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Conserved domains on  [gi|1125431596|gb|OLD60612|]
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anthranilate/aminodeoxychorismate synthase component II [Gemmatimonadetes bacterium 13_1_20CM_69_28]

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 ...
 2-189 3.53e-120

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: 338.94  E-value: 3.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRHP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*...
gi 1125431596 162 VIGLQFHPESVLTEHGYRLLDRFLHGAA 189
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELAG 188
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-189 3.53e-120

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: 338.94  E-value: 3.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRHP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*...
gi 1125431596 162 VIGLQFHPESVLTEHGYRLLDRFLHGAA 189
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELAG 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 8.66e-115

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 325.55  E-value: 8.66e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*.
gi 1125431596 161 PVIGLQFHPESVLTEHGYRLLDRFLH 186
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLE 186
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 5.04e-99

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: 285.20  E-value: 5.04e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRHP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 1125431596 162 VIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 4.72e-76

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: 227.36  E-value: 4.72e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDG-EIMAVAHVR 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*..
gi 1125431596 160 HPVIGLQFHPESVLTEHGYRLLDRFLH 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLH 187
GATase pfam00117
Glutamine amidotransferase class-I;
3-188 1.43e-65

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 200.54  E-value: 1.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   3 LLIDNYDSFVHNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRR-FGATTPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGR-PVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTAT-ADDGEIMAVAHVR 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATsENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 1125431596 160 HPVIGLQFHPESVLTEHGYRLLDRFLHGA 188
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-188 1.54e-58

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 182.92  E-value: 1.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   5 IDNYDSFVHNLARYVRELGE--ETVVRRHDAtSFEEIEQLRPSHIIISPGPCSPG---EAGISTDVVRRFGATTPILGVC 79
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEQREhaETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  80 LGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIArrGMPPVLNVTATADDGE---IMAVA 156
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIR 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1125431596 157 HVRHPVIGLQFHPESVLTEHGYRLLDRFLHGA 188
Cdd:NF041322  159 HREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-189 3.53e-120

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: 338.94  E-value: 3.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:COG0512     1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRHP 161
Cdd:COG0512    81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                         170       180
                  ....*....|....*....|....*...
gi 1125431596 162 VIGLQFHPESVLTEHGYRLLDRFLHGAA 189
Cdd:COG0512   161 IEGVQFHPESILTEHGHQLLANFLELAG 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 8.66e-115

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 325.55  E-value: 8.66e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*.
gi 1125431596 161 PVIGLQFHPESVLTEHGYRLLDRFLH 186
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLE 186
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 5.04e-99

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: 285.20  E-value: 5.04e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:cd01743     1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRHP 161
Cdd:cd01743    81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                         170       180
                  ....*....|....*....|....
gi 1125431596 162 VIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:cd01743   161 IYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-196 1.92e-91

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 278.14  E-value: 1.92e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELG-EETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVC 79
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGpEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  80 LGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVR 159
Cdd:PRK14607   81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1125431596 160 HPVIGLQFHPESVLTEHGYRLLDRFLHGAATPRHPLP 196
Cdd:PRK14607  161 HPIFGVQFHPESILTEEGKRILKNFLNYQREEIDIKS 197
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-185 1.71e-84

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 248.95  E-value: 1.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:PRK07649    1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:PRK07649   81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                         170       180
                  ....*....|....*....|....*
gi 1125431596 161 PVIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:PRK07649  161 PIEGVQFHPESIMTSHGKELLQNFI 185
trpG CHL00101
anthranilate synthase component 2
 1-185 8.61e-78

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 231.93  E-value: 8.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:CHL00101    1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:CHL00101   81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                         170       180
                  ....*....|....*....|....*.
gi 1125431596 161 PVI-GLQFHPESVLTEHGYRLLDRFL 185
Cdd:CHL00101  161 KMLrGIQFHPESLLTTHGQQILRNFL 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 4.72e-76

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: 227.36  E-value: 4.72e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDG-EIMAVAHVR 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*..
gi 1125431596 160 HPVIGLQFHPESVLTEHGYRLLDRFLH 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLH 187
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-186 8.13e-76

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 226.72  E-value: 8.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:PRK08007    1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:PRK08007   81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                         170       180
                  ....*....|....*....|....*.
gi 1125431596 161 PVIGLQFHPESVLTEHGYRLLDRFLH 186
Cdd:PRK08007  161 DLEGVQFHPESILSEQGHQLLANFLH 186
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 6.06e-74

