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Conserved domains on  [gi|636854652|ref|WP_024374087|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [Vibrio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08857 super family cl32332
aminodeoxychorismate/anthranilate synthase component II;
1-192 1.42e-143

aminodeoxychorismate/anthranilate synthase component II;


The actual alignment was detected with superfamily member PRK08857:

Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 396.94  E-value: 1.42e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTELPDGTPDEIMGY 160
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGSMDEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 636854652 161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
 
Name Accession Description Interval E-value
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-192 1.42e-143

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 396.94  E-value: 1.42e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTELPDGTPDEIMGY 160
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGSMDEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 636854652 161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-191 1.66e-135

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: 376.30  E-value: 1.66e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  82 HQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpdEIMGYQ 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTE--DG---EIMGIR 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 636854652 162 HKTLPIDAVQFHPESIKTEQGHELLANFLR 191
Cdd:COG0512  156 HRELPIEGVQFHPESILTEHGHQLLANFLE 185
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-192 1.06e-110

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: 313.65  E-value: 1.06e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652    1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpdgTPDEIMGY 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEE----ENIEIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 636854652  161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-190 9.08e-109

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: 308.69  E-value: 9.08e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  82 HQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpdEIMGYQ 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTE--DG---VIMALR 155

                        170       180
                 ....*....|....*....|....*....
gi 636854652 162 HKTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:cd01743  156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
3-192 1.64e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 227.12  E-value: 1.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652    3 LIIDNYDSFTYNLYQYFCELGATVKVVRNDEvTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEH-FAGRLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   82 HQAIAQVFGGEVVRA-RQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpDEIMGY 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSE--ND--GTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 636854652  161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
4-192 3.90e-65

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 198.33  E-value: 3.90e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   4 IIDNYDSFTYNLYQYFCE--LGATVKVVRNdEVTLEQIEALAPSHLVISPGPCTP-NE--AGISLAAIEHFAGRLPILGV 78
Cdd:NF041322   1 FVDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkNDrdVGVTADVLRELSPEVPTLGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  79 CLGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVknGTLPDCFELTAWTElpDGTPDEIM 158
Cdd:NF041322  80 CLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTD--HDGEELVM 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 636854652 159 GYQHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:NF041322 156 GIRHREHPIECVQFHPESVLTGVGHDVIENFLAA 189
 
Name Accession Description Interval E-value
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-192 1.42e-143

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 396.94  E-value: 1.42e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTELPDGTPDEIMGY 160
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGSMDEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 636854652 161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-191 1.66e-135

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: 376.30  E-value: 1.66e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  82 HQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpdEIMGYQ 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTE--DG---EIMGIR 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 636854652 162 HKTLPIDAVQFHPESIKTEQGHELLANFLR 191
Cdd:COG0512  156 HRELPIEGVQFHPESILTEHGHQLLANFLE 185
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-191 5.10e-133

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 370.23  E-value: 5.10e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpdEIMGY 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTD--DG---EIMGV 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 636854652 161 QHKTLPIDAVQFHPESIKTEQGHELLANFLR 191
Cdd:PRK05670 156 RHKELPIYGVQFHPESILTEHGHKLLENFLE 186
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-191 3.59e-121

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 340.30  E-value: 3.59e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElPDGTPDEIMGY 160
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSE-RGGEMDEIMGI 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 636854652 161 QHKTLPIDAVQFHPESIKTEQGHELLANFLR 191
Cdd:PRK06774 160 RHRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-192 1.14e-112

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 318.78  E-value: 1.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpdgtPDEIMGY 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSE-----TREIMGI 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 636854652 161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:PRK08007 156 RHRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-192 1.06e-110

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: 313.65  E-value: 1.06e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652    1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpdgTPDEIMGY 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEE----ENIEIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 636854652  161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-190 9.08e-109

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: 308.69  E-value: 9.08e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  82 HQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpdEIMGYQ 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTE--DG---VIMALR 155

