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Conserved domains on  [gi|1601136355|gb|TFB09440|]
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aminodeoxychorismate/anthranilate synthase component II [Candidatus Atribacteria bacterium MT.SAG.1]

Protein Classification

aminodeoxychorismate/anthranilate synthase component II( domain architecture ID 11423509)

aminodeoxychorismate/anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA), and anthranilate, an intermediate in the biosynthesis of L-tryptophan, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-190 3.55e-130

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: 362.82  E-value: 3.55e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEYP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*....
gi 1601136355 162 VEGVQFHPESILTSVGRDILKNFITMAEE 190
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELAGE 189
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-190 3.55e-130

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: 362.82  E-value: 3.55e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEYP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*....
gi 1601136355 162 VEGVQFHPESILTSVGRDILKNFITMAEE 190
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELAGE 189
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-188 8.41e-125

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 349.43  E-value: 8.41e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEY 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*...
gi 1601136355 161 PVEGVQFHPESILTSVGRDILKNFITMA 188
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLELA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 6.95e-110

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: 311.39  E-value: 6.95e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEYP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 1601136355 162 VEGVQFHPESILTSVGRDILKNFI 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-185 4.80e-86

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: 251.63  E-value: 4.80e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGT-IMGIRHKE 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFL 186
GATase pfam00117
Glutamine amidotransferase class-I;
3-184 5.51e-73

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 218.26  E-value: 5.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   3 LVIDNYDSFTYNLVQYLGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKL-GAKIPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREArELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKL-MHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDG-TIMGIRHKE 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDgTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNF 184
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNF 184
Anth_synII_Halo NF041322
anthranilate synthase component II;
4-188 7.95e-73

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 217.98  E-value: 7.95e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   4 VIDNYDSFTYNLVQYLGE--LGIKIQVYRNdKISIREITKKDLTGIVISPGPCTPK---EAGISVEVVQKLGAKIPILGV 78
Cdd:NF041322    1 FVDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  79 CLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVldPLSLPLCLKITAHTEDGT---IMGI 155
Cdd:NF041322   80 CLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDHDGeelVMGI 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1601136355 156 RHKEYPVEGVQFHPESILTSVGRDILKNFITMA 188
Cdd:NF041322  158 RHREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-190 3.55e-130

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: 362.82  E-value: 3.55e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEYP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*....
gi 1601136355 162 VEGVQFHPESILTSVGRDILKNFITMAEE 190
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELAGE 189
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-188 8.41e-125

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 349.43  E-value: 8.41e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEY 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*...
gi 1601136355 161 PVEGVQFHPESILTSVGRDILKNFITMA 188
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLELA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 6.95e-110

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: 311.39  E-value: 6.95e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEYP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 1601136355 162 VEGVQFHPESILTSVGRDILKNFI 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-190 1.18e-103

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 308.18  E-value: 1.18e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIK-IQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVC 79
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  80 LGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKE 159
Cdd:PRK14607   81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNFITMAEE 190
Cdd:PRK14607  161 HPIFGVQFHPESILTEEGKRILKNFLNYQRE 191
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-185 1.01e-95

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 276.30  E-value: 1.01e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEY 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                         170       180
                  ....*....|....*....|....*
gi 1601136355 161 PVEGVQFHPESILTSVGRDILKNFI 185
Cdd:PRK07649  161 PIEGVQFHPESIMTSHGKELLQNFI 185
trpG CHL00101
anthranilate synthase component 2
 1-185 9.52e-93

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 268.52  E-value: 9.52e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:CHL00101    1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEY 160
Cdd:CHL00101   81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                         170       180
                  ....*....|....*....|....*.
gi 1601136355 161 P-VEGVQFHPESILTSVGRDILKNFI 185
Cdd:CHL00101  161 KmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-190 1.87e-89

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 261.27  E-value: 1.87e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLG 81
Cdd:PLN02335   21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAK-KLMHGKTSPIYHNQK---GLYLGIDNPFIAGRYHSLVLDPLSLPL-CLKITAHTEDGTIMGIR 156
Cdd:PLN02335  101 LQCIGEAFGGKIVRSPfGVMHGKSSPVHYDEKgeeGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1601136355 157 HKEYP-VEGVQFHPESILTSVGRDILKNFITMAEE 190
Cdd:PLN02335  181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIKIIEK 215
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-186 3.70e-88

