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: 331.81  E-value: 4.52e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQWD 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 446524507 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.43e-77

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 229.05  E-value: 2.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507    3 LLIDNYDSFTWNLYQYFCELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAG-RLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   82 HQAMAQAFGGKVVRA-AKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSET-REIMGIRHRQ 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENdGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 446524507  160 WDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 3.12e-72

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 216.44  E-value: 3.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   5 IDNYDSFTWNLYQYFCE--LGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPD---EAGISLDVIRHYAGRLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  80 LGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEpdSLPECFEVTAWSETRE---IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446524507 157 HRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 1.72e-148

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 408.92  E-value: 1.72e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 446524507 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-185 3.20e-143

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: 395.56  E-value: 3.20e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQWD 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....
gi 446524507 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFL 184
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 1.87e-138

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 383.71  E-value: 1.87e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQW 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 446524507 161 DLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 3.54e-129

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: 360.26  E-value: 3.54e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETR-EIMGIRHRQ 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 446524507  160 WDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 7.95e-121

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 339.15  E-value: 7.95e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSE----TREIMGIR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSErggeMDEIMGIR 160

                        170       180
                 ....*....|....*....|....*....
gi 446524507 157 HRQWDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK06774 161 HRTLPLEGVQFHPESILSEQGHQLLDNFL 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 4.52e-118

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: 331.81  E-value: 4.52e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQWD 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 446524507 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-187 6.23e-117

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 329.53  E-value: 6.23e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETR-----EIMGI 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEdgsmdEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446524507 156 RHRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-186 3.22e-112

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 329.75  E-value: 3.22e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGAD-VLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  80 LGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQ 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180
                 ....*....|....*....|....*..
gi 446524507 160 WDLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:PRK14607 161 HPIFGVQFHPESILTEEGKRILKNFLN 187
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-185 1.02e-108

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 309.04  E-value: 1.02e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQW 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180
                 ....*....|....*....|....*
gi 446524507 161 DLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFI 185
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-185 2.13e-93

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 270.77  E-value: 2.13e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQ--KIVISPGPCTPDEAGISLDVIRHYAG-RLPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQfdGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHR 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|....*..
gi 446524507 159 QWDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK07765 163 ELPIHGVQFHPESVLTEGGHRMLANWL 189
trpG CHL00101
anthranilate synthase component 2
 1-185 3.72e-92

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 266.60  E-value: 3.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQW 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*.
gi 446524507 161 D-LEGVQFHPESILSEQGHQLLANFL 185
Cdd:CHL00101 161 KmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-185 2.43e-80

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 238.16  E-value: 2.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  82 HQAMAQAFGGKVVRAA-KVMHGKTSPITHN---GVGVFKGLANPLTVTRYHSLVVEPDSLPE-CFEVTAWSETREIMGIR 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPfGVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 446524507 157 HRQWD-LEGVQFHPESILSEQGHQLLANFL 185
Cdd:PLN02335 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.43e-77

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 229.05  E-value: 2.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507    3 LLIDNYDSFTWNLYQYFCELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAG-RLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   82 HQAMAQAFGGKVVRA-AKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSET-REIMGIRHRQ 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENdGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 446524507  160 WDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 3.12e-72

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 216.44  E-value: 3.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   5 IDNYDSFTWNLYQYFCE--LGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPD---EAGISLDVIRHYAGRLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  80 LGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEpdSLPECFEVTAWSETRE---IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446524507 157 HRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
PRK13566 PRK13566
anthranilate synthase component I;
2-183 8.88e-56

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 187.05  E-value: 8.88e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRND-ALTLadIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGfAEEM--LDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVG-VFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQ 159
Cdd:PRK13566 607 GLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKT 686

                        170       180
                 ....*....|....*....|....*..
gi 446524507 160 WDLEGVQFHPESILS---EQGHQLLAN 183
Cdd:PRK13566 687 LPVAAVQFHPESIMTlggDVGLRIIEN 713
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-185 1.90e-49