                        170       180
                 ....*....|....*....|....*....
gi 636854652 162 HKTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:cd01743  156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-190 1.19e-108

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 320.90  E-value: 1.19e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGA-TVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPeEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  80 LGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpdEIMG 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSD--DG---EIMG 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 636854652 160 YQHKTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:PRK14607 156 IRHKEHPIFGVQFHPESILTEEGKRILKNFL 186
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-191 8.48e-108

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 306.73  E-value: 8.48e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpdgtPDEIMGY 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTE-----EGEIMAI 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 636854652 161 QHKTLPIDAVQFHPESIKTEQGHELLANFLR 191
Cdd:PRK07649 156 RHKTLPIEGVQFHPESIMTSHGKELLQNFIR 186
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-190 1.65e-81

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 240.72  E-value: 1.65e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSH--LVISPGPCTPNEAGISLAAIEHFAG-RLPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFdgVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  79 CLGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGTpdeIM 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTD--SGV---IM 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 636854652 159 GYQHKTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:PRK07765 158 AVRHRELPIHGVQFHPESVLTEGGHRMLANWL 189
trpG CHL00101
anthranilate synthase component 2
 1-190 7.14e-81

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 238.48  E-value: 7.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGTpdeIMGY 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTE--DGL---IMAC 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 636854652 161 QHKTLP-IDAVQFHPESIKTEQGHELLANFL 190
Cdd:CHL00101 156 RHKKYKmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-191 8.79e-77

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 229.30  E-value: 8.79e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  82 HQAIAQVFGGEVVRARQ-VMHGKTSPVRHT---GRSVFAGLNNPLTVTRYHSLVVKNGTLP-DCFELTAWTElpDGTpde 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTE--DGL--- 175

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 636854652 157 IMGYQHKTLP-IDAVQFHPESIKTEQGHELLANFLR 191
Cdd:PLN02335 176 IMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIK 211
GATase pfam00117
Glutamine amidotransferase class-I;
3-192 1.64e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 227.12  E-value: 1.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652    3 LIIDNYDSFTYNLYQYFCELGATVKVVRNDEvTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEH-FAGRLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   82 HQAIAQVFGGEVVRA-RQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGtpDEIMGY 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSE--ND--GTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 636854652  161 QHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
4-192 3.90e-65

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 198.33  E-value: 3.90e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   4 IIDNYDSFTYNLYQYFCE--LGATVKVVRNdEVTLEQIEALAPSHLVISPGPCTP-NE--AGISLAAIEHFAGRLPILGV 78
Cdd:NF041322   1 FVDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkNDrdVGVTADVLRELSPEVPTLGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  79 CLGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVknGTLPDCFELTAWTElpDGTPDEIM 158
Cdd:NF041322  80 CLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTD--HDGEELVM 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 636854652 159 GYQHKTLPIDAVQFHPESIKTEQGHELLANFLRR 192
Cdd:NF041322 156 GIRHREHPIECVQFHPESVLTGVGHDVIENFLAA 189
PRK13566 PRK13566
anthranilate synthase component I;
2-191 3.96e-56

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 188.20  E-value: 3.96e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDeVTLEQIEALAPSHLVISPGPCTPNEAGISlAAIEHFAGR-LPILGVCL 80
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFDCK-ATIDAALARnLPIFGVCL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTG-RSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpDGTpdeIMG 159
Cdd:PRK13566 607 GLQAIVEAFGGELGQLAYPMHGKPSRIRVRGpGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETE--DGV---IMA 681

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 636854652 160 YQHKTLPIDAVQFHPESIKT---EQGHELLANFLR 191
Cdd:PRK13566 682 IEHKTLPVAAVQFHPESIMTlggDVGLRIIENVVR 716
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-190 1.11e-46

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 160.19  E-value: 1.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRND---EVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  79 CLGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKNgtLPDCFELTAWTElpdgtpDEIM 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSN--IPAGLTINAHFN------GMVM 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 636854652 159 GYQHKTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:PRK09522 156 AVRHDADRVCGFQFHPESILTTQGARLLEQTL 187
PRK06895 PRK06895
anthranilate synthase component II;
1-190 3.02e-44

