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Conserved domains on  [gi|983472009|ref|WP_060629983|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [Bacillus cereus group]

Protein Classification

aminodeoxychorismate/anthranilate synthase component II( domain architecture ID 10792604)

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

CATH:  3.40.50.880
EC:  4.1.3.27
Gene Ontology:  GO:0000162|GO:0046820|GO:0004049
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-190 3.12e-121

anthranilate synthase component II; Provisional


:

Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 340.57  E-value: 3.12e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNY 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWT-DDGEIMGVRHKE 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 983472009 161 YPLFGLQFHPESIATEEGGKLIRAFLTEVK 190
Cdd:PRK05670 160 LPIYGVQFHPESILTEHGHKLLENFLELAR 189
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-190 3.12e-121

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 340.57  E-value: 3.12e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNY 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWT-DDGEIMGVRHKE 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 983472009 161 YPLFGLQFHPESIATEEGGKLIRAFLTEVK 190
Cdd:PRK05670 160 LPIYGVQFHPESILTEHGHKLLENFLELAR 189
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-191 7.83e-121

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: 339.32  E-value: 7.83e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  82 HQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNYY 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWT-EDGEIMGIRHREL 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 983472009 162 PLFGLQFHPESIATEEGGKLIRAFLTEVKE 191
Cdd:COG0512  160 PIEGVQFHPESILTEHGHQLLANFLELAGE 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-186 2.35e-104

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: 297.52  E-value: 2.35e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  82 HQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNYY 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDL 159

                        170       180
                 ....*....|....*....|....*
gi 983472009 162 PLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:cd01743  160 PIYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 2.31e-84

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: 247.39  E-value: 2.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAMDDGEIMAVRHNY 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 983472009  161 YPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFL 186
GATase pfam00117
Glutamine amidotransferase class-I;
3-189 1.21e-69

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 209.79  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    3 VLIDNYDSFTYNLYQLLGEYEEDIVVVRNDqITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRH-FYKNVPILGICLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   82 HQAIIAAFGGDIVRA-ERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAMDDGEIMAVRHNY 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 983472009  161 YPLFGLQFHPESIATEEGGKLIRAFLTEV 189
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-189 3.29e-63

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 193.71  E-value: 3.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   5 IDNYDSFTYNLYQLLGEYEE--DIVVVRNdQITIEQLEEMKPKGIVLSPGPGKPE---DAGICIEVIRHFYKNVPILGIC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  80 LGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAeqTSLPECFDILATAMDDGE--IMAVR 157
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGEelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 983472009 158 HNYYPLFGLQFHPESIATEEGGKLIRAFLTEV 189
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-190 3.12e-121

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 340.57  E-value: 3.12e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNY 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWT-DDGEIMGVRHKE 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 983472009 161 YPLFGLQFHPESIATEEGGKLIRAFLTEVK 190
Cdd:PRK05670 160 LPIYGVQFHPESILTEHGHKLLENFLELAR 189
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-191 7.83e-121

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: 339.32  E-value: 7.83e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  82 HQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNYY 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWT-EDGEIMGIRHREL 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 983472009 162 PLFGLQFHPESIATEEGGKLIRAFLTEVKE 191
Cdd:COG0512  160 PIEGVQFHPESILTEHGHQLLANFLELAGE 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-186 2.35e-104

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: 297.52  E-value: 2.35e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  82 HQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNYY 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDL 159

                        170       180
                 ....*....|....*....|....*
gi 983472009 162 PLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:cd01743  160 PIYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-186 6.68e-104

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 308.95  E-value: 6.68e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYE-EDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGIC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGpEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  80 LGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHN 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKS-DDGEIMGIRHK 159

                        170       180
                 ....*....|....*....|....*..
gi 983472009 160 YYPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:PRK14607 160 EHPIFGVQFHPESILTEEGKRILKNFL 186
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-193 4.93e-86

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 251.65  E-value: 4.93e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNY 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWT-EEGEIMAIRHKT 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 983472009 161 YPLFGLQFHPESIATEEGGKLIRAFLTEVKEEE 193
Cdd:PRK07649 160 LPIEGVQFHPESIMTSHGKELLQNFIRKYSPSV 192
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 2.31e-84

