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Conserved domains on  [gi|695713285|ref|WP_032644554|]
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aminodeoxychorismate synthase component 2 [Enterobacter chengduensis]

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 4.36e-144

aminodeoxychorismate synthase component 2;


:

Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 397.75  E-value: 4.36e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 695713285 161 DLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 4.36e-144

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 397.75  E-value: 4.36e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 695713285 161 DLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-185 1.51e-140

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: 389.01  E-value: 1.51e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  82 HQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREWD 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....
gi 695713285 162 LEGVQFHPESILSEQGHDLLANFL 185
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 6.33e-118

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: 331.75  E-value: 6.33e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285    1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDT-QEIMGIRHRE 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEEnIEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 695713285  160 WDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 5.76e-116

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 326.80  E-value: 5.76e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  82 HQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREWD 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 695713285 162 LEGVQFHPESILSEQGHDLLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.88e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 226.35  E-value: 2.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285    3 LLIDNYDSFTWNLYQYFCELGAEVVVRRNDEiELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAG-KLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   82 HQAIAQAFGATIVRA-AKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDT-QEIMGIRHRE 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENdGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 695713285  160 WDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 2.99e-69

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 208.73  E-value: 2.99e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   5 IDNYDSFTWNLYQYFCE--LGAEVVVRRNdEIELADIETLAPQKIVISPGPCTPS---ESGVSLEVIRHYAGKLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  80 LGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDppTLPACFEVTAWSD---TQEIMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDhdgEELVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 695713285 157 HREWDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 4.36e-144

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 397.75  E-value: 4.36e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 695713285 161 DLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-185 1.51e-140

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: 389.01  E-value: 1.51e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  82 HQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREWD 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....
gi 695713285 162 LEGVQFHPESILSEQGHDLLANFL 185
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFL 184
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 6.49e-136

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 377.16  E-value: 6.49e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 695713285 161 DLEGVQFHPESILSEQGHDLLANFLH 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 3.17e-120

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 337.99  E-value: 3.17e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSD----TQEIMGIR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSErggeMDEIMGIR 160

                        170       180
                 ....*....|....*....|....*....
gi 695713285 157 HREWDLEGVQFHPESILSEQGHDLLANFL 185
Cdd:PRK06774 161 HRTLPLEGVQFHPESILSEQGHQLLDNFL 189
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 6.33e-118

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: 331.75  E-value: 6.33e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285    1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDT-QEIMGIRHRE 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEEnIEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 695713285  160 WDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 5.76e-116

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 326.80  E-value: 5.76e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  82 HQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREWD 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 695713285 162 LEGVQFHPESILSEQGHDLLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-187 4.34e-114

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 322.21  E-value: 4.34e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQ-----EIMGI 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEdgsmdEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 695713285 156 RHREWDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-186 1.45e-110

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 325.52  E-value: 1.45e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVV-VRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEEIeVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  80 LGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHRE 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180
                 ....*....|....*....|....*..
gi 695713285 160 WDLEGVQFHPESILSEQGHDLLANFLH 186
Cdd:PRK14607 161 HPIFGVQFHPESILTEEGKRILKNFLN 187
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-185 3.11e-105

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 300.18  E-value: 3.11e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180
                 ....*....|....*....|....*
gi 695713285 161 DLEGVQFHPESILSEQGHDLLANFL 185
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFI 185
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-185 8.20e-94

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 271.92  E-value: 8.20e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQ--KIVISPGPCTPSESGVSLEVIRHYAG-KLPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQfdGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  79 CLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHR 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|....*..
gi 695713285 159 EWDLEGVQFHPESILSEQGHDLLANFL 185
Cdd:PRK07765 163 ELPIHGVQFHPESVLTEGGHRMLANWL 189
trpG CHL00101
anthranilate synthase component 2
 1-185 7.68e-88

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 255.81  E-value: 7.68e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*.
gi 695713285 161 D-LEGVQFHPESILSEQGHDLLANFL 185
Cdd:CHL00101 161 KmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-185 8.61e-78