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 145.27  E-value: 3.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDEVTLEQIEALapSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENF--SHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRS-VFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpdgtPDEIMG 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCD-----ENVVMA 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 636854652 160 YQHKTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:PRK06895 156 MQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-189 5.19e-40

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 144.22  E-value: 5.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   3 LIIDNYDSFTYNLYQyfcEL----GATVKVVRNDEVTLEQI-----EALAPSHLVISPGPCTPNEA---GISLAAIEHfA 70
Cdd:PLN02889  85 LLIDNYDSYTYNIYQ---ELsivnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPTCPadiGICLRLLLE-C 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  71 GRLPILGVCLGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVF----AGLNNPLTVTRYHSLVVKNGTLPDCFELTAW 146
Cdd:PLN02889 161 RDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKELVPIAW 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652 147 T-----------ELPDGTPDE-------------------------------------IMGYQHKTLPIDAVQFHPESIK 178
Cdd:PLN02889 241 TsssdtlsflesQKSGLVPDAyesqigqsgssdpfssklkngtswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIA 320

                        250
                 ....*....|.
gi 636854652 179 TEQGHELLANF 189
Cdd:PLN02889 321 TCYGRQIFKNF 331
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-191 8.79e-37

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: 126.28  E-value: 8.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652    2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNDeVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   82 HQAIAQVFGGEVVRARQVMHGKTSpVRHTGRSV-FAGLNNPLTVTRYHSLVVKNgtLPDCFELTAWTelpDGTPDEIMgy 160
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAE-LEILDEDDlFRGLPDESTVWMSHGDKVKE--LPEGFKVLATS---DNCPVAAM-- 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 636854652  161 QHKTLPIDAVQFHPESIKTEQGHELLANFLR 191
Cdd:TIGR00888 152 AHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-190 7.19e-32

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: 113.40  E-value: 7.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   3 LIIDNYDSFTYNLYQYFCELGATVKVVRNDEvTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLGH 82
Cdd:cd01742    2 LILDFGSQYTHLIARRVRELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  83 QAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKngTLPDCFELTAWTElpdgtPDEIMGYQH 162
Cdd:cd01742   81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVV--KLPEGFKVIASSD-----NCPVAAIAN 153

                        170       180
                 ....*....|....*....|....*...
gi 636854652 163 KTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:cd01742  154 EEKKIYGVQFHPEVTHTEKGKEILKNFL 181
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-190 1.13e-31

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 113.02  E-value: 1.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   1 MLLIIDNYDSFTYNLYQYFCELGATVKVVRNDeVTLEQIEALaPSHLVISPGPcTPNEAGISLAAIEHFagRLPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  81 GHQAIAQVFGGEVVRARQVMHGKT--SPVRHTGrsVFAGLNNPLTVTRYHSLVVKNgtLPDCFELTAWTELPdgtpdEIM 158
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALVevEILDEDD--ILKGLPPEIRVWASHADEVKE--LPDGFEILARSDIC-----EVE 146

                        170       180       190
                 ....*....|....*....|....*....|..
gi 636854652 159 GYQHKTLPIDAVQFHPESIKTEQGHELLANFL 190
Cdd:PRK00758 147 AMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFL 178
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-182 1.67e-29