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: 247.39  E-value: 2.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAMDDGEIMAVRHNY 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 983472009  161 YPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFL 186
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-186 3.48e-80

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 236.74  E-value: 3.48e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNY 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWS-ETREIMGIRHRQ 159

                        170       180
                 ....*....|....*....|....*.
gi 983472009 161 YPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:PRK08007 160 WDLEGVQFHPESILSEQGHQLLANFL 185
trpG CHL00101
anthranilate synthase component 2
 1-186 4.39e-79

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 233.86  E-value: 4.39e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNY 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWT-EDGLIMACRHKK 159

                        170       180
                 ....*....|....*....|....*..
gi 983472009 161 YP-LFGLQFHPESIATEEGGKLIRAFL 186
Cdd:CHL00101 160 YKmLRGIQFHPESLLTTHGQQILRNFL 186
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-186 4.20e-77

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 228.99  E-value: 4.20e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILA-TAMDDG---EIMAV 156
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAwTELEDGsmdEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 983472009 157 RHNYYPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-186 2.07e-76

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 227.44  E-value: 2.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAMDDG---EIMAVR 157
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGGemdEIMGIR 160

                        170       180
                 ....*....|....*....|....*....
gi 983472009 158 HNYYPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:PRK06774 161 HRTLPLEGVQFHPESILSEQGHQLLDNFL 189
PLN02335 PLN02335
anthranilate synthase
 2-194 1.98e-71

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 215.82  E-value: 1.98e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  82 HQAIIAAFGGDIVRAER-IKHGKTSRVKHN---GTSIFSYATQPLTAMRYHSLVAEQTSLPEcfDIL-ATA-MDDGEIMA 155
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPS--DELeVTAwTEDGLIMA 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 983472009 156 VRHNYYP-LFGLQFHPESIATEEGGKLIRAF--LTEVKEEER 194
Cdd:PLN02335 179 ARHRKYKhIQGVQFHPESIITTEGKTIVRNFikIIEKKESEK 220
GATase pfam00117
Glutamine amidotransferase class-I;
3-189 1.21e-69

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 209.79  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    3 VLIDNYDSFTYNLYQLLGEYEEDIVVVRNDqITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRH-FYKNVPILGICLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   82 HQAIIAAFGGDIVRA-ERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAMDDGEIMAVRHNY 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 983472009  161 YPLFGLQFHPESIATEEGGKLIRAFLTEV 189
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-188 8.56e-69

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 208.75  E-value: 8.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKPK--GIVLSPGPGKPEDAGICIEVIRHFYK-NVPILGI 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQfdGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  79 CLGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAEQTSLPEcfDILATA-MDDGEIMAVR 157
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPA--ELEVTArTDSGVIMAVR 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 983472009 158 HNYYPLFGLQFHPESIATEEGGKLIRAFLTE 188
Cdd:PRK07765 161 HRELPIHGVQFHPESVLTEGGHRMLANWLTV 191
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-189 3.29e-63

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 193.71  E-value: 3.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   5 IDNYDSFTYNLYQLLGEYEE--DIVVVRNdQITIEQLEEMKPKGIVLSPGPGKPE---DAGICIEVIRHFYKNVPILGIC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  80 LGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAeqTSLPECFDILATAMDDGE--IMAVR 157
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGEelVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 983472009 158 HNYYPLFGLQFHPESIATEEGGKLIRAFLTEV 189
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-186 2.86e-51

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 172.52  E-value: 2.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRND---QITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGI 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  79 CLGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSLVAeqTSLPECFDIlaTAMDDGEIMAVRH 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVG--SNIPAGLTI--NAHFNGMVMAVRH 159

                        170       180
                 ....*....|....*....|....*...
gi 983472009 159 NYYPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:PRK09522 160 DADRVCGFQFHPESILTTQGARLLEQTL 187
PRK13566 PRK13566
anthranilate synthase component I;
2-179 5.82e-43

