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Conserved domains on  [gi|15833465|ref|NP_312238|]
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aminodeoxychorismate synthase subunit II [Escherichia coli O157:H7 str. Sakai]

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 5.62e-148

aminodeoxychorismate synthase component 2;


:

Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 407.77  E-value: 5.62e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 15833465  161 DLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 5.62e-148

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 407.77  E-value: 5.62e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 15833465  161 DLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-185 6.45e-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: 394.79  E-value: 6.45e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:COG0512   1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQWD 161
Cdd:COG0512  81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                       170       180
                ....*....|....*....|....
gi 15833465 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:COG0512 161 IEGVQFHPESILTEHGHQLLANFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 8.68e-130

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: 361.80  E-value: 8.68e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465     1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETR-EIMGIRHRQ 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 15833465   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 4.28e-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: 332.19  E-value: 4.28e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:cd01743   1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQWD 161
Cdd:cd01743  81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                       170       180
                ....*....|....*....|....
gi 15833465 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:cd01743 161 IYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.51e-77

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 229.05  E-value: 2.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465     3 LLIDNYDSFTWNLYQYFCELGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAG-RLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    82 HQAMAQAFGGKVVRA-AKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSET-REIMGIRHRQ 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENdGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 15833465   160 WDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 1.45e-72

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 217.21  E-value: 1.45e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    5 IDNYDSFTWNLYQYFCE--LGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPD---EAGISLDVIRHYAGRLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   80 LGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEpdSLPACFEVTAWSETRE---IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15833465  157 HRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 5.62e-148

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 407.77  E-value: 5.62e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 15833465  161 DLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-185 6.45e-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: 394.79  E-value: 6.45e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:COG0512   1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQWD 161
Cdd:COG0512  81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                       170       180
                ....*....|....*....|....
gi 15833465 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:COG0512 161 IEGVQFHPESILTEHGHQLLANFL 184
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 1.44e-137

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 381.40  E-value: 1.44e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 15833465  161 DLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 8.68e-130

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: 361.80  E-value: 8.68e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465     1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETR-EIMGIRHRQ 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 15833465   160 WDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 1.17e-121

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 341.46  E-value: 1.17e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSE----TREIMGIR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSErggeMDEIMGIR 160

                        170       180
                 ....*....|....*....|....*....
gi 15833465  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 4.28e-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: 332.19  E-value: 4.28e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:cd01743   1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQWD 161
Cdd:cd01743  81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                       170       180
                ....*....|....*....|....
gi 15833465 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:cd01743 161 IYGVQFHPESILTEYGLRLLENFL 184
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-187 8.75e-117

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 329.14  E-value: 8.75e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETR-----EIMGI 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEdgsmdEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15833465  156 RHRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-186 1.91e-111

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 327.83  E-value: 1.91e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGAD-VLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   80 LGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQ 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180
                 ....*....|....*....|....*..
gi 15833465  160 WDLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:PRK14607 161 HPIFGVQFHPESILTEEGKRILKNFLN 187
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-185 2.15e-108

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 307.89  E-value: 2.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180
                 ....*....|....*....|....*
gi 15833465  161 DLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFI 185
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-185 7.57e-93

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 269.23  E-value: 7.57e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQ--KVVISPGPCTPDEAGISLDVIRHYAG-RLPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQfdGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHR 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|....*..
gi 15833465  159 QWDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK07765 163 ELPIHGVQFHPESVLTEGGHRMLANWL 189
trpG CHL00101
anthranilate synthase component 2
 1-185 8.21e-93

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 268.52  E-value: 8.21e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*.
gi 15833465  161 D-LEGVQFHPESILSEQGHQLLANFL 185
Cdd:CHL00101 161 KmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-185 1.52e-80

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 238.54  E-value: 1.52e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   82 HQAMAQAFGGKVVRAA-KVMHGKTSPITHN---GEGVFRGLANPLTVTRYHSLVVEPDSLPA-CFEVTAWSETREIMGIR 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPfGVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 15833465  157 HRQWD-LEGVQFHPESILSEQGHQLLANFL 185
Cdd:PLN02335 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.51e-77

