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Conserved domains on  [gi|1832516713|ref|WP_168417738|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [Acinetobacter]

Protein Classification

anthranilate synthase component II( domain architecture ID 11423509)

anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan

CATH:  3.40.50.880|3.60.120.10|3.40.50.880
EC:  4.1.3.27
Gene Ontology:  GO:0004049|GO:0000162
PubMed:  10387030|7495530|35816663
SCOP:  3001405|4002317|4003747

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 ...
 2-194 1.67e-131

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: 366.29  E-value: 1.67e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTneADGsmeEIMGVK 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWT--EDG---EIMGIR 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1832516713 162 HKTLPVEGVQFHPESILSQHGHQIFKNFLDIYA 194
Cdd:COG0512   156 HRELPIEGVQFHPESILTEHGHQLLANFLELAG 188
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-194 1.67e-131

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: 366.29  E-value: 1.67e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTneADGsmeEIMGVK 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWT--EDG---EIMGIR 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1832516713 162 HKTLPVEGVQFHPESILSQHGHQIFKNFLDIYA 194
Cdd:COG0512   156 HRELPIEGVQFHPESILTEHGHQLLANFLELAG 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-192 3.31e-131

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 365.61  E-value: 3.31e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNeaDGsmeEIMGV 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTD--DG---EIMGV 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFLDI 192
Cdd:PRK05670  156 RHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-190 1.96e-106

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: 302.92  E-value: 1.96e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEadgsmEEIMGVK 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTED-----GVIMALR 155

                         170       180
                  ....*....|....*....|....*....
gi 1832516713 162 HKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:cd01743   156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-190 4.50e-98

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: 282.06  E-value: 4.50e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEADgsmeEIMGV 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI----EIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFL 186
GATase pfam00117
Glutamine amidotransferase class-I;
3-190 6.00e-72

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 215.95  E-value: 6.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   3 LMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWqPKYLVIGPGPCSPSEAGISIPAIQH-FAGKIPLLGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEN-PDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKT-VMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEAdgsmEEIMGV 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSEND----GTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFF 185
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-194 1.67e-131

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: 366.29  E-value: 1.67e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTneADGsmeEIMGVK 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWT--EDG---EIMGIR 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1832516713 162 HKTLPVEGVQFHPESILSQHGHQIFKNFLDIYA 194
Cdd:COG0512   156 HRELPIEGVQFHPESILTEHGHQLLANFLELAG 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-192 3.31e-131

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 365.61  E-value: 3.31e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNeaDGsmeEIMGV 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTD--DG---EIMGV 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFLDI 192
Cdd:PRK05670  156 RHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-192 6.32e-107

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 316.66  E-value: 6.32e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQE-VKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVC 79
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  80 LGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNeaDGsmeEIMG 159
Cdd:PRK14607   81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSD--DG---EIMG 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1832516713 160 VKHKTLPVEGVQFHPESILSQHGHQIFKNFLDI 192
Cdd:PRK14607  156 IRHKEHPIFGVQFHPESILTEEGKRILKNFLNY 188
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-193 1.50e-106

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 303.65  E-value: 1.50e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEAdgsmeEIMGV 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEG-----EIMAI 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFLDIY 193
Cdd:PRK07649  156 RHKTLPIEGVQFHPESIMTSHGKELLQNFIRKY 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-190 1.96e-106

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: 302.92  E-value: 1.96e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEadgsmEEIMGVK 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTED-----GVIMALR 155

                         170       180
                  ....*....|....*....|....*....
gi 1832516713 162 HKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:cd01743   156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-190 1.37e-105

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 301.01  E-value: 1.37e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:PRK06774    1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTnEADGSMEEIMGV 160
Cdd:PRK06774   81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWS-ERGGEMDEIMGI 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:PRK06774  160 RHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-190 2.71e-102