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 152.38  E-value: 5.82e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDqITIEQLEEMKPKGIVLSPGPGKPEDAGiCIEVIRHFY-KNVPILGICL 80
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFD-CKATIDAALaRNLPIFGVCL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNG-TSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHN 159
Cdd:PRK13566 607 GLQAIVEAFGGELGQLAYPMHGKPSRIRVRGpGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAET-EDGVIMAIEHK 685

                        170       180
                 ....*....|....*....|
gi 983472009 160 YYPLFGLQFHPESIATEEGG 179
Cdd:PRK13566 686 TLPVAAVQFHPESIMTLGGD 705
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-185 4.27e-40

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 144.61  E-value: 4.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   3 VLIDNYDSFTYNLYQLLGEYEE-DIVVVRNDQITIEQL-----EEMKPKGIVLSPGPGKP---EDAGICIEVIRHFyKNV 73
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIVNGvPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLLLEC-RDI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  74 PILGICLGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIF----SYATQPLTAMRYHSLVAEQTSLPE---------- 139
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKelvpiawtss 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009 140 ---------------------------CFDILATAMDDGE---------------IMAVRHNYYPLFGLQFHPESIATEE 177
Cdd:PLN02889 244 sdtlsflesqksglvpdayesqigqsgSSDPFSSKLKNGTswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIATCY 323


                 ....*...
gi 983472009 178 GGKLIRAF 185
Cdd:PLN02889 324 GRQIFKNF 331
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-186 6.86e-37

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: 135.42  E-value: 6.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    2 IVLIDNYDSFTYNLYQLLGEYEED---IVVVRNDQITIEQLEEMKP-KGIVLSPGPGKP---EDAGIcievIRHFYKN-- 72
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLEQQTDIsvhVTTVHSDTFQDQLLELLPLfDAIVVGPGPGNPnnaQDMGI----ISELWELan 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   73 ---VPILGICLGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSyATQPLTAMRYHSLVAEQTSlPECFDILATAMD 149
Cdd:TIGR01823  84 ldeVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFC-GLFSVKSTRYHSLYANPEG-IDTLLPLCLTED 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 983472009  150 DGEI--MAVRHNYYPLFGLQFHPESIATEEG-GKLIRAFL 186
Cdd:TIGR01823 162 EEGIilMSAQTKKKPWFGVQYHPESCCSELGsGKLVSNFL 201
PRK06895 PRK06895
anthranilate synthase component II;
1-187 1.11e-34

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 121.00  E-value: 1.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDQITIEQLEEMKpkGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTS-IFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHN 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVC-DENVVMAMQHK 159

                        170       180
                 ....*....|....*....|....*...
gi 983472009 160 YYPLFGLQFHPESIATEEGGKLIRAFLT 187
Cdd:PRK06895 160 TLPIYGVQFHPESYISEFGEQILRNWLA 187
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-189 3.01e-33

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: 117.03  E-value: 3.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    2 IVLIDNYDSFTynlyQL-------LGEYEEdivVVRNDQiTIEQLEEMKPKGIVLSPGPGKpEDAGICIEVIRHFYK-NV 73
Cdd:TIGR00888   1 ILVLDFGSQYT----QLiarrlreLGVYSE---LVPNTT-PLEEIREKNPKGIILSGGPSS-VYAENAPRADEKIFElGV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   74 PILGICLGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSlvAEQTSLPECFDILATAmDDGEI 153
Cdd:TIGR00888  72 PVLGICYGMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHG--DKVKELPEGFKVLATS-DNCPV 148

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 983472009  154 MAVRHNYYPLFGLQFHPESIATEEGGKLIRAFLTEV 189
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVYDV 184
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-186 7.37e-33

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 116.10  E-value: 7.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   1 MIVLIDNYDSFTYNLYQLLGEYEEDIVVVRNDqITIEQLEEMKpKGIVLSPGPGKpEDAGICIEVIRHFykNVPILGICL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAFE-DGLILSGGPDI-ERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  81 GHQAIIAAFGGDIVRAERIKHGKT--SRVKHNGtsIFSYATQPLTAMRYHSlvAEQTSLPECFDILATAmDDGEIMAVRH 158
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALVevEILDEDD--ILKGLPPEIRVWASHA--DEVKELPDGFEILARS-DICEVEAMKH 150