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 108.01  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIIDNYDSFTYNLYQYFCELGATVKVVRNdEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  82 HQAIAQVFGGEvVRARQVMHGKTSPVRHTG----RSVFAGL------NNP------LTVTRYHSLVVKNgtLPDcfELTA 145
Cdd:PRK05637  83 FQALLEHHGGK-VEPCGPVHGTTDNMILTDagvqSPVFAGLatdvepDHPeipgrkVPIARYHSLGCVV--APD--GMES 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 636854652 146 WTELPDGTPDEIMGYQHKTLPIDAVQFHPESIKTEQG 182
Cdd:PRK05637 158 LGTCSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTG 194
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-190 4.92e-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: 110.00  E-value: 4.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652    2 LLIIDNYDSFTYNLYQYF---CELGATVKVVRNDEVT------LEQIEALapshlVISPGPCTPNEA---GIsLAAIEHF 69
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQdqllelLPLFDAI-----VVGPGPGNPNNAqdmGI-ISELWEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   70 AG--RLPILGVCLGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGRSVFAGLNNpLTVTRYHSLVVkNGTLPDcfELTAWT 147
Cdd:TIGR01823  82 ANldEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYA-NPEGID--TLLPLC 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 636854652  148 ELPDGTPDEIMGYQHKTLPIDAVQFHPESIKTEQGH-ELLANFL 190
Cdd:TIGR01823 158 LTEDEEGIILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFL 201
guaA PRK00074
GMP synthase; Reviewed
 21-192 1.25e-25

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 102.43  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  21 ELGATVKVVRNDeVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLGHQAIAQVFGGEVVRARQVM 100
Cdd:PRK00074  25 ELGVYSEIVPYD-ISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICYGMQLMAHQLGGKVERAGKRE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652 101 HGKTSPVRHTGRSVFAGLNNPLTVTRYHSLVVKngTLPDCFELTAWTElpdGTPdeIMGYQHKTLPIDAVQFHPESIKTE 180
Cdd:PRK00074 104 YGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVT--ELPEGFKVIASTE---NCP--IAAIANEERKFYGVQFHPEVTHTP 176

                        170
                 ....*....|..
gi 636854652 181 QGHELLANFLRR 192
Cdd:PRK00074 177 QGKKLLENFVFD 188
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-176 8.76e-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: 94.87  E-value: 8.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  13 YNLYQYFCELGATVKVVRNDeVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGR-LPILGVCLGHQAIAQVFGG 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYN-TDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  92 EVVRARQVMHGKTSPVRH--TGRSVFAGLNnpltvtryHSLVVKNGTLPDCFELTaWTELPDGTpdeIMGYQHKTLPIDA 169
Cdd:cd01744   89 KTYKMKFGHRGSNHPVKDliTGRVYITSQN--------HGYAVDPDSLPGGLEVT-HVNLNDGT---VEGIRHKDLPVFS 156


                 ....*..
gi 636854652 170 VQFHPES 176
Cdd:cd01744  157 VQFHPEA 163
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-192 9.38e-24

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


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 93.47  E-value: 9.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   2 LLIID---NYDSFTYNLYQYFCELGATVKVVR--NDEVTLEQIEALAPSHLVISPGPCTPNEAGISL----AAIEH-FAG 71
Cdd:COG0518    2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLedepALIREaFEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  72 RLPILGVCLGHQAIAQVFGGEVVRARQVMHGKTsPVRHTGRS-VFAGLNNPLTVTRYHSLVVKngTLPDCFELTAWTelp 150
Cdd:COG0518   82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVELTEADpLFAGLPDEFTVWMSHGDTVT--ELPEGAEVLASS--- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636854652 151 DGTPDEIMGYQHKTLpidAVQFHPE------------------------------SIKTEQGHELLANFLRR 192
Cdd:COG0518  156 DNCPNQAFRYGRRVY---GVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 35-175 2.29e-21

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 89.57  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  35 TLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLGHQAIAQVFGGEVVRARQVMHGKTSPVRH--TGR 112
Cdd:PRK12838 200 SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDltTGR 279

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636854652 113 SVFAGLNnpltvtryHSLVVKNGTLPDCFELTAWTELPDGTpdeIMGYQHKTLPIDAVQFHPE 175
Cdd:PRK12838 280 VWMTSQN--------HGYVVDEDSLDGTPLSVRFFNVNDGS---IEGLRHKKKPVLSVQFHPE 331
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
19-176 1.68e-18