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 292.94  E-value: 2.71e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:PRK08857    1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEADGSMEEIMGV 160
Cdd:PRK08857   81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGSMDEIMGF 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:PRK08857  161 QHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-190 4.50e-98

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: 282.06  E-value: 4.50e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEADgsmeEIMGV 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI----EIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFL 186
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-190 8.81e-95

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 273.72  E-value: 8.81e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:PRK08007    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEadgsmEEIMGV 160
Cdd:PRK08007   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSET-----REIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:PRK08007  156 RHRQWDLEGVQFHPESILSEQGHQLLANFL 185
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-192 1.10e-84

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 249.20  E-value: 1.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKY--LVIGPGPCSPSEAGISIPAIQHFAG-KIPLLGV 78
Cdd:PRK07765    3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFdgVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  79 CLGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTneADGSmeeIM 158
Cdd:PRK07765   83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTART--DSGV---IM 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1832516713 159 GVKHKTLPVEGVQFHPESILSQHGHQIFKNFLDI 192
Cdd:PRK07765  158 AVRHRELPIHGVQFHPESVLTEGGHRMLANWLTV 191
trpG CHL00101
anthranilate synthase component 2
 1-191 8.25e-84

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 245.80  E-value: 8.25e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:CHL00101    1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEAdgsmeEIMGV 160
Cdd:CHL00101   81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDG-----LIMAC 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1832516713 161 KHKTLP-VEGVQFHPESILSQHGHQIFKNFLD 191
Cdd:CHL00101  156 RHKKYKmLRGIQFHPESLLTTHGQQILRNFLS 187
PLN02335 PLN02335
anthranilate synthase
 2-192 8.12e-78

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 231.99  E-value: 8.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:PLN02335   21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKT-VMHGRLSDMYHSN---TGIFSNLPSPFSATRYHSLVIDQATLP-DCLEVTCWTNeaDGSmee 156
Cdd:PLN02335  101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDEkgeEGLFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTE--DGL--- 175

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1832516713 157 IMGVKHKTLP-VEGVQFHPESILSQHGHQIFKNFLDI 192
Cdd:PLN02335  176 IMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKI 212
GATase pfam00117
Glutamine amidotransferase class-I;
3-190 6.00e-72

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 215.95  E-value: 6.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   3 LMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWqPKYLVIGPGPCSPSEAGISIPAIQH-FAGKIPLLGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEN-PDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKT-VMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEAdgsmEEIMGV 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSEND----GTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFF 185
PRK13566 PRK13566
anthranilate synthase component I;
2-194 1.70e-49

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 170.48  E-value: 1.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDaVTLEDIERWQPKYLVIGPGPCSPSEAGIS--IPAIqhFAGKIPLLGVC 79
Cdd:PRK13566  529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFDCKatIDAA--LARNLPIFGVC 605

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  80 LGHQSIGQAFGGNIVRAKTVMHGRLSDMYHS-NTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNeaDGSmeeIM 158
Cdd:PRK13566  606 LGLQAIVEAFGGELGQLAYPMHGKPSRIRVRgPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETE--DGV---IM 680

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1832516713 159 GVKHKTLPVEGVQFHPESILS---QHGHQIFKNFLDIYA 194
Cdd:PRK13566  681 AIEHKTLPVAAVQFHPESIMTlggDVGLRIIENVVRLLA 719
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-192 2.39e-45

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 159.63  E-value: 2.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   3 LMIDNYDSFTYNIVQYFGELNQEVKVV-RNDAVTLEDI-----ERWQPKYLVIGPGPCSPSEA---GISIPAIQHfAGKI 73
Cdd:PLN02889   85 LLIDNYDSYTYNIYQELSIVNGVPPVVvRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPTCPadiGICLRLLLE-CRDI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  74 PLLGVCLGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLP----SPFSATRYHSLVIDQATLPDCLEVTCWTNE 149
Cdd:PLN02889  164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAESLPKELVPIAWTSS 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713 150 AD-GSMEEI-----------------------------------------------MGVKHKTLPVEGVQFHPESILSQH 181
Cdd:PLN02889  244 SDtLSFLESqksglvpdayesqigqsgssdpfssklkngtswpsshsermqngkilMGIMHSTRPHYGLQFHPESIATCY 323