                        170       180
                 ....*....|....*....|....*...
gi 983472009 159 NYYPLFGLQFHPESIATEEGGKLIRAFL 186
Cdd:PRK00758 151 KEKPIYGVQFHPEVAHTEYGEEIFKNFL 178
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-178 1.43e-30

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 111.09  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLYQLLGEYEEDIVVVRNdQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  82 HQAIIAAFGGDiVRAERIKHGKT-------SRVKH---NGTSIFSYATQP------LTAMRYHSL-----VAEQTSLPEC 140
Cdd:PRK05637  83 FQALLEHHGGK-VEPCGPVHGTTdnmiltdAGVQSpvfAGLATDVEPDHPeipgrkVPIARYHSLgcvvaPDGMESLGTC 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 983472009 141 fdilATAMDDgEIMAVRHNYYPLFGLQFHPESIATEEG 178
Cdd:PRK05637 162 ----SSEIGP-VIMAAETTDGKAIGLQFHPESVLSPTG 194
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-172 7.60e-30

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: 107.97  E-value: 7.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  13 YNLYQLLGEYEEDIVVVRNDQiTIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHF-YKNVPILGICLGHQAIIAAFGG 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLlGKKIPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  92 DIVraeRIKHGktsrvkHNGtsifsyATQP----------LTAMRYHSLVAEQtSLPECFDILATAMDDGEIMAVRHNYY 161
Cdd:cd01744   89 KTY---KMKFG------HRG------SNHPvkdlitgrvyITSQNHGYAVDPD-SLPGGLEVTHVNLNDGTVEGIRHKDL 152

                        170
                 ....*....|.
gi 983472009 162 PLFGLQFHPES 172
Cdd:cd01744  153 PVFSVQFHPEA 163
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 34-186 1.17e-26

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: 99.92  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  34 ITIEQLEEMKPKGIVLSPGPG--KPEDA-GICIEVIRHfykNVPILGICLGHQAIIAAFGGDIVRAERIKHGKTSRVKHN 110
Cdd:cd01742   32 TPLEEIKLKNPKGIILSGGPSsvYEEDApRVDPEIFEL---GVPVLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009 111 GTSIFSyatqpltamryhSLVAEQT----------SLPECFDILATAmDDGEIMAVRHNYYPLFGLQFHPESIATEEGGK 180
Cdd:cd01742  109 SSPLFE------------GLPDEQTvwmshgdevvKLPEGFKVIASS-DNCPVAAIANEEKKIYGVQFHPEVTHTEKGKE 175


                 ....*.
gi 983472009 181 LIRAFL 186
Cdd:cd01742  176 ILKNFL 181
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 27-171 1.89e-25

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 100.74  E-value: 1.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  27 VVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLGHQAIIAAFGGDIvraERIKHGktsr 106
Cdd:PRK12838 192 VTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADT---EKLPFG---- 264

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983472009 107 vkHNGtsifsyATQP----------LTAMRYHSLVAEQTSLPECFDILATAMDDGEIMAVRHNYYPLFGLQFHPE 171
Cdd:PRK12838 265 --HRG------ANHPvidlttgrvwMTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPE 331
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 25-172 3.36e-24

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: 97.40  E-value: 3.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  25 DIVVVRNDqITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFY-KNVPILGICLGHQaIIA-AFGGDIVraeRIKHG 102
Cdd:COG0505  200 RVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLgKGIPIFGICLGHQ-LLAlALGAKTY---KLKFG 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009 103 ktsrvkHNGtsifsyATQP----------LTAMRyHSLVAEQTSLPEcFDILAT--AMDDGEIMAVRHNYYPLFGLQFHP 170
Cdd:COG0505  275 ------HRG------ANHPvkdletgrveITSQN-HGFAVDEDSLPA-TDLEVThvNLNDGTVEGLRHKDLPAFSVQYHP 340