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 229.05  E-value: 2.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465     3 LLIDNYDSFTWNLYQYFCELGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAG-RLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    82 HQAMAQAFGGKVVRA-AKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSET-REIMGIRHRQ 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENdGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 15833465   160 WDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 1.45e-72

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 217.21  E-value: 1.45e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    5 IDNYDSFTWNLYQYFCE--LGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPD---EAGISLDVIRHYAGRLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   80 LGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEpdSLPACFEVTAWSETRE---IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15833465  157 HRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
PRK13566 PRK13566
anthranilate synthase component I;
2-183 1.63e-55

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 186.28  E-value: 1.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRND-ALTLadIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGfAEEM--LDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNG-EGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQ 159
Cdd:PRK13566 607 GLQAIVEAFGGELGQLAYPMHGKPSRIRVRGpGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKT 686

                        170       180
                 ....*....|....*....|....*..
gi 15833465  160 WDLEGVQFHPESILS---EQGHQLLAN 183
Cdd:PRK13566 687 LPVAAVQFHPESIMTlggDVGLRIIEN 713
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-185 9.40e-51

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 170.98  E-value: 9.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRND--ALTLAD-IDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipAQTLIErLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVvePDSLPACFEVTAwSETREIMGIRHR 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160

                        170       180
                 ....*....|....*....|....*..
gi 15833465  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 4.25e-43

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


Pssm-ID: 130874 [Multi-domain]  Cd Length: 717  Bit Score: 152.35  E-value: 4.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465     2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNdALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRH-SHAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGV-FRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRVLGPDAlFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180       190
                  ....*....|....*....|....*....|
gi 15833465   161 DLEGVQFHPESILS---EQGHQLLANFLHR 187
Cdd:TIGR01815 678 PLAAVQFHPESIMTldgGAGLAMIGNVVDR 707
PRK06895 PRK06895
anthranilate synthase component II;
1-185 2.10e-36

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 125.23  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALkpQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENF--SHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEG-VFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQ 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*.
gi 15833465  160 WDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK06895 161 LPIYGVQFHPESYISEFGEQILRNWL 186
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 21-185 1.17e-35

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: 123.03  E-value: 1.17e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  21 ELGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVM 100
Cdd:cd01742  20 ELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKRE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465 101 HGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEpdSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQL 180
Cdd:cd01742  99 YGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVV--KLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKEI 176


                ....*
gi 15833465 181 LANFL 185
Cdd:cd01742 177 LKNFL 181
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 1.54e-35

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 131.51  E-value: 1.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    3 LLIDNYDSFTWNLYQyfcEL----GADVLVKRNDALTLADI-----DALKPQKVVISPGPCTP---DEAGISLDVIRHyA 70
Cdd:PLN02889  85 LLIDNYDSYTYNIYQ---ELsivnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLLLE-C 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   71 GRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVF----RGLANPLTVTRYHSLVVEPDSLPACFEVTAW 146
Cdd:PLN02889 161 RDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKELVPIAW 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  147 ---SETRE--------------------------------------------------IMGIRHRQWDLEGVQFHPESIL 173
Cdd:PLN02889 241 tssSDTLSflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIA 320

                        250
                 ....*....|.
gi 15833465  174 SEQGHQLLANF 184
Cdd:PLN02889 321 TCYGRQIFKNF 331
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-177 1.61e-34

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 120.72  E-value: 1.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNdALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   82 HQAMAQAFGGKvVRAAKVMHGKTSPITHNGEG----VFRGLA------NP------LTVTRYHSL--VVEPD---SLPAC 140
Cdd:PRK05637  83 FQALLEHHGGK-VEPCGPVHGTTDNMILTDAGvqspVFAGLAtdvepdHPeipgrkVPIARYHSLgcVVAPDgmeSLGTC 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15833465  141 F----EVTAWSETREIMGIrhrqwdleGVQFHPESILSEQG 177
Cdd:PRK05637 162 SseigPVIMAAETTDGKAI--------GLQFHPESVLSPTG 194
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-185 4.68e-32