                         250
                  ....*....|.
gi 1832516713 182 GHQIFKNFLDI 192
Cdd:PLN02889  324 GRQIFKNFREI 334
PRK06895 PRK06895
anthranilate synthase component II;
1-192 4.72e-44

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 144.88  E-value: 4.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDAVTLEDIERWQpkYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCL 80
Cdd:PRK06895    3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYH-SNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTcwtneADGSMEEIMG 159
Cdd:PRK06895   81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVrSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEIT-----AVCDENVVMA 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1832516713 160 VKHKTLPVEGVQFHPESILSQHGHQIFKNFLDI 192
Cdd:PRK06895  156 MQHKTLPIYGVQFHPESYISEFGEQILRNWLAI 188
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-190 1.81e-40

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 143.63  E-value: 1.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRND---AVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGV 78
Cdd:PRK09522    4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  79 CLGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSLVidQATLPDCLEVtcwtNEADGSMeeIM 158
Cdd:PRK09522   84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTI----NAHFNGM--VM 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1832516713 159 GVKHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:PRK09522  156 AVRHDADRVCGFQFHPESILTTQGARLLEQTL 187
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-192 4.58e-32

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: 121.55  E-value: 4.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYF---GELNQEVKVVRNDAVT---LEDIERWQPkyLVIGPGPCSPSEA---GIsIPAIQHFAG- 71
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQdqlLELLPLFDA--IVVGPGPGNPNNAqdmGI-ISELWELANl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  72 -KIPLLGVCLGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLpSPFSATRYHSLVIDQATlPDCLEVTCWTNEA 150
Cdd:TIGR01823  85 dEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLYANPEG-IDTLLPLCLTEDE 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1832516713 151 DGSMeeIMGVKHKTLPVEGVQFHPESILSQHGH-QIFKNFLDI 192
Cdd:TIGR01823 163 EGII--LMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKL 203
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-192 1.68e-30

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 109.94  E-value: 1.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   1 MLLMIDNYDSFTYNIVQYFGELNQEVKVVRNDaVTLEDIERwQPKYLVIGPGPcSPSEAGISIPAIQHFagKIPLLGVCL 80
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKA-FEDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  81 GHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSlviDQ-ATLPDCLEVTcwtneADGSMEEIMG 159
Cdd:PRK00758   76 GHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHA---DEvKELPDGFEIL-----ARSDICEVEA 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1832516713 160 VKHKTLPVEGVQFHPESILSQHGHQIFKNFLDI 192
Cdd:PRK00758  148 MKHKEKPIYGVQFHPEVAHTEYGEEIFKNFLEI 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-190 2.71e-29

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: 107.02  E-value: 2.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNDaVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSlviDQAT-LPDCLEVTCwtnEADGSMEEIMgv 160
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHG---DKVKeLPEGFKVLA---TSDNCPVAAM-- 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 161 KHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:TIGR00888 152 AHEEKPIYGVQFHPEVTHTEYGNELLENFV 181
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-190 3.61e-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: 3.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   3 LMIDNYDSFTYNIVQYFGELNQEVKVVRNDAvTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLGH 82
Cdd:cd01742     2 LILDFGSQYTHLIARRVRELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  83 QSIGQAFGGNIVRA------KTVMHGRLSDmyhsntGIFSNLPSPFSATRYHSlviDQAT-LPDCLEVTCWTneaDGSme 155
Cdd:cd01742    81 QLIAKALGGKVERGdkreygKAEIEIDDSS------PLFEGLPDEQTVWMSHG---DEVVkLPEGFKVIASS---DNC-- 146

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1832516713 156 EIMGVKHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:cd01742   147 PVAAIANEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-191 4.97e-27