                 ..
gi 983472009 171 ES 172
Cdd:COG0505  341 EA 342
guaA PRK00074
GMP synthase; Reviewed
 33-189 7.19e-24

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 97.81  E-value: 7.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  33 QITIEQLEEMKPKGIVLSPGP------GKPE-DAGIcievirhFYKNVPILGICLGHQAIIAAFGGDIVRAERIKHGKTS 105
Cdd:PRK00074  36 DISAEEIRAFNPKGIILSGGPasvyeeGAPRaDPEI-------FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009 106 RVKHNGTSIFSYATQPLTAMRYHS-LVaeqTSLPECFDILATAmDDGEIMAVRHNYYPLFGLQFHPESIATEEGGKLIRA 184
Cdd:PRK00074 109 LEVDNDSPLFKGLPEEQDVWMSHGdKV---TELPEGFKVIAST-ENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLEN 184


                 ....*
gi 983472009 185 FLTEV 189
Cdd:PRK00074 185 FVFDI 189
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
25-172 5.30e-23

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 93.99  E-value: 5.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  25 DIVVVRNDqITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFY-KNVPILGICLGHQaIIA-AFGGDIVraeRIKHG 102
Cdd:PRK12564 201 RVTVVPAT-TTAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLeKKIPIFGICLGHQ-LLAlALGAKTY---KMKFG 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009 103 ktsrvkHNGtsifsyATQP----------LTAMRyHSLVAEQTSLPECFDILATAMDDGEIMAVRHNYYPLFGLQFHPES 172
Cdd:PRK12564 276 ------HRG------ANHPvkdletgkveITSQN-HGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEA 342
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 2-172 5.59e-21

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 88.45  E-value: 5.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    2 IVLIDNydSFTYNLYQLLGEYEEDIVVVRNDQiTIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLG 81
Cdd:TIGR01368 175 VVVIDF--GVKRNILRRLVKRGCEVTVVPYDT-DAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLG 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   82 HQAIIAAFGGDIvraERIKHGktsrvkHNGtsifsyATQPLTAMRY---------HSL-VAEQTSLPECFDILATAMDDG 151
Cdd:TIGR01368 252 HQLLALAFGAKT---YKMKFG------HRG------GNHPVKDLITgrveitsqnHGYaVDPDSLPAGDLEVTHVNLNDG 316

                         170       180
                  ....*....|....*....|.
gi 983472009  152 EIMAVRHNYYPLFGLQFHPES 172
Cdd:TIGR01368 317 TVEGIRHKDLPVFSVQYHPEA 337
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-171 2.22e-20

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: 84.61  E-value: 2.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFTYNLyQLLGE------YEEDIVVVRNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIE----VIRHFYK 71
Cdd:COG0518    2 ILILDHDPFGGQYP-GLIARrlreagIELDVLRVYAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEdepaLIREAFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  72 -NVPILGICLGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPLTAMRYHSlvaEQ-TSLPECFDILATAmD 149
Cdd:COG0518   81 lGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHG---DTvTELPEGAEVLASS-D 156

                        170       180
                 ....*....|....*....|..
gi 983472009 150 DGEIMAVRHNyYPLFGLQFHPE 171
Cdd:COG0518  157 NCPNQAFRYG-RRVYGVQFHPE 177
PLN02347 PLN02347
GMP synthetase
 36-189 3.89e-19

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 84.35  E-value: 3.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  36 IEQLEEMKPKGIVLSPGP------GKPEDAGICIEVIRHfyKNVPILGICLGHQAIIAAFGGDIVRAERIKHGKTSRVKH 109
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009 110 NGTSIFSYATQPLTAMRYHSLVAEQTSLPECFDILATAmDDGEIMAVRHNYYPLFGLQFHPESIATEEGGKLIRAFLTEV 189
Cdd:PLN02347 124 CGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKS-VQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDV 202
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-172 1.10e-18