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 81.66  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  19 FCELGATVKVVRNDeVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGR-LPILGVCLGHQAIAQVFGGEVVRAR 97
Cdd:PRK12564 195 LAERGCRVTVVPAT-TTAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKkIPIFGICLGHQLLALALGAKTYKMK 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  98 QVMHGKTSPVRH--TGRSVFAGLNnpltvtryHSLVVKNGTLPDCFELTAWtELPDGTpdeIMGYQHKTLPIDAVQFHPE 175
Cdd:PRK12564 274 FGHRGANHPVKDleTGKVEITSQN--------HGFAVDEDSLPANLEVTHV-NLNDGT---VEGLRHKDLPAFSVQYHPE 341


                 .
gi 636854652 176 S 176
Cdd:PRK12564 342 A 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 13-176 2.10e-16

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: 75.83  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  13 YNLYQYFCELGATVKVVRNDeVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGR-LPILGVCLGHQAIAQVFGG 91
Cdd:COG0505  188 RNILRELAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGA 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  92 EVVRarqvM----HGKTSPVRH--TGRSVFAGLNnpltvtryHSLVVKNGTLPD-CFELTaWTELPDGTpdeIMGYQHKT 164
Cdd:COG0505  267 KTYK----LkfghRGANHPVKDleTGRVEITSQN--------HGFAVDEDSLPAtDLEVT-HVNLNDGT---VEGLRHKD 330

                        170
                 ....*....|..
gi 636854652 165 LPIDAVQFHPES 176
Cdd:COG0505  331 LPAFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 34-190 1.54e-14

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 70.87  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  34 VTLEQIEALAPSHLVISPGPCTPNEAG---ISLAAIEHFAGR-LPILGVCLGHQAIAQVFGGEVVRARQVMHGKTSPVRH 109
Cdd:PLN02347  44 ASLDRIASLNPRVVILSGGPHSVHVEGaptVPEGFFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652 110 TGRSVFAGLNNPLTVTRYHSLVVKNGTLPDCFELTAWTElpdgtPDEIMGYQHKTLPIDAVQFHPESIKTEQGHELLANF 189
Cdd:PLN02347 124 CGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSV-----QGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHF 198


                 .
gi 636854652 190 L 190
Cdd:PLN02347 199 L 199
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 8-176 5.20e-14

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 69.24  E-value: 5.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   8 YD-SFTYNLYQYFCELGATVKVVRNDEVTLEQIEaLAPSHLVISPGPCTPNEAGISLAAIEHFAGRLPILGVCLGHQAIA 86
Cdd:PLN02771 246 YDfGIKHNILRRLASYGCKITVVPSTWPASEALK-MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLG 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  87 QVFGGEVVRARQVMHGKTSPVRH--TGRSVFAGLNnpltvtryHSLVVKNGTLPDCFELTAwTELPDGTpdeIMGYQHKT 164
Cdd:PLN02771 325 QALGGKTFKMKFGHHGGNHPVRNnrTGRVEISAQN--------HNYAVDPASLPEGVEVTH-VNLNDGS---CAGLAFPA 392

                        170
                 ....*....|..
gi 636854652 165 LPIDAVQFHPES 176
Cdd:PLN02771 393 LNVMSLQYHPEA 404
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 69-190 9.76e-12

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 60.72  E-value: 9.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  69 FAGRLPILGVCLGHQAIAQVFGGEVVRARQVMHGKTSPVRHTGR----SVFAGLNNPLTVTRYHSLVVknGTLPDCFELT 144
Cdd:cd01741   78 LAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAgkadPLFAGLPDEFPVFHWHGDTV--VELPPGAVLL 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 636854652 145 AWTElpdGTPDEIMGYQHKTLpidAVQFHPEsikteqgHELLANFL 190
Cdd:cd01741  156 ASSE---ACPNQAFRYGDRAL---GLQFHPE-------ERLLRNFL 188
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-176 1.76e-11