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 101.84  E-value: 4.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVRNdAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLG 81
Cdd:PRK05637    4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  82 HQSIGQAFGGNiVRAKTVMHGRLSDMYHSNTG----IFSNLPS---PFSAT---------RYHSLVIDQAtlPDCLEVTC 145
Cdd:PRK05637   83 FQALLEHHGGK-VEPCGPVHGTTDNMILTDAGvqspVFAGLATdvePDHPEipgrkvpiaRYHSLGCVVA--PDGMESLG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1832516713 146 WTNEADGSMeeIMGVKHKTLPVEGVQFHPESILSQHGHQIFKNFLD 191
Cdd:PRK05637  160 TCSSEIGPV--IMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVE 203
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-190 1.71e-24

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 94.10  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  13 YNIVQYFGELNQEVKVVRNDAvTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGK-IPLLGVCLGHQSIGQAFGG 91
Cdd:cd01744    10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  92 NIVRAKTVMHGrlsdmyhsntgifSNLPSPFSATR--Y-----HSLVIDQATLPDCLEVTcWTNEADGSMEeimGVKHKT 164
Cdd:cd01744    89 KTYKMKFGHRG-------------SNHPVKDLITGrvYitsqnHGYAVDPDSLPGGLEVT-HVNLNDGTVE---GIRHKD 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1832516713 165 LPVEGVQFHPESilsqHG-----HQIFKNFL 190
Cdd:cd01744   152 LPVFSVQFHPEA----SPgphdtEYLFDEFL 178
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 13-176 3.39e-21

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: 88.92  E-value: 3.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  13 YNIVQYFGELNQEVKVVRNDAvTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGK-IPLLGVCLGHQSIGQAFGg 91
Cdd:COG0505   188 RNILRELAERGCRVTVVPATT-SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALG- 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  92 nivrAKTV-M----HGrlsdmyhSN-------TG---IFS-NlpspfsatryHSLVIDQATLPD-CLEVTcWTNEADGSM 154
Cdd:COG0505   266 ----AKTYkLkfghRG-------ANhpvkdleTGrveITSqN----------HGFAVDEDSLPAtDLEVT-HVNLNDGTV 323

                         170       180
                  ....*....|....*....|..
gi 1832516713 155 EeimGVKHKTLPVEGVQFHPES 176
Cdd:COG0505   324 E---GLRHKDLPAFSVQYHPEA 342
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
13-176 1.97e-20

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 87.05  E-value: 1.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  13 YNIVQYFGELNQEVKVVRNDAvTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAG-KIPLLGVCLGHQSIGQAFGG 91
Cdd:PRK12564  189 RNILRELAERGCRVTVVPATT-TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEkKIPIFGICLGHQLLALALGA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  92 NIVRAKTVMHGrlsdmyhSN-------TG---IFS-NlpspfsatryHSLVIDQATLPDCLEVTcWTNEADGSMEeimGV 160
Cdd:PRK12564  268 KTYKMKFGHRG-------ANhpvkdleTGkveITSqN----------HGFAVDEDSLPANLEVT-HVNLNDGTVE---GL 326

                         170
                  ....*....|....*.
gi 1832516713 161 KHKTLPVEGVQFHPES 176
Cdd:PRK12564  327 RHKDLPAFSVQYHPEA 342
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 25-175 1.66e-16

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 76.08  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  25 EVKVVRNDAvTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLGHQSIGQAFGGNIVRAKTVMHGRL 104
Cdd:PRK12838  191 KVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGAN 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832516713 105 SDMYHSNTGifsnlpSPFSATRYHSLVIDQATLPDCLEVTCWTNEADGSMEeimGVKHKTLPVEGVQFHPE 175
Cdd:PRK12838  270 HPVIDLTTG------RVWMTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIE---GLRHKKKPVLSVQFHPE 331
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 8-181 2.38e-15