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 82.54  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  13 YNLYQLLGEYEEDIVVVrNDQITIEQLEEMKPKGIVLSPGPGKPEDAGICIEVIRHFYK-NVPILGICLGHQAIIAAFGg 91
Cdd:CHL00197 204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALE- 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  92 divraerikhGKTSRVK--HNGTSIFSYATQPL-TAMRYHSLVAEQTSLPE-CFDILATAMDDGEIMAVRHNYYPLFGLQ 167
Cdd:CHL00197 282 ----------AKTFKLKfgHRGLNHPSGLNQQVeITSQNHGFAVNLESLAKnKFYITHFNLNDGTVAGISHSPKPYFSVQ 351


                 ....*
gi 983472009 168 FHPES 172
Cdd:CHL00197 352 YHPEA 356
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 8-172 4.63e-18

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 80.79  E-value: 4.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   8 YD-SFTYNLYQLLGEYEEDIVVVRNDQITIEQLEeMKPKGIVLSPGPGKPEDAGICIEVIRHFYKNVPILGICLGHQAII 86
Cdd:PLN02771 246 YDfGIKHNILRRLASYGCKITVVPSTWPASEALK-MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLG 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  87 AAFGGDIVRAERIKHGKTSRVKHNGTSIFSYATQPltamryHSLVAEQTSLPECFDILATAMDDGEIMAVRHNYYPLFGL 166
Cdd:PLN02771 325 QALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQN------HNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSL 398


                 ....*.
gi 983472009 167 QFHPES 172
Cdd:PLN02771 399 QYHPEA 404
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-91 6.62e-12

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: 59.53  E-value: 6.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFT---YNLYQLLGEYEEDIVVVRNDQITIEQLEEM-KPKGIVLSPGPGKPEDAGIC---IEVIRHFYKN-V 73
Cdd:cd01653    1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLARDealLALLREAAAAgK 80

                         90
                 ....*....|....*...
gi 983472009  74 PILGICLGHQAIIAAFGG 91
Cdd:cd01653   81 PILGICLGAQLLVLGVQF 98
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 3.68e-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: 54.51  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   2 IVLIDNYDSFT---YNLYQLLGEYEEDIVVVRNDQITIEQLEEM-KPKGIVLSPGPGKPEDAGIC---IEVIRHFYKN-V 73
Cdd:cd03128    1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLAWDealLALLREAAAAgK 80

                         90
                 ....*....|..
gi 983472009  74 PILGICLGHQAI 85
Cdd:cd03128   81 PVLGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-185 1.90e-09

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 54.50  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  63 IEVIRHFYK-NVPILGICLGHQAIIAAFGGDIVRAERIkhgktsrvkhngTSIFSYAtqpltamryhslVAEqtsLPECF 141
Cdd:cd01745   90 LALLRAALErGKPILGICRGMQLLNVALGGTLYQDIRV------------NSLHHQA------------IKR---LADGL 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983472009 142 DILATAmDDGEIMAVRH-NYYPLFGLQFHPESIATEEGG--KLIRAF 185
Cdd:cd01745  143 RVEARA-PDGVIEAIESpDRPFVLGVQWHPEWLADTDPDslKLFEAF 188
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 63-191 2.13e-09

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: 55.17  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  63 IEVIRHFYK-NVPILGICLGHQAIIAAFGGDIVRaeRIKHGKTSRVKHNGTSIFSYATQPLT---AMRYHSLVAEQTS-- 136
Cdd:COG2071   86 LALIRAALErGKPVLGICRGMQLLNVALGGTLYQ--DLPDQVPGALDHRQPAPRYAPRHTVEiepGSRLARILGEEEIrv 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983472009 137 ----------LPECFDILATAmDDGEIMAVRHNYYP-LFGLQFHPESIAT--EEGGKLIRAFLTEVKE 191
Cdd:COG2071  164 nslhhqavkrLGPGLRVSARA-PDGVIEAIESPGAPfVLGVQWHPEWLAAsdPLSRRLFEAFVEAARA 230
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-186 3.60e-09