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 113.79  E-value: 4.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDaLTLADIDALKpQKVVISPGPcTPDEAGISLDVIRHYagRLPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAFE-DGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEpdSLPACFEVTAWSETREIMGIRHRQW 160
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVK--ELPDGFEILARSDICEVEAMKHKEK 153

                        170       180
                 ....*....|....*....|....*
gi 15833465  161 DLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK00758 154 PIYGVQFHPEVAHTEYGEEIFKNFL 178
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-186 1.65e-31

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: 112.41  E-value: 1.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465     2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDAlTLADIDALKPQKVVISPGPCT--------PDEAGISLDVirhyagrl 73
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSSvyaenaprADEKIFELGV-------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    74 PILGVCLGHQAMAQAFGGKVVRAAKVMHGKTS-PITHNGEgVFRGLANPLTVTRYH-SLVVEpdsLPACFEVTAWSETRE 151
Cdd:TIGR00888  72 PVLGICYGMQLMAKQLGGEVGRAEKREYGKAElEILDEDD-LFRGLPDESTVWMSHgDKVKE---LPEGFKVLATSDNCP 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15833465   152 IMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:TIGR00888 148 VAAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-185 1.16e-28

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: 111.54  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465     2 ILLIDNYDSFTWNLYQYFcELGADVLVkrndALTLADIDALKPQ---------KVVISPGPCTPDEA---GISLDVIR-H 68
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLL-EQQTDISV----HVTTVHSDTFQDQllellplfdAIVVGPGPGNPNNAqdmGIISELWElA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    69 YAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANpLTVTRYHSLVVEPDS----LPACfeVT 144
Cdd:TIGR01823  83 NLDEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGidtlLPLC--LT 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 15833465   145 AWSETREIMGIRHRQWDLEGVQFHPESILSEQGH-QLLANFL 185
Cdd:TIGR01823 160 EDEEGIILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFL 201
guaA PRK00074
GMP synthase; Reviewed
 35-187 2.27e-28

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 110.14  E-value: 2.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   35 TLADIDALKPQKVVISPGPC--------TPDEAGISLDVirhyagrlPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSP 106
Cdd:PRK00074  38 SAEEIRAFNPKGIILSGGPAsvyeegapRADPEIFELGV--------PVLGICYGMQLMAHQLGGKVERAGKREYGRAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  107 ITHNGEGVFRGLANPLTVTRYHSLVVEpdSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
Cdd:PRK00074 110 EVDNDSPLFKGLPEEQDVWMSHGDKVT--ELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVF 187


                 .
gi 15833465  187 R 187
Cdd:PRK00074 188 D 188
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 2.89e-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: 96.03  E-value: 2.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  13 WNLYQYFCELGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCLGHQAMAQAFGG 91
Cdd:cd01744  10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  92 KVVRaakvM----HGKTSPITHNGEG-VFrglanplTVTRYHSLVVEPDSLPACFEVTAWS---ETREimGIRHRQWDLE 163
Cdd:cd01744  89 KTYK----MkfghRGSNHPVKDLITGrVY-------ITSQNHGYAVDPDSLPGGLEVTHVNlndGTVE--GIRHKDLPVF 155


                ....*...
gi 15833465 164 GVQFHPES 171
Cdd:cd01744 156 SVQFHPEA 163
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-187 4.44e-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: 96.94  E-value: 4.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   2 ILLID---NYDSFTWNLYQYFCELGADVLVKR--NDALTLADIDALKPQKVVISPGPCTPDEAGISL----DVIRH-YAG 71
Cdd:COG0518   2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLedepALIREaFEL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  72 RLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTsPIT-HNGEGVFRGLANPLTVtrYHSLVVEPDSLPACFEVTAWSETR 150
Cdd:COG0518  82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTV--WMSHGDTVTELPEGAEVLASSDNC 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833465 151 EIMGIRHRQWDLeGVQFHPE------------------------------SILSEQGHQLLANFLHR 187
Cdd:COG0518 159 PNQAFRYGRRVY-GVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 23-170 4.09e-19