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 167.51  E-value: 1.90e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRND--ALTLAD-IDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipAQTLIErLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANPLTVTRYHSLVvePDSLPECFEVTAwSETREIMGIRHR 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160

                        170       180
                 ....*....|....*....|....*..
gi 446524507 159 QWDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTL 187
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-187 1.71e-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: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNdALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRH-SHAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGV-FKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQW 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRVLGPDAlFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180       190
                  ....*....|....*....|....*....|
gi 446524507  161 DLEGVQFHPESILS---EQGHQLLANFLHR 187
Cdd:TIGR01815 678 PLAAVQFHPESIMTldgGAGLAMIGNVVDR 707
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 21-185 2.18e-36

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: 124.57  E-value: 2.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  21 ELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVM 100
Cdd:cd01742   20 ELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKRE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507 101 HGKTSPITHNGVGVFKGLANPLTVTRYHSLVVEpdSLPECFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQL 180
Cdd:cd01742   99 YGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVV--KLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKEI 176


                 ....*
gi 446524507 181 LANFL 185
Cdd:cd01742  177 LKNFL 181
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 3.22e-36

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 133.43  E-value: 3.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   3 LLIDNYDSFTWNLYQyfcEL----GADVLVKRNDALTLADI-----DALKPQKIVISPGPCTP---DEAGISLDVIRHyA 70
Cdd:PLN02889  85 LLIDNYDSYTYNIYQ---ELsivnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLLLE-C 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  71 GRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVF----KGLANPLTVTRYHSLVVEPDSLPECFEVTAW 146
Cdd:PLN02889 161 RDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKELVPIAW 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507 147 ---SETRE--------------------------------------------------IMGIRHRQWDLEGVQFHPESIL 173
Cdd:PLN02889 241 tssSDTLSflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIA 320

                        250
                 ....*....|.
gi 446524507 174 SEQGHQLLANF 184
Cdd:PLN02889 321 TCYGRQIFKNF 331
PRK06895 PRK06895
anthranilate synthase component II;
1-185 4.72e-36

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 124.08  E-value: 4.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALkpQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENF--SHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKTSP-ITHNGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQ 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPlKVRSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*.
gi 446524507 160 WDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK06895 161 LPIYGVQFHPESYISEFGEQILRNWL 186
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-177 2.05e-35

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 123.03  E-value: 2.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNdALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  82 HQAMAQAFGGKvVRAAKVMHGKTSPITHNGVG----VFKGLA------NP------LTVTRYHSL--VVEPD---SLPEC 140
Cdd:PRK05637  83 FQALLEHHGGK-VEPCGPVHGTTDNMILTDAGvqspVFAGLAtdvepdHPeipgrkVPIARYHSLgcVVAPDgmeSLGTC 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446524507 141 F----EVTAWSETREIMGIrhrqwdleGVQFHPESILSEQG 177
Cdd:PRK05637 162 SseigPVIMAAETTDGKAI--------GLQFHPESVLSPTG 194
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-185 5.96e-33

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 116.10  E-value: 5.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDaLTLADIDALKpQKIVISPGPcTPDEAGISLDVIRHYagRLPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAFE-DGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVRAAKVMHGKT--SPITHNGVgvFKGLANPLTVTRYHSLVVEpdSLPECFEVTAWSETREIMGIRHR 158
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALVevEILDEDDI--LKGLPPEIRVWASHADEVK--ELPDGFEILARSDICEVEAMKHK 151

                        170       180
                 ....*....|....*....|....*..
gi 446524507 159 QWDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK00758 152 EKPIYGVQFHPEVAHTEYGEEIFKNFL 178
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-186 1.48e-32