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 53.79  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  63 IEVIRHFYK-NVPILGICLGHQAIIAAFGGDIVRAERIKHGKTSRVKHNGT----SIFSYATQPLTAMRYHSlvaEQ-TS 136
Cdd:cd01741   71 KELIRQALAaGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAgkadPLFAGLPDEFPVFHWHG---DTvVE 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983472009 137 LPECFDILAT-AMDDGEIMAVRHNYYplfGLQFHPEsiateegGKLIRAFL 186
Cdd:cd01741  148 LPPGAVLLASsEACPNQAFRYGDRAL---GLQFHPE-------ERLLRNFL 188
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 48-176 5.59e-08

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 51.17  E-value: 5.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  48 VLSPGPGKPEDAGICIEVIRHFYKNV----------PILGICLGHQAIIAAFGGDIVRAERIK------------HGKTS 105
Cdd:cd01747   58 ILFPGGAVDIDTSGYARTAKIIYNLAlerndagdyfPVWGTCLGFELLTYLTSGETLLLEATEatnsalplnfteDALQS 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009 106 RVKHNGTS--IFSYATQPLTaMRYHSL------VAEQTSLPECFDILATAMDDGE---IMAVRHNYYPLFGLQFHPESIA 174
Cdd:cd01747  138 RLFKRFPPdlLKSLATEPLT-MNNHRYgispenFTENGLLSDFFNVLTTNDDWNGvefISTVEAYKYPIYGVQWHPEKNA 216


                 ..
gi 983472009 175 TE 176
Cdd:cd01747  217 FE 218
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 72-171 1.61e-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: 46.87  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   72 NVPILGICLGHQAIIAAFGGDIVRA-----ERIKHGKTSRVK-----HN-----GTSIFSY--ATQPLTAMRYHSLVAEq 134
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYQDiqeqpGFTDHREHCQVApyapsHAvnvepGSLLASLlgSEEFRVNSLHHQAIDR- 183

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 983472009  135 tsLPECFDILATAmDDGEIMAVRHNYYPLF--GLQFHPE 171
Cdd:pfam07722 184 --LAPGLRVEAVA-PDGTIEAIESPNAKGFalGVQWHPE 219
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-186 1.67e-04

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: 40.77  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009    2 IVLID----NYDSFTYNLyqllgEYEEDIVVVRNDQITIEQLEemkpkGIVLsPGPGKPEDA-------GICIEVIRHFY 70
Cdd:TIGR01855   1 IVIIDygvgNLGSVKRAL-----KRVGAEPVVVKDSKEAELAD-----KLIL-PGVGAFGAAmarlrenGLDLFVELVVR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009   71 KNVPILGICLGHQAI------------IAAFGGDIVRAERIKhgktsrVKHNG-TSIFSYATQPLTA-----MRY---HS 129
Cdd:TIGR01855  70 LGKPVLGICLGMQLLferseegggvpgLGLIKGNVVKLEARK------VPHMGwNEVHPVKESPLLNgidegAYFyfvHS 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 983472009  130 LVAEqtslPECFDILATAmDDGEIM--AVRHNYYplFGLQFHPESiATEEGGKLIRAFL 186
Cdd:TIGR01855 144 YYAV----CEEEAVLAYA-DYGEKFpaAVQKGNI--FGTQFHPEK-SGKTGLKLLENFL 194
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 72-171 2.33e-04

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 40.71  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472009  72 NVPILGICLGHQAIIAAFGGdivRAERIKHGKtsrvkhngTSIFSYATQPLTA---------MRYHsLVAEQTSLPECFD 142
Cdd:PRK06490  86 NKPFLGICLGAQMLARHLGA---RVAPHPDGR--------VEIGYYPLRPTEAgralmhwpeMVYH-WHREGFDLPAGAE 153

                         90       100       110
                 ....*....|....*....|....*....|
gi 983472009 143 ILATAmDDGEIMAVRhnYYP-LFGLQFHPE 171
Cdd:PRK06490 154 LLATG-DDFPNQAFR--YGDnAWGLQFHPE 180
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 46-89 2.11e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 37.53  E-value: 2.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983472009  46 GIVLSPG------PGKpedagicIEVIRHFYKN-VPILGICLGHQAIIAAF 89
Cdd:cd01746   58 GILVPGGfgirgvEGK-------ILAIKYARENnIPFLGICLGMQLAVIEF 101
 
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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