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 61.74  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  13 YNLYQYFCELGATVKVVrNDEVTLEQIEALAPSHLVISPGPCTPNEAGISLAAIEHFAGR-LPILGVCLGHQAIAQVFGG 91
Cdd:CHL00197 204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYnIPIFGICMGHQILSLALEA 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  92 EVVRARQVMHGKTSPVrhtgrsvfaGLNNPLTVT-RYHSLVVKngtLPDCFELTAWT---ELPDGTpdeIMGYQHKTLPI 167
Cdd:CHL00197 283 KTFKLKFGHRGLNHPS---------GLNQQVEITsQNHGFAVN---LESLAKNKFYIthfNLNDGT---VAGISHSPKPY 347


                 ....*....
gi 636854652 168 DAVQFHPES 176
Cdd:CHL00197 348 FSVQYHPEA 356
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 4.97e-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: 56.83  E-value: 4.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   3 LIIDNYDSFT---YNLYQYFCELGATVKVVRNDEVTLEQIEALA-PSHLVISPGPCTPNEAGISLAAI----EHFAGRLP 74
Cdd:cd03128    2 AVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDdYDGLILPGGPGTPDDLAWDEALLallrEAAAAGKP 81

                         90
                 ....*....|.
gi 636854652  75 ILGVCLGHQAI 85
Cdd:cd03128   82 VLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-92 6.26e-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: 57.22  E-value: 6.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   3 LIIDNYDSFT---YNLYQYFCELGATVKVVRNDEVTLEQIEALA-PSHLVISPGPCTPNEAGISLAAI----EHFAGRLP 74
Cdd:cd01653    2 AVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDdYDGLILPGGPGTPDDLARDEALLallrEAAAAGKP 81

                         90
                 ....*....|....*...
gi 636854652  75 ILGVCLGHQAIaqVFGGE 92
Cdd:cd01653   82 ILGICLGAQLL--VLGVQ 97
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 64-175 1.75e-07

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: 49.11  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  64 AAIEHfagRLPILGVCLGHQAIAQVFGGevvrarqvmhgktspvrhtgrsvfaGLNNPLTVTRYHSLVVKngTLPDCFEL 143
Cdd:cd01745   95 AALER---GKPILGICRGMQLLNVALGG-------------------------TLYQDIRVNSLHHQAIK--RLADGLRV 144

                         90       100       110
                 ....*....|....*....|....*....|...
gi 636854652 144 TAWTelPDGTpdeIMGYQHKTLP-IDAVQFHPE 175
Cdd:cd01745  145 EARA--PDGV---IEAIESPDRPfVLGVQWHPE 172
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 22-191 1.09e-06

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: 46.93  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   22 LGATVKVVRNDEVtLEQIEALapshlvISPGPCTPNEA-------GISLAAIEHFAGRLPILGVCLGHQAIAQ------- 87
Cdd:TIGR01855  21 VGAEPVVVKDSKE-AELADKL------ILPGVGAFGAAmarlrenGLDLFVELVVRLGKPVLGICLGMQLLFErseeggg 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   88 -----VFGGEVVR--ARQVMH---GKTSPVRhtGRSVFAGLNNPLTVTRYHSLVVKngtlPDCFELTAWTELpdGTP--- 154
Cdd:TIGR01855  94 vpglgLIKGNVVKleARKVPHmgwNEVHPVK--ESPLLNGIDEGAYFYFVHSYYAV----CEEEAVLAYADY--GEKfpa 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 636854652  155 ----DEIMGyqhktlpidaVQFHPE-SIKTeqGHELLANFLR 191
Cdd:TIGR01855 166 avqkGNIFG----------TQFHPEkSGKT--GLKLLENFLE 195
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 62-175 1.71e-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: 46.48  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652   62 SLAAIEHFAGR-LPILGVCLGHQAIAQVFGG----------EVVRARQVMHGKTSPVRHTGR----SVFAGL--NNPLTV 124
Cdd:pfam07722  94 ELALIRAALARgKPILGICRGFQLLNVALGGtlyqdiqeqpGFTDHREHCQVAPYAPSHAVNvepgSLLASLlgSEEFRV 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 636854652  125 TRYHSLVVKngTLPDCFELTAWTelPDGTPDEIMGYQHKTlPIDAVQFHPE 175
Cdd:pfam07722 174 NSLHHQAID--RLAPGLRVEAVA--PDGTIEAIESPNAKG-FALGVQWHPE 219
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 64-175 1.62e-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: 44.00  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  64 AAIEHfagRLPILGVCLGHQAIAQVFGG------EVVRARQVMHGKTSP---VRHT-----GrSVFAGL--NNPLTVTRY 127
Cdd:COG2071   91 AALER---GKPVLGICRGMQLLNVALGGtlyqdlPDQVPGALDHRQPAPryaPRHTveiepG-SRLARIlgEEEIRVNSL 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 636854652 128 HSLVVKngTLPDCFELTAWTelPDGTpdeIMGYQHKTLP-IDAVQFHPE 175
Cdd:COG2071  167 HHQAVK--RLGPGLRVSARA--PDGV---IEAIESPGAPfVLGVQWHPE 208
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 73-175 7.74e-05