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 257.67  E-value: 3.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITK--KDLTGIVISPGPCTPKEAGISVEVVQKL-GAKIPILGV 78
Cdd:PRK07765    3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAvaAQFDGVLLSPGPGTPERAGASIDMVRACaAAGTPLLGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  79 CLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHK 158
Cdd:PRK07765   83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                         170       180
                  ....*....|....*....|....*...
gi 1601136355 159 EYPVEGVQFHPESILTSVGRDILKNFIT 186
Cdd:PRK07765  163 ELPIHGVQFHPESVLTEGGHRMLANWLT 190
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-185 1.36e-86

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 252.92  E-value: 1.36e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK08007    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKEY 160
Cdd:PRK08007   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                         170       180
                  ....*....|....*....|....*
gi 1601136355 161 PVEGVQFHPESILTSVGRDILKNFI 185
Cdd:PRK08007  161 DLEGVQFHPESILSEQGHQLLANFL 185
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-185 4.80e-86

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: 251.63  E-value: 4.80e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGT-IMGIRHKE 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFL 186
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 5.19e-85

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 249.01  E-value: 5.19e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK06774    1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTE-DGT---IMGIR 156
Cdd:PRK06774   81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSErGGEmdeIMGIR 160

                         170       180
                  ....*....|....*....|....*....
gi 1601136355 157 HKEYPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:PRK06774  161 HRTLPLEGVQFHPESILSEQGHQLLDNFL 189
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-185 1.82e-83

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 245.17  E-value: 1.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK08857    1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTE--DGT---IMGI 155
Cdd:PRK08857   81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGSmdeIMGF 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1601136355 156 RHKEYPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:PRK08857  161 QHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
GATase pfam00117
Glutamine amidotransferase class-I;
3-184 5.51e-73

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 218.26  E-value: 5.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   3 LVIDNYDSFTYNLVQYLGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKL-GAKIPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREArELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKL-MHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDG-TIMGIRHKE 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDgTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNF 184
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNF 184
Anth_synII_Halo NF041322
anthranilate synthase component II;
4-188 7.95e-73

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 217.98  E-value: 7.95e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   4 VIDNYDSFTYNLVQYLGE--LGIKIQVYRNdKISIREITKKDLTGIVISPGPCTPK---EAGISVEVVQKLGAKIPILGV 78
Cdd:NF041322    1 FVDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  79 CLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVldPLSLPLCLKITAHTEDGT---IMGI 155
Cdd:NF041322   80 CLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDHDGeelVMGI 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1601136355 156 RHKEYPVEGVQFHPESILTSVGRDILKNFITMA 188
Cdd:NF041322  158 RHREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
PRK13566 PRK13566
anthranilate synthase component I;
2-188 2.59e-52

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 177.80  E-value: 2.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDK-ISIREITKKDLtgIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK13566  529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFaEEMLDRVNPDL--VVLSPGPGRPSDFDCKATIDAALARNLPIFGVCL 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRV----VPakklMHGKTSPIYHNQKG-LYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGI 155
Cdd:PRK13566  607 GLQAIVEAFGGELgqlaYP----MHGKPSRIRVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAI 682

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1601136355 156 RHKEYPVEGVQFHPESILT---SVGRDILKNFITMA 188
Cdd:PRK13566  683 EHKTLPVAAVQFHPESIMTlggDVGLRIIENVVRLL 718
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-188 1.65e-47

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 162.50  E-value: 1.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRND---KISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGV 78
Cdd:PRK09522    4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  79 CLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDplSLPLCLKITAHTEdGTIMGIRHK 158
Cdd:PRK09522   84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGS--NIPAGLTINAHFN-GMVMAVRHD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1601136355 159 EYPVEGVQFHPESILTSVGRDILKNFITMA 188
Cdd:PRK09522  161 ADRVCGFQFHPESILTTQGARLLEQTLAWA 190
PRK06895 PRK06895
anthranilate synthase component II;
1-186 1.11e-41

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 138.72  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKISIREItkKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:PRK06895    3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEV--ENFSHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKG-LYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKE 159
Cdd:PRK06895   81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                         170       180
                  ....*....|....*....|....*..
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNFIT 186
Cdd:PRK06895  161 LPIYGVQFHPESYISEFGEQILRNWLA 187
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-185 6.37e-40

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: 143.87  E-value: 6.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKI-SIREITKKDLtgIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCL 80
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRHSHAeAAFDERRPDL--VVLSPGPGRPADFDVAGTIDAALARGLPVFGVCL 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKG-LYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGIRHKE 159
Cdd:TIGR01815 597 GLQGMVEAFGGALDVLPEPVHGKASRIRVLGPDaLFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRR 676