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 222.04  E-value: 6.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:PRK06774    1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTA-TADDG---EIMAVA 156
Cdd:PRK06774   81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAwSERGGemdEIMGIR 160

                         170       180
                  ....*....|....*....|....*....
gi 1125431596 157 HVRHPVIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:PRK06774  161 HRTLPLEGVQFHPESILSEQGHQLLDNFL 189
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-185 1.31e-72

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 219.54  E-value: 1.31e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSH--IIISPGPCSPGEAGISTDVVRRFGAT-TPILGV 78
Cdd:PRK07765    3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFdgVLLSPGPGTPERAGASIDMVRACAAAgTPLLGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  79 CLGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHV 158
Cdd:PRK07765   83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                         170       180
                  ....*....|....*....|....*..
gi 1125431596 159 RHPVIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:PRK07765  163 ELPIHGVQFHPESVLTEGGHRMLANWL 189
PLN02335 PLN02335
anthranilate synthase
 2-185 2.15e-68

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 209.27  E-value: 2.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:PLN02335   21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPV-HGKASRIFHD---GRAIFAGLPNPFQAARYHSLAIARRGMPP-VLNVTATADDGEIMAVA 156
Cdd:PLN02335  101 LQCIGEAFGGKIVRSPFGVmHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                         170       180       190
                  ....*....|....*....|....*....|
gi 1125431596 157 HVRHPVI-GLQFHPESVLTEHGYRLLDRFL 185
Cdd:PLN02335  181 HRKYKHIqGVQFHPESIITTEGKTIVRNFI 210
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-185 2.96e-67

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 205.11  E-value: 2.96e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:PRK08857    1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTA--TADDG---EIMAV 155
Cdd:PRK08857   81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAwtELEDGsmdEIMGF 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1125431596 156 AHVRHPVIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:PRK08857  161 QHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
GATase pfam00117
Glutamine amidotransferase class-I;
3-188 1.43e-65

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 200.54  E-value: 1.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   3 LLIDNYDSFVHNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRR-FGATTPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGR-PVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTAT-ADDGEIMAVAHVR 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATsENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 1125431596 160 HPVIGLQFHPESVLTEHGYRLLDRFLHGA 188
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-188 1.54e-58

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 182.92  E-value: 1.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   5 IDNYDSFVHNLARYVRELGE--ETVVRRHDAtSFEEIEQLRPSHIIISPGPCSPG---EAGISTDVVRRFGATTPILGVC 79
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEQREhaETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  80 LGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIArrGMPPVLNVTATADDGE---IMAVA 156
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATTDHDGeelVMGIR 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1125431596 157 HVRHPVIGLQFHPESVLTEHGYRLLDRFLHGA 188
Cdd:NF041322  159 HREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
PRK13566 PRK13566
anthranilate synthase component I;
2-181 4.91e-52

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 178.57  E-value: 4.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:PRK13566  529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLG 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIF-HDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:PRK13566  608 LQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKTL 687

                         170       180
                  ....*....|....*....|....
gi 1125431596 161 PVIGLQFHPESVLT---EHGYRLL 181
Cdd:PRK13566  688 PVAAVQFHPESIMTlggDVGLRII 711
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-190 1.54e-49

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 169.05  E-value: 1.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHD---ATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGV 78
Cdd:PRK09522    4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  79 CLGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIArrGMPPVLNVTATAdDGEIMAVAHV 158
Cdd:PRK09522   84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGS--NIPAGLTINAHF-NGMVMAVRHD 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1125431596 159 RHPVIGLQFHPESVLTEHGYRLLDRFLHGAAT 190
Cdd:PRK09522  161 ADRVCGFQFHPESILTTQGARLLEQTLAWAQQ 192
PRK06895 PRK06895
anthranilate synthase component II;
1-185 6.06e-41

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 137.95  E-value: 6.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDATSFEEIEQLrpSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCL 80
Cdd:PRK06895    3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENF--SHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKASRIFH-DGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVR 159
Cdd:PRK06895   81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVrSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                         170       180
                  ....*....|....*....|....*.
gi 1125431596 160 HPVIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:PRK06895  161 LPIYGVQFHPESYISEFGEQILRNWL 186
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-190 2.67e-40

anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of anthranilate synthases from alpha proteobacteria and Nostoc (a cyanobacterium). This enzyme is the first step in the pathway for the biosynthesis of tryprophan from chorismate. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130874 [Multi-domain]  Cd Length: 717  Bit Score: 146.18  E-value: 2.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHdATSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRH-SHAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIF-HDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRvLGPDALFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1125431596 161 PVIGLQFHPESVLT---EHGYRLL----DRFLHGAAT 190
Cdd:TIGR01815 678 PLAAVQFHPESIMTldgGAGLAMIgnvvDRLAAGALT 714
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-187 2.05e-33