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 231.61  E-value: 8.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  82 HQAIAQAFGATIVRAA-KVMHGKTSPVTHT---GTGVFTGLNNPLTVTRYHSLVIDPPTLPA-CFEVTAWSDTQEIMGIR 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPfGVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 695713285 157 HREWD-LEGVQFHPESILSEQGHDLLANFL 185
Cdd:PLN02335 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.88e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 226.35  E-value: 2.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285    3 LLIDNYDSFTWNLYQYFCELGAEVVVRRNDEiELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAG-KLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   82 HQAIAQAFGATIVRA-AKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDT-QEIMGIRHRE 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENdGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 695713285  160 WDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-187 2.99e-69

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 208.73  E-value: 2.99e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   5 IDNYDSFTWNLYQYFCE--LGAEVVVRRNdEIELADIETLAPQKIVISPGPCTPS---ESGVSLEVIRHYAGKLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  80 LGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDppTLPACFEVTAWSD---TQEIMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDhdgEELVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 695713285 157 HREWDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAA 189
PRK13566 PRK13566
anthranilate synthase component I;
2-183 5.53e-54

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 182.42  E-value: 5.53e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIElADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAE-EMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLG 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  82 HQAIAQAFGATIVRAAKVMHGKTSPVTHTG-TGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:PRK13566 608 LQAIVEAFGGELGQLAYPMHGKPSRIRVRGpGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKTL 687

                        170       180
                 ....*....|....*....|....*.
gi 695713285 161 DLEGVQFHPESILS---EQGHDLLAN 183
Cdd:PRK13566 688 PVAAVQFHPESIMTlggDVGLRIIEN 713
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-185 1.60e-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: 1.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLAPQK---IVISPGPCTPSESGVSLEVIRHYAGKLPILGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSnpvLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  79 CLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVidPPTLPACFEVTAwSDTQEIMGIRHR 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160

                        170       180
                 ....*....|....*....|....*..
gi 695713285 159 EWDLEGVQFHPESILSEQGHDLLANFL 185
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTL 187
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-187 2.31e-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: 150.42  E-value: 2.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285    2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELAdIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRHSHAEAA-FDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   82 HQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGV-FTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRVLGPDAlFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180       190
                  ....*....|....*....|....*....|
gi 695713285  161 DLEGVQFHPESILS---EQGHDLLANFLHR 187
Cdd:TIGR01815 678 PLAAVQFHPESIMTldgGAGLAMIGNVVDR 707
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 3.77e-38

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 138.83  E-value: 3.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   3 LLIDNYDSFTWNLYQyfcEL----GAEVVVRRNDEIELADI-----ETLAPQKIVISPGPCTPSES---GVSLEVIRHyA 70
Cdd:PLN02889  85 LLIDNYDSYTYNIYQ---ELsivnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPTCPadiGICLRLLLE-C 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  71 GKLPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVF----TGLNNPLTVTRYHSLVIDPPTLPACFEVTAW 146
Cdd:PLN02889 161 RDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKELVPIAW 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285 147 ---SDTQE--------------------------------------------------IMGIRHREWDLEGVQFHPESIL 173
Cdd:PLN02889 241 tssSDTLSflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIA 320

                        250
                 ....*....|.
gi 695713285 174 SEQGHDLLANF 184
Cdd:PLN02889 321 TCYGRQIFKNF 331
PRK06895 PRK06895
anthranilate synthase component II;
1-185 2.39e-37

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 127.55  E-value: 2.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEIELADIETLApqKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPV-THTGTGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHRE 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLkVRSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*.
gi 695713285 160 WDLEGVQFHPESILSEQGHDLLANFL 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 1.28e-31