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 73.09  E-value: 2.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   8 YD-SFTYNIVQYFGELNQEVKVVRNDAVTLEDIErWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLGHQSIG 86
Cdd:PLN02771  246 YDfGIKHNILRRLASYGCKITVVPSTWPASEALK-MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLG 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  87 QAFGGNIVRAKTVMHGrlsdmyhSNTGIFSNLPSPFS-ATRYHSLVIDQATLPDCLEVTcWTNEADGSmeeIMGVKHKTL 165
Cdd:PLN02771  325 QALGGKTFKMKFGHHG-------GNHPVRNNRTGRVEiSAQNHNYAVDPASLPEGVEVT-HVNLNDGS---CAGLAFPAL 393

                         170
                  ....*....|....*.
gi 1832516713 166 PVEGVQFHPESILSQH 181
Cdd:PLN02771  394 NVMSLQYHPEASPGPH 409
guaA PRK00074
GMP synthase; Reviewed
 34-190 2.47e-15

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 73.16  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  34 VTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAGKIPLLGVCLGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTG 113
Cdd:PRK00074   37 ISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSP 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832516713 114 IFSNLPSPFSATRYHSlviDQAT-LPDCLEVTCWTNEAdgsmeEIMGVKHKTLPVEGVQFHPESILSQHGHQIFKNFL 190
Cdd:PRK00074  117 LFKGLPEEQDVWMSHG---DKVTeLPEGFKVIASTENC-----PIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFV 186
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-191 1.99e-13

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: 66.12  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   2 LLMIDNYDSFTYNIVQYFGELNQEVKVVR---NDAV-TLEDIErwQPKYLVIGPGPCSPSEAGISIPAIQH-----FAGK 72
Cdd:COG0518     5 LDHDPFGGQYPGLIARRLREAGIELDVLRvyaGEILpYDPDLE--DPDGLILSGGPMSVYDEDPWLEDEPAlireaFELG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  73 IPLLGVCLGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTGIFSNLPSPFSATRYHSlviDQ-ATLPDCLEVTCWTnead 151
Cdd:COG0518    83 KPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHG---DTvTELPEGAEVLASS---- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713 152 gSMEEIMGVKHKTlPVEGVQFHPE------------------------------SILSQHGHQIFKNFLD 191
Cdd:COG0518   156 -DNCPNQAFRYGR-RVYGVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLR 223
PLN02347 PLN02347
GMP synthetase
 33-190 3.93e-12

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 63.94  E-value: 3.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  33 AVTLEDIERWQPKYLVIGPGPCSPSEAGI-SIPA--IQHFAGK-IPLLGVCLGHQSIGQAFGGNIVRAKTVMHGRLSDMY 108
Cdd:PLN02347   43 TASLDRIASLNPRVVILSGGPHSVHVEGApTVPEgfFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713 109 HSNTGIFSNLPSPFSATRYHSLVIDQATLPDCLEVTCWTNEADgsmeeIMGVKHKTLPVEGVQFHPESILSQHGHQIFKN 188
Cdd:PLN02347  123 VCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGA-----VVAIENRERRIYGLQYHPEVTHSPKGMETLRH 197


                  ..
gi 1832516713 189 FL 190
Cdd:PLN02347  198 FL 199
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-192 9.53e-12

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 62.51  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  13 YNIVQYFGELNQEVKVVrNDAVTLEDIERWQPKYLVIGPGPCSPSEAGISIPAIQHFAG-KIPLLGVCLGHQSIGQAFGG 91
Cdd:CHL00197  204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  92 NIVRAKTVMHG--------RLSDMYHSNTGIFSNLPSPFSATRYhslvidqatlpdcleVTCWtNEADGSmeeIMGVKHK 163
Cdd:CHL00197  283 KTFKLKFGHRGlnhpsglnQQVEITSQNHGFAVNLESLAKNKFY---------------ITHF-NLNDGT---VAGISHS 343

