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Conserved domains on  [gi|2495647018|ref|WP_279904547|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [unclassified Pseudomonas]

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
 1-192 5.14e-138

anthranilate synthase component II; Provisional


:

Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 382.94  E-value: 5.14e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhADGsvdEIMGL 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWT--DDG---EIMGV 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQ 192
Cdd:PRK05670  156 RHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-192 5.14e-138

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 382.94  E-value: 5.14e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhADGsvdEIMGL 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWT--DDG---EIMGV 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQ 192
Cdd:PRK05670  156 RHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-195 8.23e-138

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: 382.46  E-value: 8.23e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhADGsvdEIMGLR 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWT--EDG---EIMGIR 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2495647018 162 HKTLNIEGVQFHPESILTEQGHELFANFLKQQGG 195
Cdd:COG0512   156 HRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-190 1.83e-109

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


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 310.62  E-value: 1.83e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhADGsvdEIMGLR 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAST--EDG---VIMALR 155

                         170       180
                  ....*....|....*....|....*....
gi 2495647018 162 HKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:cd01743   156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-191 2.00e-109

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: 310.95  E-value: 2.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHAdgsvDEIMGL 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEEN----IEIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLK 191
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLH 187
GATase pfam00117
Glutamine amidotransferase class-I;
3-192 4.31e-78

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 231.36  E-value: 4.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   3 LMIDNYDSFTYNVVQYLGELGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILH-FAGKLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDVVRA-RQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHAdgsvDEIMGL 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSEND----GTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQ 192
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-190 2.21e-66

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 201.80  E-value: 2.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   5 IDNYDSFTYNVVQYLGE--LGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPT---EAGVSIEAILHFAGKLPILGVC 79
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  80 LGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVkrETLPDCLEVTAWTQHADGSVdeIMG 159
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGEEL--VMG 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 160 LRHKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:NF041322  157 IRHREHPIECVQFHPESVLTGVGHDVIENFL 187
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-192 5.14e-138

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 382.94  E-value: 5.14e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhADGsvdEIMGL 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWT--DDG---EIMGV 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQ 192
Cdd:PRK05670  156 RHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-195 8.23e-138

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: 382.46  E-value: 8.23e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhADGsvdEIMGLR 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWT--EDG---EIMGIR 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2495647018 162 HKTLNIEGVQFHPESILTEQGHELFANFLKQQGG 195
Cdd:COG0512   156 HRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-193 2.07e-121

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 341.47  E-value: 2.07e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK08857    1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHADGSVDEIMGL 160
Cdd:PRK08857   81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGSMDEIMGF 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQQ 193
Cdd:PRK08857  161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLART 193
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-191 1.34e-116

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 329.13  E-value: 1.34e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK06774    1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHaDGSVDEIMGL 160
Cdd:PRK06774   81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSER-GGEMDEIMGI 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLK 191
Cdd:PRK06774  160 RHRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-196 4.66e-111

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 315.20  E-value: 4.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHadgsvDEIMGL 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEE-----GEIMAI 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQQGGA 196
Cdd:PRK07649  156 RHKTLPIEGVQFHPESIMTSHGKELLQNFIRKYSPS 191
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-190 1.83e-109

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


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 310.62  E-value: 1.83e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhADGsvdEIMGLR 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAST--EDG---VIMALR 155

                         170       180
                  ....*....|....*....|....*....
gi 2495647018 162 HKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:cd01743   156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-191 2.00e-109

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: 310.95  E-value: 2.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHAdgsvDEIMGL 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEEN----IEIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLK 191
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLH 187
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-190 2.76e-108

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 320.12  E-value: 2.76e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGAD-VHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVC 79
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  80 LGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQhaDGsvdEIMG 159
Cdd:PRK14607   81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSD--DG---EIMG 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 160 LRHKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:PRK14607  156 IRHKEHPIFGVQFHPESILTEEGKRILKNFL 186
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-192 4.33e-107

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 304.92  E-value: 4.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK08007    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQhadgsVDEIMGL 160
Cdd:PRK08007   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSE-----TREIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQ 192
Cdd:PRK08007  156 RHRQWDLEGVQFHPESILSEQGHQLLANFLHR 187
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-197 1.25e-89