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: 112.63  E-value: 1.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  21 ELGAEVVVRRNDeIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLGHQAIAQAFGATIVRAAKVM 100
Cdd:cd01742   20 ELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKRE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285 101 HGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDppTLPACFEVTAWSDTQEIMGIRHREWDLEGVQFHPESILSEQGHDL 180
Cdd:cd01742   99 YGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVV--KLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKEI 176


                 ....*
gi 695713285 181 LANFL 185
Cdd:cd01742  177 LKNFL 181
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-177 2.93e-29

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 107.24  E-value: 2.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNdEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  82 HQAIAQAFGATiVRAAKVMHGKTSPVTHTGTG----VFTGL------NNP------LTVTRYHSLviDPPTLPACFEVTA 145
Cdd:PRK05637  83 FQALLEHHGGK-VEPCGPVHGTTDNMILTDAGvqspVFAGLatdvepDHPeipgrkVPIARYHSL--GCVVAPDGMESLG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 695713285 146 WSDTQ---EIMGIRHREWDLEGVQFHPESILSEQG 177
Cdd:PRK05637 160 TCSSEigpVIMAAETTDGKAIGLQFHPESVLSPTG 194
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 1.06e-28

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: 104.89  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  13 WNLYQYFCELGAEV-VVRRNDEIElaDIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGK-LPILGVCLGHQAIAQAFG 90
Cdd:cd01744   10 HNILRELLKRGCEVtVVPYNTDAE--EILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  91 ATIVRaakvM----HGKTSPVTHTGTG-VF-TGLNnpltvtryHSLVIDPPTLPACFEVTAWS-DTQEIMGIRHREWDLE 163
Cdd:cd01744   88 AKTYK----MkfghRGSNHPVKDLITGrVYiTSQN--------HGYAVDPDSLPGGLEVTHVNlNDGTVEGIRHKDLPVF 155


                 ....*...
gi 695713285 164 GVQFHPES 171
Cdd:cd01744  156 SVQFHPEA 163
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-186 4.61e-28

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: 103.55  E-value: 4.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285    2 ILLIDNYDSFTWNLYQYFCELGAEVVVRRNDEiELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   82 HQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYH-SLVIDPPTlpaCFEVTAWSDTQEIMGIRHREW 160
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHgDKVKELPE---GFKVLATSDNCPVAAMAHEEK 156

                         170       180
                  ....*....|....*....|....*.
gi 695713285  161 DLEGVQFHPESILSEQGHDLLANFLH 186
Cdd:TIGR00888 157 PIYGVQFHPEVTHTEYGNELLENFVY 182
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-185 4.84e-28

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 103.39  E-value: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   1 MILLIDNYDSFTWNLYQYFCELGAEVVVRRNDeIELADIETLaPQKIVISPGPcTPSESGVSLEVIRHYagKLPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNPLTVTRYHSLVIDppTLPACFEVTAWSDTQEIMGIRHREW 160
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVK--ELPDGFEILARSDICEVEAMKHKEK 153

                        170       180
                 ....*....|....*....|....*
gi 695713285 161 DLEGVQFHPESILSEQGHDLLANFL 185
Cdd:PRK00758 154 PIYGVQFHPEVAHTEYGEEIFKNFL 178
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-185 1.96e-27

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: 108.07  E-value: 1.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285    2 ILLIDNYDSFTWNLYQYF---CELGAEVVVRRNDEIElADIETLAPQ--KIVISPGPCTPS---ESGVSLEVIR-HYAGK 72
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQ-DQLLELLPLfdAIVVGPGPGNPNnaqDMGIISELWElANLDE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   73 LPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTGVFTGLNNpLTVTRYHSL---VIDPPTLPACFeVTAWSDT 149
Cdd:TIGR01823  87 VPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLyanPEGIDTLLPLC-LTEDEEG 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 695713285  150 QEIMGIRHREWDLEGVQFHPESILSEQGH-DLLANFL 185
Cdd:TIGR01823 165 IILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFL 201
guaA PRK00074
GMP synthase; Reviewed
 33-187 1.53e-24