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 115.10  E-value: 1.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDAlTLADIDALKPQKIVISPGPCT--------PDEAGISLDVirhyagrl 73
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSSvyaenaprADEKIFELGV-------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   74 PILGVCLGHQAMAQAFGGKVVRAAKVMHGKTS-PITHNGVgVFKGLANPLTVTRYH-SLVVEpdsLPECFEVTAWSETRE 151
Cdd:TIGR00888  72 PVLGICYGMQLMAKQLGGEVGRAEKREYGKAElEILDEDD-LFRGLPDESTVWMSHgDKVKE---LPEGFKVLATSDNCP 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446524507  152 IMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:TIGR00888 148 VAAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
guaA PRK00074
GMP synthase; Reviewed
 35-187 1.34e-29

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 113.22  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  35 TLADIDALKPQKIVISPGPC--------TPDEAGISLDVirhyagrlPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSP 106
Cdd:PRK00074  38 SAEEIRAFNPKGIILSGGPAsvyeegapRADPEIFELGV--------PVLGICYGMQLMAHQLGGKVERAGKREYGRAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507 107 ITHNGVGVFKGLANPLTVTRYHSLVVEpdSLPECFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:PRK00074 110 EVDNDSPLFKGLPEEQDVWMSHGDKVT--ELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVF 187


                 .
gi 446524507 187 R 187
Cdd:PRK00074 188 D 188
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-185 3.97e-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: 112.69  E-value: 3.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507    2 ILLIDNYDSFTWNLYQYFcELGADVLVkrndALTLADIDALKPQ---------KIVISPGPCTPDEA---GISLDVIR-H 68
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLL-EQQTDISV----HVTTVHSDTFQDQllellplfdAIVVGPGPGNPNNAqdmGIISELWElA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   69 YAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFKGLANpLTVTRYHSLVVEPDS----LPECfeVT 144
Cdd:TIGR01823  83 NLDEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGidtlLPLC--LT 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446524507  145 AWSETREIMGIRHRQWDLEGVQFHPESILSEQGH-QLLANFL 185
Cdd:TIGR01823 160 EDEEGIILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFL 201
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 1.60e-25

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: 96.80  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  13 WNLYQYFCELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCLGHQAMAQAFGG 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  92 KVVRaakvM----HGKTSPITHNGVG-VFkglanplTVTRYHSLVVEPDSLPECFEVTAWS---ETREimGIRHRQWDLE 163
Cdd:cd01744   89 KTYK----MkfghRGSNHPVKDLITGrVY-------ITSQNHGYAVDPDSLPGGLEVTHVNlndGTVE--GIRHKDLPVF 155


                 ....*...
gi 446524507 164 GVQFHPES 171
Cdd:cd01744  156 SVQFHPEA 163
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-187 2.59e-25

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: 97.32  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLID---NYDSFTWNLYQYFCELGADVLVKR--NDALTLADIDALKPQKIVISPGPCTPDEAGISL----DVIRH-YAG 71
Cdd:COG0518    2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLedepALIREaFEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  72 RLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTsPIT-HNGVGVFKGLANPLTVtrYHSLVVEPDSLPECFEVTAWSETR 150
Cdd:COG0518   82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTV--WMSHGDTVTELPEGAEVLASSDNC 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446524507 151 EIMGIRHRQWDLeGVQFHPE------------------------------SILSEQGHQLLANFLHR 187
Cdd:COG0518  159 PNQAFRYGRRVY-GVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 23-170 1.21e-19

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 84.56  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  23 GADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHG 102
Cdd:PRK12838 189 GCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRG 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446524507 103 KTSPITHNGVG-VFkglanplTVTRYHSLVVEPDSLPEcfevTAWSET------REIMGIRHRQWDLEGVQFHPE 170
Cdd:PRK12838 268 ANHPVIDLTTGrVW-------MTSQNHGYVVDEDSLDG----TPLSVRffnvndGSIEGLRHKKKPVLSVQFHPE 331
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
19-171 1.56e-18