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 261.52  E-value: 1.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPE--RIVVSPGPCTPTEAGVSIEAILHFAG-KLPILGV 78
Cdd:PRK07765    3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQfdGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  79 CLGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTqhaDGSVdeIM 158
Cdd:PRK07765   83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTART---DSGV--IM 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2495647018 159 GLRHKTLNIEGVQFHPESILTEQGHELFANFLKQQGGAR 197
Cdd:PRK07765  158 AVRHRELPIHGVQFHPESVLTEGGHRMLANWLTVCGWAP 196
trpG CHL00101
anthranilate synthase component 2
 1-190 1.39e-86

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 253.12  E-value: 1.39e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:CHL00101    1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQhaDGSvdeIMGL 160
Cdd:CHL00101   81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTE--DGL---IMAC 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 161 RHKTLN-IEGVQFHPESILTEQGHELFANFL 190
Cdd:CHL00101  156 RHKKYKmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-191 2.11e-85

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 251.25  E-value: 2.11e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLG 81
Cdd:PLN02335   21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDVVRARQ-VMHGKTSPVFHEDK---GVFAGLNKPLTVTRYHSLVVKRETLP-DCLEVTAWTQhaDGSvde 156
Cdd:PLN02335  101 LQCIGEAFGGKIVRSPFgVMHGKSSPVHYDEKgeeGLFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTE--DGL--- 175

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2495647018 157 IMGLRHKTL-NIEGVQFHPESILTEQGHELFANFLK 191
Cdd:PLN02335  176 IMAARHRKYkHIQGVQFHPESIITTEGKTIVRNFIK 211
GATase pfam00117
Glutamine amidotransferase class-I;
3-192 4.31e-78

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 231.36  E-value: 4.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   3 LMIDNYDSFTYNVVQYLGELGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILH-FAGKLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDVVRA-RQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHAdgsvDEIMGL 160
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSEND----GTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLKQ 192
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-190 2.21e-66

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 201.80  E-value: 2.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   5 IDNYDSFTYNVVQYLGE--LGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPT---EAGVSIEAILHFAGKLPILGVC 79
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  80 LGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVkrETLPDCLEVTAWTQHADGSVdeIMG 159
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGEEL--VMG 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 160 LRHKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:NF041322  157 IRHREHPIECVQFHPESVLTGVGHDVIENFL 187
PRK13566 PRK13566
anthranilate synthase component I;
2-188 8.56e-51

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 173.95  E-value: 8.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDeLTIAEIEALKPERIVVSPGPCTPTEAGVS--IEAILhfAGKLPILGVC 79
Cdd:PRK13566  529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFDCKatIDAAL--ARNLPIFGVC 605

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  80 LGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKG-VFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQhaDGSvdeIM 158
Cdd:PRK13566  606 LGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETE--DGV---IM 680

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2495647018 159 GLRHKTLNIEGVQFHPESILT---EQGHELFAN 188
Cdd:PRK13566  681 AIEHKTLPVAAVQFHPESIMTlggDVGLRIIEN 713
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-190 1.81e-49

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 167.90  E-value: 1.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRND---ELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGV 78
Cdd:PRK09522    4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  79 CLGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVvkRETLPDCLEVTAwtqHADGSVdeiM 158
Cdd:PRK09522   84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA---HFNGMV---M 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 159 GLRHKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:PRK09522  156 AVRHDADRVCGFQFHPESILTTQGARLLEQTL 187
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-189 1.43e-40

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 146.15  E-value: 1.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   3 LMIDNYDSFTYNVVQYLGEL-GADVHVIRNDELTIAEI-----EALKPERIVVSPGPCTPTEA---GVSIEAILHfAGKL 73
Cdd:PLN02889   85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPTCPadiGICLRLLLE-CRDI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  74 PILGVCLGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVF----AGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQH 149
Cdd:PLN02889  164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKELVPIAWTSS 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018 150 AD------------------------GSVDE------------------------IMGLRHKTLNIEGVQFHPESILTEQ 181
Cdd:PLN02889  244 SDtlsflesqksglvpdayesqigqsGSSDPfssklkngtswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIATCY 323