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 99.35  E-value: 1.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  33 EIELADIETLAPQKIVISPGPCTPSESG---VSLEVirhYAGKLPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTH 109
Cdd:PRK00074  36 DISAEEIRAFNPKGIILSGGPASVYEEGaprADPEI---FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVD 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695713285 110 TGTGVFTGLNNPLTVTRYHSLVIDppTLPACFEVTAWSDTQEIMGIRHREWDLEGVQFHPESILSEQGHDLLANFLHR 187
Cdd:PRK00074 113 NDSPLFKGLPEEQDVWMSHGDKVT--ELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVFD 188
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-170 1.06e-22

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 90.39  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLID---NYDSFTWNLYQYFCELGAEVVVRR--NDEIELADIETLAPQKIVISPGPCTPSESGVSLE----VIRH-YAG 71
Cdd:COG0518    2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEdepaLIREaFEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  72 KLPILGVCLGHQAIAQAFGATIVRAAKVMHGKTsPVTHTGT-GVFTGLNNPLTVTRYHSLVIDppTLPACFEVTAWSDTQ 150
Cdd:COG0518   82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVELTEAdPLFAGLPDEFTVWMSHGDTVT--ELPEGAEVLASSDNC 158

                        170       180
                 ....*....|....*....|
gi 695713285 151 EIMGIRHREWDLeGVQFHPE 170
Cdd:COG0518  159 PNQAFRYGRRVY-GVQFHPE 177
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 36-170 2.00e-19

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 83.79  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  36 LADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTG-V 114
Cdd:PRK12838 201 LEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGrV 280

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 695713285 115 FTGLNNpltvtryHSLVIDPPTL-PACFEVTAWS-DTQEIMGIRHREWDLEGVQFHPE 170
Cdd:PRK12838 281 WMTSQN-------HGYVVDEDSLdGTPLSVRFFNvNDGSIEGLRHKKKPVLSVQFHPE 331
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
37-171 9.94e-19

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 82.05  E-value: 9.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  37 ADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAG-KLPILGVCLGHQAIAQAFGATIVRaakvM----HGKTSPVTHTG 111
Cdd:PRK12564 212 EEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEkKIPIFGICLGHQLLALALGAKTYK----MkfghRGANHPVKDLE 287

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695713285 112 TG--VFTGLNnpltvtryHSLVIDPPTLPACFEVTAWS---DTQEimGIRHREWDLEGVQFHPES 171
Cdd:PRK12564 288 TGkvEITSQN--------HGFAVDEDSLPANLEVTHVNlndGTVE--GLRHKDLPAFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 36-185 3.95e-18

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 81.27  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  36 LADIETLAPQKIVISPGPCTPSESG---VSLEVIRHYAGK-LPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTG 111
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPHSVHVEGaptVPEGFFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695713285 112 TGVFTGLNNPLTVTRYHSLVIDPPTLPACFEVTAWSDTQEIMGIRHREWDLEGVQFHPESILSEQGHDLLANFL 185
Cdd:PLN02347 126 SQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 36-171 4.34e-18

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


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 80.06  E-value: 4.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  36 LADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAGK-LPILGVCLGHQAIAQAFGATIVRaakvM----HGKTSPV--T 108
Cdd:COG0505  210 AEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYK----LkfghRGANHPVkdL 285

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695713285 109 HTGTGVFTGLNnpltvtryHSLVIDPPTLPA-CFEVTAWS---DTQEimGIRHREWDLEGVQFHPES 171
Cdd:COG0505  286 ETGRVEITSQN--------HGFAVDEDSLPAtDLEVTHVNlndGTVE--GLRHKDLPAFSVQYHPEA 342
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 42-179 1.89e-14

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 70.39  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  42 LAPQKIVISPGPCTPSESGVSLEVIRHYAGKLPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTG-VFTGLNN 120
Cdd:PLN02771 280 MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGrVEISAQN 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285 121 pltvtryHSLVIDPPTLPACFEVTAWS-DTQEIMGIRHREWDLEGVQFHPESilSEQGHD 179
Cdd:PLN02771 360 -------HNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVMSLQYHPEA--SPGPHD 410
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-185 2.46e-14