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 83.02  E-value: 4.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   23 GADVLVKRNDAlTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHG 102
Cdd:PRK12838 189 GCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRG 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833465  103 KTSPIT-HNGEGVFrglanplTVTRYHSLVVEPDSLPacfeVTAWSET------REIMGIRHRQWDLEGVQFHPE 170
Cdd:PRK12838 268 ANHPVIdLTTGRVW-------MTSQNHGYVVDEDSLD----GTPLSVRffnvndGSIEGLRHKKKPVLSVQFHPE 331
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
19-171 1.41e-18

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 81.66  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   19 FCELGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCLGHQAMAQAFGGKVV--- 94
Cdd:PRK12564 195 LAERGCRVTVVPATT-TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKkIPIFGICLGHQLLALALGAKTYkmk 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   95 ---RAA----------KVMhgktspIT-HNgegvfrglanpltvtryHSLVVEPDSLPACFEVTAWS---ETreIMGIRH 157
Cdd:PRK12564 274 fghRGAnhpvkdletgKVE------ITsQN-----------------HGFAVDEDSLPANLEVTHVNlndGT--VEGLRH 328

                        170
                 ....*....|....
gi 15833465  158 RQWDLEGVQFHPES 171
Cdd:PRK12564 329 KDLPAFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 36-185 7.74e-18

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 80.11  E-value: 7.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   36 LADIDALKPQKVVISPGPCTPDEAGIS------LDVIRhyAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITH 109
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPHSVHVEGAPtvpegfFDYCR--ERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833465  110 NGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PLN02347 124 CGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 21-171 1.38e-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: 1.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  21 ELGADVLVKRNDAlTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCLGHQAMAQAFGGKVV----- 94
Cdd:COG0505 196 ERGCRVTVVPATT-SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYklkfg 274

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  95 -RAA----------KVMhgktspIT-HNgegvfrglanpltvtryHSLVVEPDSLPA-CFEVTAWS---ETREimGIRHR 158
Cdd:COG0505 275 hRGAnhpvkdletgRVE------ITsQN-----------------HGFAVDEDSLPAtDLEVTHVNlndGTVE--GLRHK 329

                       170
                ....*....|...
gi 15833465 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 4.27e-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: 74.97  E-value: 4.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  34 LTLADIDAlkpqkVVISPGPCTPDEAGIS-----LDVIRH-YAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPI 107
Cdd:cd01741  42 PDLDDYDG-----LVILGGPMSVDEDDYPwlkklKELIRQaLAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPV 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465 108 THNGEG----VFRGLANPLTVTRYHSLVVEpdSLPACFEVTAWSETREIMGIRHRQ--WdleGVQFHPEsilseqgHQLL 181
Cdd:cd01741 117 TLTEAGkadpLFAGLPDEFPVFHWHGDTVV--ELPPGAVLLASSEACPNQAFRYGDraL---GLQFHPE-------ERLL 184


                ....
gi 15833465 182 ANFL 185
Cdd:cd01741 185 RNFL 188
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 42-171 7.80e-15

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 71.55  E-value: 7.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   42 LKPQKVVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNgegvfrgLANP 121
Cdd:PLN02771 280 MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNN-------RTGR 352

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15833465  122 LTVT-RYHSLVVEPDSLPACFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
Cdd:PLN02771 353 VEISaQNHNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVMSLQYHPEA 404
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-91 9.69e-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: 56.45  E-value: 9.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   2 ILLIDNYDSFTW---NLYQYFCELGADVLVKRNDALTL-ADIDALKPQKVVISPGPCTPDEAGISLDVI----RHYAGRL 73
Cdd:cd01653   1 VAVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVeSDVDLDDYDGLILPGGPGTPDDLARDEALLallrEAAAAGK 80