                         170       180
                  ....*....|....*....|....*....
gi 1601136355 160 YPVEGVQFHPESILT---SVGRDILKNFI 185
Cdd:TIGR01815 677 LPLAAVQFHPESIMTldgGAGLAMIGNVV 705
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-191 1.15e-38

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 140.37  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   3 LVIDNYDSFTYNLVQYLGEL-GIKIQVYRNDKISIREI-----TKKDLTGIVISPGPCTP---KEAGISVEVVQKLgAKI 73
Cdd:PLN02889   85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLLLEC-RDI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  74 PILGVCLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGI----DNPFIAGRYHSLVLDPLSLPLCLKITAHT-- 147
Cdd:PLN02889  164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIpsgrNSGFKVVRYHSLVIDAESLPKELVPIAWTss 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355 148 ------------------------------------EDGT---------------IMGIRHKEYPVEGVQFHPESILTSV 176
Cdd:PLN02889  244 sdtlsflesqksglvpdayesqigqsgssdpfssklKNGTswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIATCY 323

                         250
                  ....*....|....*
gi 1601136355 177 GRDILKNFITMAEEF 191
Cdd:PLN02889  324 GRQIFKNFREITQDY 338
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-190 2.45e-30

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 109.56  E-value: 2.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDNYDSFTYNLVQYLGELGIKIQVYRNDKiSIREItKKDLTGIVISPGPCTPKeAGISVEVVQKLgaKIPILGVCL 80
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTT-PVEEI-KAFEDGLILSGGPDIER-AGNCPEYLKEL--DVPILGICL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSlvlDPL-SLPLCLKITAHTEDGTIMGIRHKE 159
Cdd:PRK00758   76 GHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHA---DEVkELPDGFEILARSDICEVEAMKHKE 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNFITMAEE 190
Cdd:PRK00758  153 KPIYGVQFHPEVAHTEYGEEIFKNFLEICGK 183
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 3.02e-29

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: 106.43  E-value: 3.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  13 YNLVQYLGELGIKIQVYRNDKiSIREITKKDLTGIVISPGPCTPKEAGISVEVVQK-LGAKIPILGVCLGHQSIGVAYGG 91
Cdd:cd01744    10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKlLGKKIPIFGICLGHQLLALALGA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  92 RVVpakKLMHGKTSpiyHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITaHTE--DGTIMGIRHKEYPVEGVQFHP 169
Cdd:cd01744    89 KTY---KMKFGHRG---SNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVT-HVNlnDGTVEGIRHKDLPVFSVQFHP 161


                  ..
gi 1601136355 170 ES 171
Cdd:cd01744   162 EA 163
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-188 1.39e-28

aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate.


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 111.54  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYL---GELGIKIQVYRNDKIS---IREITKKDltGIVISPGPCTPKEA---GISVEVVQKLGA- 71
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQdqlLELLPLFD--AIVVGPGPGNPNNAqdmGIISELWELANLd 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  72 KIPILGVCLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNpFIAGRYHSLVLDPLS----LPLCLkiTAHT 147
Cdd:TIGR01823  86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGidtlLPLCL--TEDE 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1601136355 148 EDGTIMGIRHKEYPVEGVQFHPESILTSVGR-DILKNFITMA 188
Cdd:TIGR01823 163 EGIILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKLA 204
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-185 1.61e-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: 105.09  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGiSVEVVQK-LGAKIPILGVCL 80
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSSVYAEN-APRADEKiFELGVPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYH-SLVLDplsLPLCLKITAHTEDGTIMGIRHKE 159
Cdd:TIGR00888  79 GMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHgDKVKE---LPEGFKVLATSDNCPVAAMAHEE 155

                         170       180
                  ....*....|....*....|....*.
gi 1601136355 160 YPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:TIGR00888 156 KPIYGVQFHPEVTHTEYGNELLENFV 181
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-185 1.56e-27

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 103.00  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNdKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLG 81
Cdd:PRK05637    4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  82 HQSIGVAYGGRVVPAKKLmHGKTSPIYHNQKG----LYLGI------DNPFIAG------RYHSL---VLDPLSLPLClk 142
Cdd:PRK05637   83 FQALLEHHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLatdvepDHPEIPGrkvpiaRYHSLgcvVAPDGMESLG-- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1601136355 143 iTAHTEDG-TIMGIRHKEYPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:PRK05637  160 -TCSSEIGpVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCV 202
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 2-185 3.18e-27