                  ....*...
gi 2495647018 182 GHELFANF 189
Cdd:PLN02889  324 GRQIFKNF 331
PRK06895 PRK06895
anthranilate synthase component II;
1-190 3.80e-40

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 135.25  E-value: 3.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDELTIAEIEALkpERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCL 80
Cdd:PRK06895    3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENF--SHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFH-EDKGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAwtqHADGSVdeIMG 159
Cdd:PRK06895   81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVrSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEITA---VCDENV--VMA 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 160 LRHKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:PRK06895  156 MQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-191 2.98e-33

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 117.26  E-value: 2.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   1 MLLMIDNYDSFTYNVVQYLGELGADVHVIRNDeLTIAEIEALKpERIVVSPGPcTPTEAGVSIEAILHFagKLPILGVCL 80
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAFE-DGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRetLPDCLEVTAwtqHADgsVDEIMGL 160
Cdd:PRK00758   76 GHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKE--LPDGFEILA---RSD--ICEVEAM 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLK 191
Cdd:PRK00758  149 KHKEKPIYGVQFHPEVAHTEYGEEIFKNFLE 179
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-182 5.32e-31

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 112.25  E-value: 5.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNdELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLG 81
Cdd:PRK05637    4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  82 HQSIGQAFGGDvVRARQVMHGKTSPVFHEDKG----VFAGL------NKP------LTVTRYHSLVVKreTLPDCLEVTA 145
Cdd:PRK05637   83 FQALLEHHGGK-VEPCGPVHGTTDNMILTDAGvqspVFAGLatdvepDHPeipgrkVPIARYHSLGCV--VAPDGMESLG 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2495647018 146 WTQHADGSVdeIMGLRHKTLNIEGVQFHPESILTEQG 182
Cdd:PRK05637  160 TCSSEIGPV--IMAAETTDGKAIGLQFHPESVLSPTG 194
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-191 8.04e-31

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: 110.87  E-value: 8.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPTEAGvSIEAILH-FAGKLPILGVCL 80
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSSVYAEN-APRADEKiFELGVPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  81 GHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRetLPDCLEVTAwtqHADGSVDEIMgl 160
Cdd:TIGR00888  79 GMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLA---TSDNCPVAAM-- 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2495647018 161 RHKTLNIEGVQFHPESILTEQGHELFANFLK 191
Cdd:TIGR00888 152 AHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-190 2.07e-29

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: 107.24  E-value: 2.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   3 LMIDNYDSFTYNVVQYLGELGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLGH 82
Cdd:cd01742     2 LILDFGSQYTHLIARRVRELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  83 QSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKPLTVTRYHSLVVKRetLPDCLEVTAWTqhadgSVDEIMGLRH 162
Cdd:cd01742    81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASS-----DNCPVAAIAN 153

                         170       180
                  ....*....|....*....|....*...
gi 2495647018 163 KTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:cd01742   154 EEKKIYGVQFHPEVTHTEKGKEILKNFL 181
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-191 1.03e-28

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


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 111.92  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYL---GELGADVHVIRNDELTIAEIEALKP-ERIVVSPGPCTPTEAGVS--IEAILHFAG--KL 73
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQDQLLELLPLfDAIVVGPGPGNPNNAQDMgiISELWELANldEV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  74 PILGVCLGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFAGLNKpLTVTRYHSLVVKRETlPDCLevTAWTQHADGS 153
Cdd:TIGR01823  88 PVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEG-IDTL--LPLCLTEDEE 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2495647018 154 VDEIMGLRHKTLNIEGVQFHPESILTEQGH-ELFANFLK 191
Cdd:TIGR01823 164 GIILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLK 202
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-176 3.68e-26

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: 98.72  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  13 YNVVQYLGELGADVHVIRNDeLTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGK-LPILGVCLGHQSIGQAFGG 91
Cdd:cd01744    10 HNILRELLKRGCEVTVVPYN-TDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  92 DVVRARQVMHGKTSPVFHEDKG-VFaglnkplTVTRYHSLVVKRETLPDCLEVTAWTQHaDGSVDeimGLRHKTLNIEGV 170
Cdd:cd01744    89 KTYKMKFGHRGSNHPVKDLITGrVY-------ITSQNHGYAVDPDSLPGGLEVTHVNLN-DGTVE---GIRHKDLPVFSV 157