                        90
                ....*....|....*...
gi 15833465  74 PILGVCLGHQAMAQAFGG 91
Cdd:cd01653  81 PILGICLGAQLLVLGVQF 98
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 1.05e-10

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 55.67  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   2 ILLIDNYDSFTW---NLYQYFCELGADV-LVKRNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVI----RHYAGRL 73
Cdd:cd03128   1 VAVLLFGGSEELelaSPLDALREAGAEVdVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLallrEAAAAGK 80

                        90
                ....*....|..
gi 15833465  74 PILGVCLGHQAM 85
Cdd:cd03128  81 PVLGICLGAQLL 92
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-171 3.05e-09

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 55.19  E-value: 3.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    2 ILLIDNydSFTWNLYQYFCELGADVLVKrNDALTLADIDALKPQKVVISPGPCTPDEAGISLDVIRHYAGR-LPILGVCL 80
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYnIPIFGICM 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   81 GHQAMAQAFGGKVVrAAKVMHgktspithngegvfRGLANPLTVTRY-------HSLVVEPDSL-PACFEVTAWS-ETRE 151
Cdd:CHL00197 272 GHQILSLALEAKTF-KLKFGH--------------RGLNHPSGLNQQveitsqnHGFAVNLESLaKNKFYITHFNlNDGT 336

                        170       180
                 ....*....|....*....|
gi 15833465  152 IMGIRHRQWDLEGVQFHPES 171
Cdd:CHL00197 337 VAGISHSPKPYFSVQYHPEA 356
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 72-180 8.11e-09

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 52.58  E-value: 8.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  72 RLPILGVCLGHQAMAQAFGGKVVRAakvmhgktspithngegvfrglanpLTVTRYHSLVVepDSLPACFEVTAWSETRE 151
Cdd:cd01745 100 GKPILGICRGMQLLNVALGGTLYQD-------------------------IRVNSLHHQAI--KRLADGLRVEARAPDGV 152

                        90       100       110
                ....*....|....*....|....*....|.
gi 15833465 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 2.27e-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: 49.18  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    72 RLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFrglaNPltvtrYHSLVVEPDS--------------- 136
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREHCQVAPY----AP-----SHAVNVEPGSllasllgseefrvns 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15833465   137 --------LPACFEVTAWSE--TRE-IMGIRHRQWDLeGVQFHPE 170
Cdd:pfam07722 176 lhhqaidrLAPGLRVEAVAPdgTIEaIESPNAKGFAL-GVQWHPE 219
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 69-170 2.91e-07

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 48.80  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   69 YAGRLPILGVCLGHQAMAQAFGGKVV-----RAAKVMHGKTSPITHNgEGVFRGLAN--PLTVTRYHSlVVEPdslPACF 141
Cdd:PRK09065  85 AAAGMPLLGICYGHQLLAHALGGEVGynpagRESGTVTVELHPAAAD-DPLFAGLPAqfPAHLTHLQS-VLRL---PPGA 159

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15833465  142 EVTAWSETREIMGIRHRQ--WdleGVQFHPE 170
Cdd:PRK09065 160 VVLARSAQDPHQAFRYGPhaW---GVQFHPE 187
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 26-185 3.42e-07