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: 101.46  E-value: 3.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGIS--VEVVQKLGakIPILGVC 79
Cdd:cd01742     1 ILILDFGSQYTHLIARRVRELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDAPrvDPEIFELG--VPVLGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  80 LGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYH--SLVldplSLPLCLKITAHTEDGTIMGIRH 157
Cdd:cd01742    78 YGMQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHgdEVV----KLPEGFKVIASSDNCPVAAIAN 153

                         170       180
                  ....*....|....*....|....*...
gi 1601136355 158 KEYPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:cd01742   154 EEKKIYGVQFHPEVTHTEKGKEILKNFL 181
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
13-171 4.88e-24

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 96.68  E-value: 4.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  13 YNLVQYLGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKL-GAKIPILGVCLGHQSIGVAYGG 91
Cdd:PRK12564  189 RNILRELAERGCRVTVVPAT-TTAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELlEKKIPIFGICLGHQLLALALGA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  92 RVV-----------PAKKLMHGK---TSpiyHNqkglylgidnpfiagryHSLVLDPLSLPLCLKITaHTE--DGTIMGI 155
Cdd:PRK12564  268 KTYkmkfghrganhPVKDLETGKveiTS---QN-----------------HGFAVDEDSLPANLEVT-HVNlnDGTVEGL 326

                         170
                  ....*....|....*.
gi 1601136355 156 RHKEYPVEGVQFHPES 171
Cdd:PRK12564  327 RHKDLPAFSVQYHPEA 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 13-171 9.67e-23

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: 93.16  E-value: 9.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  13 YNLVQYLGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKL-GAKIPILGVCLGHQSIGVAYGG 91
Cdd:COG0505   188 RNILRELAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELlGKGIPIFGICLGHQLLALALGA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  92 RVV-----------PAKKLMHGK---TSpiyHNqkglylgidnpfiagryHSLVLDPLSLP-LCLKITaHTE--DGTIMG 154
Cdd:COG0505   267 KTYklkfghrganhPVKDLETGRveiTS---QN-----------------HGFAVDEDSLPaTDLEVT-HVNlnDGTVEG 325

                         170
                  ....*....|....*..
gi 1601136355 155 IRHKEYPVEGVQFHPES 171
Cdd:COG0505   326 LRHKDLPAFSVQYHPEA 342
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 14-170 1.23e-19

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 84.56  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  14 NLVQYLGELGIKIQVYRNDKiSIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLGHQSIGVAYGGRV 93
Cdd:PRK12838  180 SILRSLSKRGCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADT 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  94 vpaKKLmhgktsPIYHNqkglylGIDNP---------FIAGRYHSLVLDPLSLPLCLKITAHTE--DGTIMGIRHKEYPV 162
Cdd:PRK12838  259 ---EKL------PFGHR------GANHPvidlttgrvWMTSQNHGYVVDEDSLDGTPLSVRFFNvnDGSIEGLRHKKKPV 323


                  ....*...
gi 1601136355 163 EGVQFHPE 170
Cdd:PRK12838  324 LSVQFHPE 331
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 8-171 1.94e-19

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 84.65  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   8 YD-SFTYNLVQYLGELGIKIQVYRNdKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKLGAKIPILGVCLGHQSIG 86
Cdd:PLN02771  246 YDfGIKHNILRRLASYGCKITVVPS-TWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLG 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  87 VAYGGRVVPAKKLMHGKTSPIYHNQKGlylgidNPFIAGRYHSLVLDPLSLPLCLKIT-AHTEDGTIMGIRHKEYPVEGV 165
Cdd:PLN02771  325 QALGGKTFKMKFGHHGGNHPVRNNRTG------RVEISAQNHNYAVDPASLPEGVEVThVNLNDGSCAGLAFPALNVMSL 398


                  ....*.
gi 1601136355 166 QFHPES 171
Cdd:PLN02771  399 QYHPEA 404
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-170 2.42e-19

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: 81.92  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVID---NYDSFTYNLVQYLGELGIKIQVYR--NDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQKL-----GA 71
Cdd:COG0518     2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALireafEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  72 KIPILGVCLGHQSIGVAYGGRVVPAKKLMHGKTsPIY-HNQKGLYLGIDNPFIAGRYHSlvlD-PLSLPLCLKITAHTED 149
Cdd:COG0518    82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTVWMSHG---DtVTELPEGAEVLASSDN 157