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: 67.66  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  63 LEVIRH-YAGKLPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTHTGTG----VFTGLNNPLTVTRYHSLVIDppTL 137
Cdd:cd01741   71 KELIRQaLAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadpLFAGLPDEFPVFHWHGDTVV--EL 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 695713285 138 PACFEVTAWSDTQEIMGIRHRE--WdleGVQFHPEsilseqgHDLLANFL 185
Cdd:cd01741  149 PPGAVLLASSEACPNQAFRYGDraL---GLQFHPE-------ERLLRNFL 188
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-185 1.14e-11

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 62.12  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNydSFTWNLYQYFCELGAEVVVRrNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVIRHYAG-KLPILGVCL 80
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICM 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  81 GHQAIAQAFGATIVraaKVMHGktspvtHTGTGVFTGLNNPLTVT-RYHSLVIDPPTL-PACFEVTAWS--DTQeIMGIR 156
Cdd:CHL00197 272 GHQILSLALEAKTF---KLKFG------HRGLNHPSGLNQQVEITsQNHGFAVNLESLaKNKFYITHFNlnDGT-VAGIS 341

                        170       180
                 ....*....|....*....|....*....
gi 695713285 157 HREWDLEGVQFHPESilSEQGHDllANFL 185
Cdd:CHL00197 342 HSPKPYFSVQYHPEA--SPGPHD--ADYL 366
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 4.87e-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: 56.44  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTW---NLYQYFCELGAEV-VVRRNDEIELADIETLAPQKIVISPGPCTPSESGVSLEVI----RHYAGKL 73
Cdd:cd03128    1 VAVLLFGGSEELelaSPLDALREAGAEVdVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLallrEAAAAGK 80

                         90
                 ....*....|..
gi 695713285  74 PILGVCLGHQAI 85
Cdd:cd03128   81 PVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 6.52e-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: 6.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   2 ILLIDNYDSFTW---NLYQYFCELGAEVVVRRNDEIELADIETLA-PQKIVISPGPCTPSESGVSLEVI----RHYAGKL 73
Cdd:cd01653    1 VAVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVESDVDLDdYDGLILPGGPGTPDDLARDEALLallrEAAAAGK 80

                         90
                 ....*....|..
gi 695713285  74 PILGVCLGHQAI 85
Cdd:cd01653   81 PILGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-180 2.77e-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: 54.12  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  63 LEVIRH-YAGKLPILGVCLGHQAIAQAFGATIVRAakvmhgktspvthtgtgvftglnnpLTVTRYHSLVIDppTLPACF 141
Cdd:cd01745   90 LALLRAaLERGKPILGICRGMQLLNVALGGTLYQD-------------------------IRVNSLHHQAIK--RLADGL 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 695713285 142 EVTAWSDTQEIMGIRHREWD-LEGVQFHPESILSEQGHDL 180
Cdd:cd01745  143 RVEARAPDGVIEAIESPDRPfVLGVQWHPEWLADTDPDSL 182
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 62-170 8.33e-06

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 44.56  E-value: 8.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   62 SLEVIRH-YAGKLPILGVCLGHQAIAQAFGATIVRAAKVMHGKTSPVTHT-GTGVFTGLNNPLT---------------V 124
Cdd:pfam07722  94 ELALIRAaLARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREHCqVAPYAPSHAVNVEpgsllasllgseefrV 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 695713285  125 TRYHSLVIDppTLPACFEVTAWSDTQEIMGIRHREWD--LEGVQFHPE 170
Cdd:pfam07722 174 NSLHHQAID--RLAPGLRVEAVAPDGTIEAIESPNAKgfALGVQWHPE 219
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 63-170 1.67e-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: 43.62  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  63 LEVIRH-YAGKLPILGVCLGHQAIAQAFGATI------VRAAKVMHGKTSP---VTHT-------------GTGvftgln 119
Cdd:COG2071   86 LALIRAaLERGKPVLGICRGMQLLNVALGGTLyqdlpdQVPGALDHRQPAPryaPRHTveiepgsrlarilGEE------ 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 695713285 120 nPLTVTRYHSLVIDppTLPACFEVTAWSDTQEIMGIRHRE--WDLeGVQFHPE 170
Cdd:COG2071  160 -EIRVNSLHHQAVK--RLGPGLRVSARAPDGVIEAIESPGapFVL-GVQWHPE 208
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 22-185 9.72e-05