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 118.57  E-value: 2.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKAS-RIFHDGrAIFAGLPNPFQAARYHSLAIARrgMPPVLNVTATADDGEIMAVAHVRH 160
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAElEILDED-DLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDNCPVAAMAHEEK 156

                         170       180
                  ....*....|....*....|....*..
gi 1125431596 161 PVIGLQFHPESVLTEHGYRLLDRFLHG 187
Cdd:TIGR00888 157 PIYGVQFHPEVTHTEYGNELLENFVYD 183
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 2-185 3.93e-32

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 114.94  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:cd01742     1 ILILDFGSQYTHLIARRVRELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARrgMPPVLNVTATADDGEIMAVAHVRHP 161
Cdd:cd01742    80 MQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDNCPVAAIANEEKK 157

                         170       180
                  ....*....|....*....|....
gi 1125431596 162 VIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:cd01742   158 IYGVQFHPEVTHTEKGKEILKNFL 181
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 2.62e-31

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 120.72  E-value: 2.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   3 LLIDNYDSFVHNLaryVREL----GEETVVRRHDATSFEEI-----EQLRPSHIIISPGPCSP---GEAGISTDVVRRFg 70
Cdd:PLN02889   85 LLIDNYDSYTYNI---YQELsivnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLLLEC- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  71 ATTPILGVCLGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLP----NPFQAARYHSLAIARRGMPPVLNVTA- 145
Cdd:PLN02889  161 RDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAESLPKELVPIAw 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596 146 -TADD--------------------------------------------------GEI-MAVAHVRHPVIGLQFHPESVL 173
Cdd:PLN02889  241 tSSSDtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermqnGKIlMGIMHSTRPHYGLQFHPESIA 320

                         250
                  ....*....|.
gi 1125431596 174 TEHGYRLLDRF 184
Cdd:PLN02889  321 TCYGRQIFKNF 331
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-185 8.52e-29

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 106.47  E-value: 8.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDNYDSFVHNLARYVRELGEETVVRRHDaTSFEEIEQLrPSHIIISPGPcSPGEAGISTDVVRRFGatTPILGVCL 80
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKELD--VPILGICL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  81 GHQCIGAAYGAAIVRAGRPVHGKaSRIF---HDGraIFAGLPNPFQAARYHSLAIARrgMPPVLNVTATADDGEIMAVAH 157
Cdd:PRK00758   76 GHQLIAKAFGGEVGRGEYGEYAL-VEVEildEDD--ILKGLPPEIRVWASHADEVKE--LPDGFEILARSDICEVEAMKH 150

                         170       180
                  ....*....|....*....|....*...
gi 1125431596 158 VRHPVIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:PRK00758  151 KEKPIYGVQFHPEVAHTEYGEEIFKNFL 178
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-191 1.24e-27

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


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 110.00  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLaryVRELGEETVVRRH---------DATSFEEIEQLRPshIIISPGPCSPGEA---GISTDVVRRF 69
Cdd:TIGR01823   8 VLFIDSYDSFTYNV---VRLLEQQTDISVHvttvhsdtfQDQLLELLPLFDA--IVVGPGPGNPNNAqdmGIISELWELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  70 GATT-PILGVCLGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNpFQAARYHSLAiARRGMPPVLNVTATAD 148
Cdd:TIGR01823  83 NLDEvPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLY-ANPEGIDTLLPLCLTE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1125431596 149 DGE---IMAVAHVRHPVIGLQFHPESVLTEHGY-RLLDRFLHGAATP 191
Cdd:TIGR01823 161 DEEgiiLMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKLAFIN 207
guaA PRK00074
GMP synthase; Reviewed
 1-189 4.64e-27