                  ....*.
gi 2495647018 171 QFHPES 176
Cdd:cd01744   158 QFHPEA 163
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 14-197 3.51e-24

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 97.27  E-value: 3.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  14 NVVQYLGELGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLGHQSIGQAFGGDV 93
Cdd:PRK12838  180 SILRSLSKRGCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADT 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  94 VRARQVMHGKTSPVF-HEDKGVFaglnkplTVTRYHSLVVKRETLPDCLEVTAWTQHADGSVDeimGLRHKTLNIEGVQF 172
Cdd:PRK12838  259 EKLPFGHRGANHPVIdLTTGRVW-------MTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIE---GLRHKKKPVLSVQF 328

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495647018 173 HPEsilteqGH-------ELFANFLKQQGGAR 197
Cdd:PRK12838  329 HPE------AHpgphdaeYIFDEFLEMMEKAR 354
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 13-176 7.67e-23

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


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 93.55  E-value: 7.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  13 YNVVQYLGELGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGK-LPILGVCLGHQSIGQAFGG 91
Cdd:COG0505   188 RNILRELAERGCRVTVVPATT-SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  92 DVVRARQVMHGKTSPVFHEDKG-VFaglnkpltVTRY-HSLVVKRETLPD-CLEVTawtqHA---DGSVdEimGLRHKTL 165
Cdd:COG0505   267 KTYKLKFGHRGANHPVKDLETGrVE--------ITSQnHGFAVDEDSLPAtDLEVT----HVnlnDGTV-E--GLRHKDL 331

                         170
                  ....*....|.
gi 2495647018 166 NIEGVQFHPES 176
Cdd:COG0505   332 PAFSVQYHPEA 342
guaA PRK00074
GMP synthase; Reviewed
 35-190 3.95e-22

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 92.80  E-value: 3.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  35 TIAEIEALKPERIVVSPGPCTPTEAGVS--IEAIlhFAGKLPILGVCLGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDK 112
Cdd:PRK00074   38 SAEEIRAFNPKGIILSGGPASVYEEGAPraDPEI--FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDS 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495647018 113 GVFAGLNKPLTVTRYHSLVVkrETLPDCLEVTAWTQHAdgsvdEIMGLRHKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:PRK00074  116 PLFKGLPEEQDVWMSHGDKV--TELPEGFKVIASTENC-----PIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFV 186
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
13-176 1.59e-20

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 87.44  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  13 YNVVQYLGELGADVHVIRNDElTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAG-KLPILGVCLGHQSIGQAFGG 91
Cdd:PRK12564  189 RNILRELAERGCRVTVVPATT-TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEkKIPIFGICLGHQLLALALGA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  92 DVVRARQVMHGKTSPVFHEDKG--VFAGLNkpltvtryHSLVVKRETLPDCLEVTawtqHA---DGSVdeiMGLRHKTLN 166
Cdd:PRK12564  268 KTYKMKFGHRGANHPVKDLETGkvEITSQN--------HGFAVDEDSLPANLEVT----HVnlnDGTV---EGLRHKDLP 332

                         170
                  ....*....|
gi 2495647018 167 IEGVQFHPES 176
Cdd:PRK12564  333 AFSVQYHPEA 342
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-175 5.59e-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: 83.84  E-value: 5.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   2 LLMIDNYDSFTYNVVQYLGELGADVHVIR--NDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILH-----FAGKLP 74
Cdd:COG0518     5 LDHDPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPAlireaFELGKP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  75 ILGVCLGHQSIGQAFGGDVVRARQVMHGKTsPV-FHEDKGVFAGLNKPLTVTRYHSLVVkrETLPDCLEVTAWTQHAdgs 153
Cdd:COG0518    85 VLGICYGAQLLAHALGGKVEPGPGREIGWA-PVeLTEADPLFAGLPDEFTVWMSHGDTV--TELPEGAEVLASSDNC--- 158