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 81.66  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  19 FCELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCLGHQAMAQAFGGKVV--- 94
Cdd:PRK12564 195 LAERGCRVTVVPATT-TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKkIPIFGICLGHQLLALALGAKTYkmk 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  95 ---RAA----------KVMhgktspIT-HNgvgvfkglanpltvtryHSLVVEPDSLPECFEVTAWS---ETreIMGIRH 157
Cdd:PRK12564 274 fghRGAnhpvkdletgKVE------ITsQN-----------------HGFAVDEDSLPANLEVTHVNlndGT--VEGLRH 328

                        170
                 ....*....|....
gi 446524507 158 RQWDLEGVQFHPES 171
Cdd:PRK12564 329 KDLPAFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 36-185 1.86e-18

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 82.04  E-value: 1.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  36 LADIDALKPQKIVISPGPCTPDEAGIS------LDVIRhyAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITH 109
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPHSVHVEGAPtvpegfFDYCR--ERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446524507 110 NGVGVFKGLANPLTVTRYHSLVVEPDSLPECFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PLN02347 124 CGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 21-171 1.39e-17

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: 78.91  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  21 ELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCLGHQAMAQAFGGKVV----- 94
Cdd:COG0505  196 ERGCRVTVVPATT-SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYklkfg 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  95 -RAA----------KVMhgktspIT-HNgvgvfkglanpltvtryHSLVVEPDSLPE-CFEVTAWS---ETREimGIRHR 158
Cdd:COG0505  275 hRGAnhpvkdletgRVE------ITsQN-----------------HGFAVDEDSLPAtDLEVTHVNlndGTVE--GLRHK 329

                        170
                 ....*....|...
gi 446524507 159 QWDLEGVQFHPES 171
Cdd:COG0505  330 DLPAFSVQYHPEA 342
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 34-185 9.48e-17

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 74.20  E-value: 9.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  34 LTLADIDALkpqkiVISPGPCTPDEAGIS-----LDVIRH-YAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPI 107
Cdd:cd01741   42 PDLDDYDGL-----VILGGPMSVDEDDYPwlkklKELIRQaLAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507 108 THNGVG----VFKGLANPLTVTRYHSLVVEpdSLPECFEVTAWSETREIMGIRHRQ--WdleGVQFHPEsilseqgHQLL 181
Cdd:cd01741  117 TLTEAGkadpLFAGLPDEFPVFHWHGDTVV--ELPPGAVLLASSEACPNQAFRYGDraL---GLQFHPE-------ERLL 184


                 ....
gi 446524507 182 ANFL 185
Cdd:cd01741  185 RNFL 188
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 42-171 2.18e-15

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 73.09  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  42 LKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNgvgvfkgLANP 121
Cdd:PLN02771 280 MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNN-------RTGR 352

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446524507 122 LTVT-RYHSLVVEPDSLPECFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
Cdd:PLN02771 353 VEISaQNHNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVMSLQYHPEA 404
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-91 7.87e-11

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: 56.84  E-value: 7.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTW---NLYQYFCELGADVLVKRNDALTL-ADIDALKPQKIVISPGPCTPDEAGISLDVI----RHYAGRL 73
Cdd:cd01653    1 VAVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVeSDVDLDDYDGLILPGGPGTPDDLARDEALLallrEAAAAGK 80

                         90
                 ....*....|....*...
gi 446524507  74 PILGVCLGHQAMAQAFGG 91
Cdd:cd01653   81 PILGICLGAQLLVLGVQF 98
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 9.42e-11

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: 56.05  E-value: 9.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNYDSFTW---NLYQYFCELGADV-LVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVI----RHYAGRL 73
Cdd:cd03128    1 VAVLLFGGSEELelaSPLDALREAGAEVdVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLallrEAAAAGK 80

                         90
                 ....*....|..
gi 446524507  74 PILGVCLGHQAM 85
Cdd:cd03128   81 PVLGICLGAQLL 92
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-171 3.80e-10