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


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 48.09  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    26 VLVKRNDALTLADidalkpqkVVISPGPCTPDEA-------GISLDVIRHYAGRLPILGVCLGHQAMAQA---------- 88
Cdd:TIGR01855  26 VVVKDSKEAELAD--------KLILPGVGAFGAAmarlrenGLDLFVELVVRLGKPVLGICLGMQLLFERseegggvpgl 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465    89 --FGGKVVR--AAKVMH-G-------KTSPIthngegvFRGLANPLTVTRYHSLVVEPDSLpacfEVTAWSETREIMGIR 156
Cdd:TIGR01855  98 glIKGNVVKleARKVPHmGwnevhpvKESPL-------LNGIDEGAYFYFVHSYYAVCEEE----AVLAYADYGEKFPAA 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 15833465   157 HRQWDLEGVQFHPE-SilSEQGHQLLANFL 185
Cdd:TIGR01855 167 VQKGNIFGTQFHPEkS--GKTGLKLLENFL 194
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 67-186 9.94e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 44.39  E-value: 9.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   67 RHYAGRlPILGVCLGHQAMAQA------------FGGKVVR------AAKVMH--------GKTSPithngegVFRGLAn 120
Cdd:PRK13146  73 VLAAGR-PFLGICVGMQLLFERglehgdtpglglIPGEVVRfqpdgpALKVPHmgwntvdqTRDHP-------LFAGIP- 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833465  121 plTVTRY---HSLVVEPDSlPAcfEVTAWSEtreimgirHRQW--------DLEGVQFHPE-SilSEQGHQLLANFLH 186
Cdd:PRK13146 144 --DGARFyfvHSYYAQPAN-PA--DVVAWTD--------YGGPftaavardNLFATQFHPEkS--QDAGLALLRNFLA 206
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 63-170 5.10e-05

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: 42.46  E-value: 5.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465  63 LDVIRH-YAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPitHNGEGVFRGLAnpltvtryHSLVVEPDS----- 136
Cdd:COG2071  86 LALIRAaLERGKPVLGICRGMQLLNVALGGTLYQDLPDQVPGALD--HRQPAPRYAPR--------HTVEIEPGSrlari 155

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15833465 137 ------------------LPACFEVTAWSETREIMGIRHR--QWDLeGVQFHPE 170
Cdd:COG2071 156 lgeeeirvnslhhqavkrLGPGLRVSARAPDGVIEAIESPgaPFVL-GVQWHPE 208
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 74-170 2.63e-04

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 40.33  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   74 PILGVCLGHQAMAQAFGGKVVRAAkvmHGKTS----PITHNGEGvfRGLAN-PLTVTRYHSlvvEPDSLPACFEVTAWSE 148
Cdd:PRK06490  88 PFLGICLGAQMLARHLGARVAPHP---DGRVEigyyPLRPTEAG--RALMHwPEMVYHWHR---EGFDLPAGAELLATGD 159

                         90       100
                 ....*....|....*....|....
gi 15833465  149 TREIMGIRH--RQWdleGVQFHPE 170
Cdd:PRK06490 160 DFPNQAFRYgdNAW---GLQFHPE 180
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 70-122 3.92e-04

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 39.93  E-value: 3.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15833465   70 AGRLPILGVCLGHQAMAQAFGGKVvraaKVMHGKT---SPITHNGEgvfrGLANPL 122
Cdd:PRK07053  81 AAGLPTLGICLGAQLIARALGARV----YPGGQKEigwAPLTLTDA----GRASPL 128
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 22-185 4.22e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 36.37  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   22 LGADVLVKRndaltlaDIDALKPQKVVISPGPCTPDEAGISL------DVIRhyAGRLPILGVCLGHQAMAQAFG-GKVV 94
Cdd:PRK13170  23 LGYEPVVSR-------DPDVILAADKLFLPGVGTAQAAMDQLrereliDLIK--ACTQPVLGICLGMQLLGERSEeSGGV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833465   95 RAAKVMHGKTS-------PITH---------NGEGVFRGLANPLTVTRYHSLVVEPD--SLPAC-----FevTAWSETRE 151
Cdd:PRK13170  94 DCLGIIDGPVKkmtdfglPLPHmgwnqvtpqAGHPLFQGIEDGSYFYFVHSYAMPVNeyTIAQCnygepF--SAAIQKDN 171

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15833465  152 IMGirhrqwdlegVQFHPE-SilSEQGHQLLANFL 185
Cdd:PRK13170 172 FFG----------VQFHPErS--GAAGAQLLKNFL 194
 
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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