                         170       180
                  ....*....|....*....|..
gi 2495647018 154 vdEIMGLRHKTlNIEGVQFHPE 175
Cdd:COG0518   159 --PNQAFRYGR-RVYGVQFHPE 177
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 8-176 7.07e-18

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 80.41  E-value: 7.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   8 YD-SFTYNVVQYLGELGADVHVIRNdELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAGKLPILGVCLGHQSIG 86
Cdd:PLN02771  246 YDfGIKHNILRRLASYGCKITVVPS-TWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLG 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  87 QAFGGDVVRARQVMHGKTSPVFHEDKgvfaglNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHaDGSVdeiMGLRHKTLN 166
Cdd:PLN02771  325 QALGGKTFKMKFGHHGGNHPVRNNRT------GRVEISAQNHNYAVDPASLPEGVEVTHVNLN-DGSC---AGLAFPALN 394

                         170
                  ....*....|
gi 2495647018 167 IEGVQFHPES 176
Cdd:PLN02771  395 VMSLQYHPEA 404
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-176 1.12e-13

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 68.28  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  13 YNVVQYLGELGADVHVIrNDELTIAEIEALKPERIVVSPGPCTPTEAGVSIEAILHFAG-KLPILGVCLGHQSIGQAFGG 91
Cdd:CHL00197  204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  92 DVVRARQVMHGKTSPvfhedkgvfAGLNKPLTVT-RYHSLVVKRETL-PDCLEVTAWTQHaDGSVdeiMGLRHKTLNIEG 169
Cdd:CHL00197  283 KTFKLKFGHRGLNHP---------SGLNQQVEITsQNHGFAVNLESLaKNKFYITHFNLN-DGTV---AGISHSPKPYFS 349


                  ....*..
gi 2495647018 170 VQFHPES 176
Cdd:CHL00197  350 VQYHPEA 356
PLN02347 PLN02347
GMP synthetase
 36-190 4.06e-13

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 67.02  E-value: 4.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  36 IAEIEALKPERIVVSPGPCTPTEAGVSI--EAILHFAG--KLPILGVCLGHQSIGQAFGGDVVRARQVMHGKTSPVFHED 111
Cdd:PLN02347   46 LDRIASLNPRVVILSGGPHSVHVEGAPTvpEGFFDYCRerGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495647018 112 KGVFAGLNKPLTVTRYHSLVVKRETLPDCLEVTAWTQHADgsvdeIMGLRHKTLNIEGVQFHPESILTEQGHELFANFL 190
Cdd:PLN02347  126 SQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGA-----VVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 69-190 1.89e-11

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 59.95  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  69 FAGKLPILGVCLGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKG----VFAGLNKPLTVTRYHSLVVkrETLPDCLEVT 144
Cdd:cd01741    78 LAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadpLFAGLPDEFPVFHWHGDTV--VELPPGAVLL 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2495647018 145 AWTQHadgsvDEIMGLRhKTLNIEGVQFHPEsilteqgHELFANFL 190
Cdd:cd01741   156 ASSEA-----CPNQAFR-YGDRALGLQFHPE-------ERLLRNFL 188
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 4.95e-10

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: 54.91  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   3 LMIDNYDSFT---YNVVQYLGELGADVHVIRNDELTI-AEIEALKPERIVVSPGPCTPTEAGVS---IEAILHFAG-KLP 74
Cdd:cd01653     2 AVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVeSDVDLDDYDGLILPGGPGTPDDLARDealLALLREAAAaGKP 81

                          90
                  ....*....|.
gi 2495647018  75 ILGVCLGHQSI 85
Cdd:cd01653    82 ILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 6.39e-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: 53.74  E-value: 6.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018   3 LMIDNYDSFT---YNVVQYLGELGADVHVIRNDELTI-AEIEALKPERIVVSPGPCTPTEAGVS---IEAILHFAG-KLP 74
Cdd:cd03128     2 AVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVeSDVDLDDYDGLILPGGPGTPDDLAWDealLALLREAAAaGKP 81