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 57.88  E-value: 3.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   2 ILLIDNydSFTWNLYQYFCELGADVLVKrNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCL 80
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYnIPIFGICM 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  81 GHQAMAQAFGGKVVraaKVMHGktspitHNGVGVFKGLANPLTVT-RYHSLVVEPDSLPE-CFEVTAWS-ETREIMGIRH 157
Cdd:CHL00197 272 GHQILSLALEAKTF---KLKFG------HRGLNHPSGLNQQVEITsQNHGFAVNLESLAKnKFYITHFNlNDGTVAGISH 342

                        170
                 ....*....|....
gi 446524507 158 RQWDLEGVQFHPES 171
Cdd:CHL00197 343 SPKPYFSVQYHPEA 356
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 72-180 4.05e-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: 53.35  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  72 RLPILGVCLGHQAMAQAFGGKVVRAakvmhgktspithngvgvfkglanpLTVTRYHSLVVepDSLPECFEVTAWSETRE 151
Cdd:cd01745  100 GKPILGICRGMQLLNVALGGTLYQD-------------------------IRVNSLHHQAI--KRLADGLRVEARAPDGV 152

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446524507 152 IMGIRH--RQWDLeGVQFHPESILSEQGHQL 180
Cdd:cd01745  153 IEAIESpdRPFVL-GVQWHPEWLADTDPDSL 182
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 72-170 6.17e-08

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: 50.72  E-value: 6.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   72 RLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGVGVFkglaNPltvtrYHSLVVEPDS--------------- 136
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREHCQVAPY----AP-----SHAVNVEPGSllasllgseefrvns 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446524507  137 --------LPECFEVTAWSE--TRE-IMGIRHRQWDLeGVQFHPE 170
Cdd:pfam07722 176 lhhqaidrLAPGLRVEAVAPdgTIEaIESPNAKGFAL-GVQWHPE 219
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 26-185 1.05e-07

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 49.63  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   26 VLVKRNDALTLADidalkpqKIVIsPGPCTPDEA-------GISLDVIRHYAGRLPILGVCLGHQAMAQA---------- 88
Cdd:TIGR01855  26 VVVKDSKEAELAD-------KLIL-PGVGAFGAAmarlrenGLDLFVELVVRLGKPVLGICLGMQLLFERseegggvpgl 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507   89 --FGGKVVR--AAKVMH---GKTSPIThnGVGVFKGLANPLTVTRYHSLVVEpdslPECFEVTAWSETREIMGIRHRQWD 161
Cdd:TIGR01855  98 glIKGNVVKleARKVPHmgwNEVHPVK--ESPLLNGIDEGAYFYFVHSYYAV----CEEEAVLAYADYGEKFPAAVQKGN 171

                         170       180
                  ....*....|....*....|....*
gi 446524507  162 LEGVQFHPE-SilSEQGHQLLANFL 185
Cdd:TIGR01855 172 IFGTQFHPEkS--GKTGLKLLENFL 194
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 69-170 1.77e-06

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 46.49  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  69 YAGRLPILGVCLGHQAMAQAFGGKVV-----RAAKVMHGKTSPithNGVG--VFKGLAN--PLTVTRYHSlVVEPdslPE 139
Cdd:PRK09065  85 AAAGMPLLGICYGHQLLAHALGGEVGynpagRESGTVTVELHP---AAADdpLFAGLPAqfPAHLTHLQS-VLRL---PP 157