                         170       180       190
                  ....*....|....*....|....*....|
gi 1832516713 164 TLPVEGVQFHPESILSQH-GHQIFKNFLDI 192
Cdd:CHL00197  344 PKPYFSVQYHPEASPGPHdADYLFEYFIEI 373
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 72-175 7.62e-09

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: 53.41  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  72 KIPLLGVCLGHQSIGQAFGGNIVRA--------KTVMHGRLSDMYHSNT------GIFSNLPSP--FSATRYHSLVIDQa 135
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYQDiqeqpgftDHREHCQVAPYAPSHAvnvepgSLLASLLGSeeFRVNSLHHQAIDR- 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1832516713 136 tLPDCLEVTCWTneADGSMEEIMGVKHKTlPVEGVQFHPE 175
Cdd:pfam07722 184 -LAPGLRVEAVA--PDGTIEAIESPNAKG-FALGVQWHPE 219
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 9.74e-09

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: 51.06  E-value: 9.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   3 LMIDNYDSFT---YNIVQYFGELNQEVKVVRNDAVTLEDIERW-QPKYLVIGPGPCSPSEAGISIPAI----QHFAGKIP 74
Cdd:cd01653     2 AVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLARDEALLallrEAAAAGKP 81

                          90
                  ....*....|.
gi 1832516713  75 LLGVCLGHQSI 85
Cdd:cd01653    82 ILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 2.40e-08

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: 49.51  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713   3 LMIDNYDSFT---YNIVQYFGELNQEVKVVRNDAVTLEDIERW-QPKYLVIGPGPCSPSEAGISIPAI----QHFAGKIP 74
Cdd:cd03128     2 AVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLAWDEALLallrEAAAAGKP 81

                          90
                  ....*....|.
gi 1832516713  75 LLGVCLGHQSI 85
Cdd:cd03128    82 VLGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-189 4.98e-08

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: 50.65  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  63 IPAIQHF-AGKIPLLGVCLGHQSIGQAFGGNIVRAKTVmhgrlsdmyhsNTgifsnlpspfsatrYHSLVIDQatLPDCL 141
Cdd:cd01745    90 LALLRAAlERGKPILGICRGMQLLNVALGGTLYQDIRV-----------NS--------------LHHQAIKR--LADGL 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1832516713 142 EVTCWTneADGSMEeimGVKHKTLP-VEGVQFHPESILSQHGHQ--IFKNF 189
Cdd:cd01745   143 RVEARA--PDGVIE---AIESPDRPfVLGVQWHPEWLADTDPDSlkLFEAF 188
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 69-190 1.14e-07

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 49.55  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  69 FAGKIPLLGVCLGHQSIGQAFGGNIVRAKTVMHGRLSDMYHSNTG----IFSNLPSPFSATRYHSlviDQAT-LPDCLEV 143
Cdd:cd01741    78 LAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadpLFAGLPDEFPVFHWHG---DTVVeLPPGAVL 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1832516713 144 TcwtneADGSMEEIMGVKhKTLPVEGVQFHPEsilsqhgHQIFKNFL 190
Cdd:cd01741   155 L-----ASSEACPNQAFR-YGDRALGLQFHPE-------ERLLRNFL 188
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 74-175 2.48e-06

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 46.49  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832516713  74 PLLGVCLGHQSIGQAFGGNIV-----RAKTVMHGRLSDMYHSNTgIFSNLPSPFSATRYH--SLVidqaTLPDCLEVTCw 146
Cdd:PRK09065   90 PLLGICYGHQLLAHALGGEVGynpagRESGTVTVELHPAAADDP-LFAGLPAQFPAHLTHlqSVL----RLPPGAVVLA- 163

                          90       100
                  ....*....|....*....|....*....
gi 1832516713 147 TNEADGSmeEIMGVKHKTLpveGVQFHPE 175
Cdd:PRK09065  164 RSAQDPH--QAFRYGPHAW---GVQFHPE 187
 
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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