                         170       180
                  ....*....|....*....|.
gi 1601136355 150 GTIMGIRHKEyPVEGVQFHPE 170
Cdd:COG0518   158 CPNQAFRYGR-RVYGVQFHPE 177
guaA PRK00074
GMP synthase; Reviewed
 1-185 1.14e-18

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 82.79  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   1 MILVIDnYDSftynlvQY-------LGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGiSVEVVQK-LGAK 72
Cdd:PRK00074    5 KILILD-FGS------QYtqliarrVRELGVYSEIVPYD-ISAEEIRAFNPKGIILSGGPASVYEEG-APRADPEiFELG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  73 IPILGVCLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSlvlDPLS-LPLCLKITAHTEDGT 151
Cdd:PRK00074   76 VPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHG---DKVTeLPEGFKVIASTENCP 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1601136355 152 IMGIRHKEYPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:PRK00074  153 IAAIANEERKFYGVQFHPEVTHTPQGKKLLENFV 186
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-193 1.01e-14

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 70.98  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNydSFTYNLVQYLGELGIKIQVYrNDKISIREITKKDLTGIVISPGPCTPKEAGISVEVVQK-LGAKIPILGVCL 80
Cdd:CHL00197  195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKlLKYNIPIFGICM 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  81 GHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLylgidnpfIAGRYHSLVLDPLSL-PLCLKITA-HTEDGTIMGIRHK 158
Cdd:CHL00197  272 GHQILSLALEAKTFKLKFGHRGLNHPSGLNQQVE--------ITSQNHGFAVNLESLaKNKFYITHfNLNDGTVAGISHS 343

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1601136355 159 EYPVEGVQFHPESILTSVGRDIL-KNFITMAEEFKR 193
Cdd:CHL00197  344 PKPYFSVQYHPEASPGPHDADYLfEYFIEIIKHSKS 379
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 71-170 9.36e-13

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: 63.75  E-value: 9.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  71 AKIPILGVCLGHQSIGVAYGGRVVPAKKLmhgkTSpiYHNQkglylGIDNpfiagryhslvldplsLPLCLKITAHTEDG 150
Cdd:cd01745    99 RGKPILGICRGMQLLNVALGGTLYQDIRV----NS--LHHQ-----AIKR----------------LADGLRVEARAPDG 151

                          90       100
                  ....*....|....*....|.
gi 1601136355 151 TIMGIRHKEYP-VEGVQFHPE 170
Cdd:cd01745   152 VIEAIESPDRPfVLGVQWHPE 172
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 69-170 1.12e-12

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: 63.82  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  69 LGAKIPILGVCLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYlgidnpfiaGRYHSLVLDPLS------------ 136
Cdd:pfam07722 102 LARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREHCQVAPY---------APSHAVNVEPGSllasllgseefr 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1601136355 137 -----------LPLCLKITAHTEDGTIMGIRHKEYP--VEGVQFHPE 170
Cdd:pfam07722 173 vnslhhqaidrLAPGLRVEAVAPDGTIEAIESPNAKgfALGVQWHPE 219
PLN02347 PLN02347
GMP synthetase
 2-185 3.92e-12

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 63.94  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFTYNLVQYLGELGIKIQVYRNDkISIREITKKDLTGIVISPGPCTPKEAGIS------VEVVQKlgAKIPI 75
Cdd:PLN02347   13 VLILDYGSQYTHLITRRVRELGVYSLLLSGT-ASLDRIASLNPRVVILSGGPHSVHVEGAPtvpegfFDYCRE--RGVPV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  76 LGVCLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKGLYLGIDNPFIAGRYHSLVLDPLSLPLCLKITAHTEDGTIMGI 155
Cdd:PLN02347   90 LGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAI 169

                         170       180       190
                  ....*....|....*....|....*....|
gi 1601136355 156 RHKEYPVEGVQFHPESILTSVGRDILKNFI 185
Cdd:PLN02347  170 ENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 71-185 1.01e-11