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: 41.16  E-value: 9.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   22 LGAE-VVVRRNDEIELADietlapqKIVIsPGPCT-------PSESGVSLEVIRHYAGKLPILGVCLGHQAIA------- 86
Cdd:TIGR01855  21 VGAEpVVVKDSKEAELAD-------KLIL-PGVGAfgaamarLRENGLDLFVELVVRLGKPVLGICLGMQLLFerseegg 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285   87 QAFGATIVRaAKVMHGKTSPVTHTG---------TGVFTGLNNPLTVTRYHSLVIdPPTLPAcfeVTAWSDTQEIMGIRH 157
Cdd:TIGR01855  93 GVPGLGLIK-GNVVKLEARKVPHMGwnevhpvkeSPLLNGIDEGAYFYFVHSYYA-VCEEEA---VLAYADYGEKFPAAV 167

                         170       180
                  ....*....|....*....|....*....
gi 695713285  158 REWDLEGVQFHPE-SilSEQGHDLLANFL 185
Cdd:TIGR01855 168 QKGNIFGTQFHPEkS--GKTGLKLLENFL 194
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 69-170 1.41e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 41.10  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  69 YAGKLPILGVCLGHQAIAQAFGATIV-----RAAKVMHGKTSPVTHTGTgVFTGL--NNPLTVTRYHSLVidppTLPACF 141
Cdd:PRK09065  85 AAAGMPLLGICYGHQLLAHALGGEVGynpagRESGTVTVELHPAAADDP-LFAGLpaQFPAHLTHLQSVL----RLPPGA 159

                         90       100       110
                 ....*....|....*....|....*....|.
gi 695713285 142 EVTAWSDTQEIMGIRHRE--WdleGVQFHPE 170
Cdd:PRK09065 160 VVLARSAQDPHQAFRYGPhaW---GVQFHPE 187
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 22-185 1.92e-03

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: 37.48  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  22 LGAEVVVRRN-DEIELADietlapqKIVIsPG-----PCTPS--ESGVSlEVIRHYA--GKlPILGVCLGHQAIAQA--- 88
Cdd:cd01748   21 LGAEVIITSDpEEILSAD-------KLIL-PGvgafgDAMANlrERGLI-EALKEAIasGK-PFLGICLGMQLLFESsee 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695713285  89 FGAT--------IVRAAKVMHGKTSP--------VTHTGTGVFTGLNNPltvtRY---HSLVIDPptlPACFEVTAWSD- 148
Cdd:cd01748   91 GGGTkglglipgKVVRFPASEGLKVPhmgwnqleITKESPLFKGIPDGS----YFyfvHSYYAPP---DDPDYILATTDy 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 695713285 149 TQEIMGIRHREwDLEGVQFHPE-SilSEQGHDLLANFL 185
Cdd:cd01748  164 GGKFPAAVEKD-NIFGTQFHPEkS--GKAGLKLLKNFL 198
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 70-113 2.23e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 37.62  E-value: 2.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 695713285  70 AGKLPILGVCLGHQAIAQAFGATiVRAAKVMHGKTSPVTHTGTG 113
Cdd:PRK07053  81 AAGLPTLGICLGAQLIARALGAR-VYPGGQKEIGWAPLTLTDAG 123
 
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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