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 107.44  E-value: 4.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   1 MILLIDnYDS-FVHNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVC 79
Cdd:PRK00074    5 KILILD-FGSqYTQLIARRVRELGVYSEIVPYD-ISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGIC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  80 LGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARrgMPPVLNVTATADDGEIMAVAHVR 159
Cdd:PRK00074   83 YGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFKVIASTENCPIAAIANEE 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1125431596 160 HPVIGLQFHPESVLTEHGYRLLDRFLHGAA 189
Cdd:PRK00074  161 RKFYGVQFHPEVTHTPQGKKLLENFVFDIC 190
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-183 1.05e-25

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 99.15  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFVHNLARYVRELGEETVVRRHDATsFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLG 81
Cdd:PRK05637    4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVP-VEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  82 HQCIGAAYGAAiVRAGRPVHGKA-----------SRIFHdGRAIFAGLPNP------FQAARYHSLAIARrgMPPVLNVT 144
Cdd:PRK05637   83 FQALLEHHGGK-VEPCGPVHGTTdnmiltdagvqSPVFA-GLATDVEPDHPeipgrkVPIARYHSLGCVV--APDGMESL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1125431596 145 ATADD--GE-IMAVAHVRHPVIGLQFHPESVLTEHGYRLLDR 183
Cdd:PRK05637  159 GTCSSeiGPvIMAAETTDGKAIGLQFHPESVLSPTGPIILSR 200
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-188 3.19e-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: 85.00  E-value: 3.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLID---NYDSFVHNLARYVRELGEETVVRRHDATSF--EEIEQLRPSHIIISPGPCSPGEAGISTDVVRR-----FGA 71
Cdd:COG0518     2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRVYAGEIlpYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPAlireaFEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  72 TTPILGVCLGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARrgMPPVLNVTATADDGE 151
Cdd:COG0518    82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTE--LPEGAEVLASSDNCP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125431596 152 IMAVAHVRHpVIGLQFHPE------------------------------SVLTEHGYRLLDRFLHGA 188
Cdd:COG0518   160 NQAFRYGRR-VYGVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLREI 225
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 3.39e-19

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: 81.39  E-value: 3.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  13 HNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRF-GATTPILGVCLGHQCIGAAYGA 91
Cdd:cd01744    10 HNILRELLKRGCEVTVVPYN-TDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLlGKKIPIFGICLGHQLLALALGA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  92 AIVR-------AGRPVhgkasRIFHDGRAifaglpnpFQAARYHSLAIARRGMPPVLNVTAT-ADDGEIMAVAHVRHPVI 163
Cdd:cd01744    89 KTYKmkfghrgSNHPV-----KDLITGRV--------YITSQNHGYAVDPDSLPGGLEVTHVnLNDGTVEGIRHKDLPVF 155


                  ....*...
gi 1125431596 164 GLQFHPES 171
Cdd:cd01744   156 SVQFHPEA 163
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 13-170 5.76e-18

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 81.09  E-value: 5.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  13 HNLARYVRELGEETVVRRHDaTSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLGHQCIGAAYGAA 92
Cdd:PRK12838  179 KSILRSLSKRGCKVTVLPYD-TSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGAD 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  93 IVR-------AGRPVHGKAS-RIfhdgraifaglpnpFQAARYHSLAIARRGMPP-VLNVTAT-ADDGEIMAVAHVRHPV 162
Cdd:PRK12838  258 TEKlpfghrgANHPVIDLTTgRV--------------WMTSQNHGYVVDEDSLDGtPLSVRFFnVNDGSIEGLRHKKKPV 323


                  ....*...
gi 1125431596 163 IGLQFHPE 170
Cdd:PRK12838  324 LSVQFHPE 331
PLN02347 PLN02347
GMP synthetase
 4-185 1.06e-17

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 80.88  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   4 LIDNYDS-FVHNLARYVRELGEETVVRRHDAtSFEEIEQLRPSHIIISPGPCSPGEAGIST------DVVRRFGAttPIL 76
Cdd:PLN02347   14 LILDYGSqYTHLITRRVRELGVYSLLLSGTA-SLDRIASLNPRVVILSGGPHSVHVEGAPTvpegffDYCRERGV--PVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  77 GVCLGHQCIGAAYGAAIVRAGRPVHGKASRIFHDGRAIFAGLPNPFQAARYHSLAIARRGMPPVLNVTATADDGEIMAVA 156
Cdd:PLN02347   91 GICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIE 170

                         170       180
                  ....*....|....*....|....*....
gi 1125431596 157 HVRHPVIGLQFHPESVLTEHGYRLLDRFL 185
Cdd:PLN02347  171 NRERRIYGLQYHPEVTHSPKGMETLRHFL 199
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 34-171 8.74e-10