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: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  71 AKIPILGVCLGHQSIGVAYGGRVVPAKKLMHGKTSPIYHNQKG----LYLGIDNPFIAGRYHSlvlD-PLSLPLCLKITA 145
Cdd:cd01741    80 AGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadpLFAGLPDEFPVFHWHG---DtVVELPPGAVLLA 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1601136355 146 HTEDGTIMGIRHKEYpVEGVQFHPEsiltsvgRDILKNFI 185
Cdd:cd01741   157 SSEACPNQAFRYGDR-ALGLQFHPE-------ERLLRNFL 188
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-91 1.95e-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: 58.38  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFT---YNLVQYLGELGIKIQVYRNDKISIR-EITKKDLTGIVISPGPCTPKEAGISVEVVQKL----GAKI 73
Cdd:cd01653     1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLARDEALLALLreaaAAGK 80

                          90
                  ....*....|....*...
gi 1601136355  74 PILGVCLGHQSIGVAYGG 91
Cdd:cd01653    81 PILGICLGAQLLVLGVQF 98
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 69-170 3.45e-11

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: 59.80  E-value: 3.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  69 LGAKIPILGVCLGHQSIGVAYGGRVVPAkkLMHGKTSPIYHNQkglylgiDNPFIAGRyHSLVLDPLSLpL--------- 139
Cdd:COG2071    93 LERGKPVLGICRGMQLLNVALGGTLYQD--LPDQVPGALDHRQ-------PAPRYAPR-HTVEIEPGSR-Larilgeeei 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1601136355 140 ---------------CLKITAHTEDGTIMGIRHKEYP-VEGVQFHPE 170
Cdd:COG2071   162 rvnslhhqavkrlgpGLRVSARAPDGVIEAIESPGAPfVLGVQWHPE 208
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 2.77e-10

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 54.90  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355   2 ILVIDNYDSFT---YNLVQYLGELGIKIQVYRNDKISIR-EITKKDLTGIVISPGPCTPKEAGISVEVVQKL----GAKI 73
Cdd:cd03128     1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLAWDEALLALLreaaAAGK 80

                          90
                  ....*....|..
gi 1601136355  74 PILGVCLGHQSI 85
Cdd:cd03128    81 PVLGICLGAQLL 92
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 63-187 3.50e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 42.54  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  63 VEVVQKLgaKIPILGVCLGHQSIG-VAYGGRVVPAKKLMHGKTS-------PIYH---NQ----KG--LYLGIDNpfiaG 125
Cdd:PRK13170   63 IDLIKAC--TQPVLGICLGMQLLGeRSEESGGVDCLGIIDGPVKkmtdfglPLPHmgwNQvtpqAGhpLFQGIED----G 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1601136355 126 RY----HSLvldplslplCLKITAHTedgtimgIRHKEYPVE-----------GVQFHPE-SilTSVGRDILKNFITM 187
Cdd:PRK13170  137 SYfyfvHSY---------AMPVNEYT-------IAQCNYGEPfsaaiqkdnffGVQFHPErS--GAAGAQLLKNFLEM 196
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 67-96 1.38e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 38.39  E-value: 1.38e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1601136355  67 QKLGAKIPILGVCLGHQSIGVAYGGRVVPA 96
Cdd:PRK07053   78 QRLAAGLPTLGICLGAQLIARALGARVYPG 107
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 67-170 1.43e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 38.02  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  67 QKLGAKIPILGVCLGHQSIGVAYGGRV-----------VPAKKLMHGKTSPiyhnqkgLYLGIDNPFIAGRYH--SLvld 133
Cdd:PRK09065   83 QAAAAGMPLLGICYGHQLLAHALGGEVgynpagresgtVTVELHPAAADDP-------LFAGLPAQFPAHLTHlqSV--- 152

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1601136355 134 pLSLPLCLKITAHTEDGTIMGIRHKEYpVEGVQFHPE 170
Cdd:PRK09065  153 -LRLPPGAVVLARSAQDPHQAFRYGPH-AWGVQFHPE 187
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 72-187 4.41e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 36.74  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355  72 KIPILGVCLGHQSI-------GVAYG-----GRVV-----PAKKLMH-GKTSPIYHNQKGLYLGIDNP---FIAGRYHSL 130
Cdd:PRK13152   73 KKPILGICLGMQLFlergyegGVCEGlgfieGEVVkfeedLNLKIPHmGWNELEILKQSPLYQGIPEKsdfYFVHSFYVK 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601136355 131 VLDPLSLPLC---LKITAHTEDGTIMgirhkeypveGVQFHPESIlTSVGRDILKNFITM 187
Cdd:PRK13152  153 CKDEFVSAKAqygHKFVASLQKDNIF----------ATQFHPEKS-QNLGLKLLENFARL 201
 
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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