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446524507 140 CFEVTAWSETREIMGIRHRQ--WdleGVQFHPE 170
Cdd:PRK09065 158 GAVVLARSAQDPHQAFRYGPhaW---GVQFHPE 187
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 67-186 6.44e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 44.77  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  67 RHYAGRlPILGVCLGHQAMAQA------------FGGKVVR------AAKVMH-G-KTSPITHNGVgVFKGLAnplTVTR 126
Cdd:PRK13146  73 VLAAGR-PFLGICVGMQLLFERglehgdtpglglIPGEVVRfqpdgpALKVPHmGwNTVDQTRDHP-LFAGIP---DGAR 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446524507 127 Y---HSLVVEPDSLPEcfeVTAWSEtreimgirHRQW--------DLEGVQFHPE-SilSEQGHQLLANFLH 186
Cdd:PRK13146 148 FyfvHSYYAQPANPAD---VVAWTD--------YGGPftaavardNLFATQFHPEkS--QDAGLALLRNFLA 206
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 64-185 9.38e-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: 44.03  E-value: 9.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  64 DVIRHYA--GRlPILGVCLGHQAMAQA------------FGGKVVR-----AAKVMH--------GKTSPIthngvgvFK 116
Cdd:cd01748   62 EALKEAIasGK-PFLGICLGMQLLFESseegggtkglglIPGKVVRfpaseGLKVPHmgwnqleiTKESPL-------FK 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446524507 117 GLANPLTVtrY--HSLVVEPDslpECFEVTAWSETREIM--GIRHRqwDLEGVQFHPE-SilSEQGHQLLANFL 185
Cdd:cd01748  134 GIPDGSYF--YfvHSYYAPPD---DPDYILATTDYGGKFpaAVEKD--NIFGTQFHPEkS--GKAGLKLLKNFL 198
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 70-122 1.02e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 38.39  E-value: 1.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446524507  70 AGRLPILGVCLGHQAMAQAFGGKVvraaKVMHGKT---SPITHNGvgvfKGLANPL 122
Cdd:PRK07053  81 AAGLPTLGICLGAQLIARALGARV----YPGGQKEigwAPLTLTD----AGRASPL 128
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 74-185 1.68e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 37.90  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  74 PILGVCLGHQAMAQ---AFG---------GKVVR-----AAKVMHGKTSPITH-NGVGVFKGLANPLTVTRYHSLVVepd 135
Cdd:PRK13152  75 PILGICLGMQLFLErgyEGGvceglgfieGEVVKfeedlNLKIPHMGWNELEIlKQSPLYQGIPEKSDFYFVHSFYV--- 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446524507 136 slpECFE--VTAWSETREIMGIRHRQWDLEGVQFHPESILSeQGHQLLANFL 185
Cdd:PRK13152 152 ---KCKDefVSAKAQYGHKFVASLQKDNIFATQFHPEKSQN-LGLKLLENFA 199
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 74-170 2.78e-03

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 37.25  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  74 PILGVCLGHQAMAQAFGGKVVRAAkvmHGKTS----PITHNGVGvfKGLAN-PLTVTRYHSlvvEPDSLPECFEVTAWSE 148
Cdd:PRK06490  88 PFLGICLGAQMLARHLGARVAPHP---DGRVEigyyPLRPTEAG--RALMHwPEMVYHWHR---EGFDLPAGAELLATGD 159

                         90       100
                 ....*....|....*....|....
gi 446524507 149 TREIMGIRH--RQWdleGVQFHPE 170
Cdd:PRK06490 160 DFPNQAFRYgdNAW---GLQFHPE 180
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 74-185 5.26e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 36.38  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446524507  74 PILGVCLGHQAMAQA------------FGGKVVR---AAKVMH-G-------KTSPIthngvgvFKGLANpltvtRY--- 127
Cdd:PRK13143  73 PFLGICLGMQLLFESseegggvrglglFPGRVVRfpaGVKVPHmGwntvkvvKDCPL-------FEGIDG-----EYvyf 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446524507 128 -HSLVVEPDSlPECF--------EVTAWSETREIMgirhrqwdleGVQFHPE-SilSEQGHQLLANFL 185
Cdd:PRK13143 141 vHSYYAYPDD-EDYVvattdygiEFPAAVCNDNVF----------GTQFHPEkS--GETGLKILENFV 195
 
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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