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 41.87  E-value: 7.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  73 LPILGVCLGHQAIAQVFGGEVV---RARQV--MHGKTSPvrhtgrsvfAGLNNPLTvtryhslvvknGTLPDCF-----E 142
Cdd:PRK09065  89 MPLLGICYGHQLLAHALGGEVGynpAGRESgtVTVELHP---------AAADDPLF-----------AGLPAQFpahltH 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 636854652 143 LTAWTELPDGT---------PDEIMGYQHKTLpidAVQFHPE 175
Cdd:PRK09065 149 LQSVLRLPPGAvvlarsaqdPHQAFRYGPHAW---GVQFHPE 187
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 22-175 8.27e-05

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 41.85  E-value: 8.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  22 LGATVKVVRNDEVTLEQIEALAPSH---LVISPGPCTPNEAGI------SLAAIE-HFAGRLPILGVCLGHQAIAQVFGG 91
Cdd:PRK07053  23 LGARGYRVRYVDVGVDDLETLDALEpdlLVVLGGPIGVYDDELypflapEIALLRqRLAAGLPTLGICLGAQLIARALGA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  92 EVVrarqVMHGKT---SPVRHTGR---SVFAGLNNPLTVTRYHSlvvkngtlpDCFELTAWTELPDGTPdeimGYQHKTL 165
Cdd:PRK07053 103 RVY----PGGQKEigwAPLTLTDAgraSPLRHLGAGTPVLHWHG---------DTFDLPEGATLLASTP----ACRHQAF 165

                        170
                 ....*....|....
gi 636854652 166 PID----AVQFHPE 175
Cdd:PRK07053 166 AWGnhvlALQFHPE 179
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 74-191 3.65e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 36.74  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636854652  74 PILGVCLGHQAIAQV---FG---------GEVVRAR-----QVMHGKTSPVRHTGRS-VFAGLNNPLTVTRYHSLVVKng 135
Cdd:PRK13152  75 PILGICLGMQLFLERgyeGGvceglgfieGEVVKFEedlnlKIPHMGWNELEILKQSpLYQGIPEKSDFYFVHSFYVK-- 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636854652 136 tlpdCFE--LTAWTElpdgtpdeimgYQHKTLP------IDAVQFHPEsiKTEQ-GHELLANFLR 191
Cdd:PRK13152 153 ----CKDefVSAKAQ-----------YGHKFVAslqkdnIFATQFHPE--KSQNlGLKLLENFAR 200
PRK05665 PRK05665
amidotransferase; Provisional
 75-98 6.69e-03

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 36.33  E-value: 6.69e-03
                         10        20
                 ....*....|....*....|....
gi 636854652  75 ILGVCLGHQAIAQVFGGEVVRARQ 98
Cdd:PRK05665  94 LLGVCFGHQLLALLLGGKAERASQ 117
 
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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