                          90
                  ....*....|.
gi 2495647018  75 ILGVCLGHQSI 85
Cdd:cd03128    82 VLGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 72-175 9.83e-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: 52.58  E-value: 9.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  72 KLPILGVCLGHQSIGQAFGGDvvrarqvmhgktspvfhedkgvfagLNKPLTVTRYHSLVVKRetLPDCLEVTAWTqhAD 151
Cdd:cd01745   100 GKPILGICRGMQLLNVALGGT-------------------------LYQDIRVNSLHHQAIKR--LADGLRVEARA--PD 150

                          90       100
                  ....*....|....*....|....
gi 2495647018 152 GSVdEIMGLRHKTLNIeGVQFHPE 175
Cdd:cd01745   151 GVI-EAIESPDRPFVL-GVQWHPE 172
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 63-175 8.60e-07

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: 47.64  E-value: 8.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  63 IEAILhfAGKLPILGVCLGHQSIGQAFGG--------DVVRARQVMHGKTSPVFH------EDKGVFA---GLNKPLtVT 125
Cdd:pfam07722  98 IRAAL--ARGKPILGICRGFQLLNVALGGtlyqdiqeQPGFTDHREHCQVAPYAPshavnvEPGSLLAsllGSEEFR-VN 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2495647018 126 RYHSLVVKRetLPDCLEVTAWTqhADGSVDEIMGLRHKTLNIeGVQFHPE 175
Cdd:pfam07722 175 SLHHQAIDR--LAPGLRVEAVA--PDGTIEAIESPNAKGFAL-GVQWHPE 219
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 13-190 1.92e-06

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 46.16  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  13 YNVVQYLGELGADVHVIRNDEltiaeiEALKPERIVVsPGPCTPTEA-------GVSIEAILHFAGKLPILGVCLGHQSI 85
Cdd:TIGR01855  12 GSVKRALKRVGAEPVVVKDSK------EAELADKLIL-PGVGAFGAAmarlrenGLDLFVELVVRLGKPVLGICLGMQLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  86 GQA------------FGGDVVR--ARQVMH---GKTSPVFheDKGVFAGLNKPLTVTRYHSLVVKRETlpdcLEVTAWTQ 148
Cdd:TIGR01855  85 FERseegggvpglglIKGNVVKleARKVPHmgwNEVHPVK--ESPLLNGIDEGAYFYFVHSYYAVCEE----EAVLAYAD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2495647018 149 HadgsvdeimglRHKTL------NIEGVQFHPESIlTEQGHELFANFL 190
Cdd:TIGR01855 159 Y-----------GEKFPaavqkgNIFGTQFHPEKS-GKTGLKLLENFL 194
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 73-175 2.29e-05

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 43.41  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  73 LPILGVCLGHQSIGQAFGGDVV---RARQV--MHGKTSPVFHEDKgVFAGL--NKPLTVTRYHSLVvkreTLPDCLEVTA 145
Cdd:PRK09065   89 MPLLGICYGHQLLAHALGGEVGynpAGRESgtVTVELHPAAADDP-LFAGLpaQFPAHLTHLQSVL----RLPPGAVVLA 163

                          90       100       110
                  ....*....|....*....|....*....|
gi 2495647018 146 WTQHadgsvDEIMGLRHKTlNIEGVQFHPE 175
Cdd:PRK09065  164 RSAQ-----DPHQAFRYGP-HAWGVQFHPE 187
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 72-175 6.43e-05

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 42.08  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647018  72 KLPILGVCLGHQSIGQAFGG----DV--VRARQVMHGKTSPVFHEDKGV-------FAGL--NKPLTVTRYHSLVVKRet 136
Cdd:COG2071    96 GKPVLGICRGMQLLNVALGGtlyqDLpdQVPGALDHRQPAPRYAPRHTVeiepgsrLARIlgEEEIRVNSLHHQAVKR-- 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2495647018 137 LPDCLEVTAWTqhADGsVdeIMGLRHKTLN-IEGVQFHPE 175
Cdd:COG2071   174 LGPGLRVSARA--PDG-V--IEAIESPGAPfVLGVQWHPE 208
 
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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