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: 57.34  E-value: 8.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  34 TSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRF-GATTPILGVCLGHQCIGAAYGAAIVR-------AGRPVHGKAS 105
Cdd:COG0505   208 TSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELlGKGIPIFGICLGHQLLALALGAKTYKlkfghrgANHPVKDLET 287

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125431596 106 rifhdGRAifaglpnpFQAARYHSLAIARRGMPPvLNVTAT---ADDGEIMAVAHVRHPVIGLQFHPES 171
Cdd:COG0505   288 -----GRV--------EITSQNHGFAVDEDSLPA-TDLEVThvnLNDGTVEGLRHKDLPAFSVQYHPEA 342
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 67-185 1.25e-09

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 55.71  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  67 RRFGATTPILGVCLGHQCIGAAYGAAIVRAGRPVHGKASRIF--HDGRA--IFAGLPNPFQAARYHSLAIARrgMPPVLN 142
Cdd:cd01741    76 QALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTltEAGKAdpLFAGLPDEFPVFHWHGDTVVE--LPPGAV 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1125431596 143 VTATADDGEIMAVAhVRHPVIGLQFHPESvltehgyRLLDRFL 185
Cdd:cd01741   154 LLASSEACPNQAFR-YGDRALGLQFHPEE-------RLLRNFL 188
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
34-171 1.31e-09

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 57.01  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  34 TSFEEIEQLRPSHIIISPGPCSPGEAGISTDVVRRF-GATTPILGVCLGHQCIGAAYGAAIVR-------AGRPVHGKAS 105
Cdd:PRK12564  209 TTAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELlEKKIPIFGICLGHQLLALALGAKTYKmkfghrgANHPVKDLET 288

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125431596 106 rifhdGRAIFaglpnpfqAARYHSLAIARRGMPPVLNVTAT-ADDGEIMAVAHVRHPVIGLQFHPES 171
Cdd:PRK12564  289 -----GKVEI--------TSQNHGFAVDEDSLPANLEVTHVnLNDGTVEGLRHKDLPAFSVQYHPEA 342
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 13-171 2.25e-09

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 56.53  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  13 HNLARYVRELGEETVVRRHDATSFEEIEqLRPSHIIISPGPCSPGEAGISTDVVRRFGATTPILGVCLGHQCIGAAYGAA 92
Cdd:PLN02771  252 HNILRRLASYGCKITVVPSTWPASEALK-MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGK 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  93 IVRAGRPVHGKAsrifHDGRAIFAGLPNpfQAARYHSLAIARRGMPPVLNVT-ATADDGEIMAVAHVRHPVIGLQFHPES 171
Cdd:PLN02771  331 TFKMKFGHHGGN----HPVRNNRTGRVE--ISAQNHNYAVDPASLPEGVEVThVNLNDGSCAGLAFPALNVMSLQYHPEA 404
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-171 7.69e-09

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 54.80  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSFvhNLARYVRELGEE-TVVRRHdaTSFEEIEQLRPSHIIISPGPcspGEAGISTDVVRR----FGATTPIL 76
Cdd:CHL00197  195 IIVIDFGVKY--NILRRLKSFGCSiTVVPAT--SPYQDILSYQPDGILLSNGP---GDPSAIHYGIKTvkklLKYNIPIF 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  77 GVCLGHQCIGAAYGAAIVRAgrpvhgkasRIFHDGRAIFAGLPNPFQ-AARYHSLAIarrGMPPVLNVTATA-----DDG 150
Cdd:CHL00197  268 GICMGHQILSLALEAKTFKL---------KFGHRGLNHPSGLNQQVEiTSQNHGFAV---NLESLAKNKFYIthfnlNDG 335

                         170       180
                  ....*....|....*....|.
gi 1125431596 151 EIMAVAHVRHPVIGLQFHPES 171
Cdd:CHL00197  336 TVAGISHSPKPYFSVQYHPEA 356
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 74-170 6.51e-08

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: 51.10  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  74 PILGVCLGHQCIGAAYGAAIVRA-----GRPVHGKASRIFHDGRA---------IFAGLP--NPFQAARYHSLAIARrgM 137
Cdd:pfam07722 107 PILGICRGFQLLNVALGGTLYQDiqeqpGFTDHREHCQVAPYAPShavnvepgsLLASLLgsEEFRVNSLHHQAIDR--L 184

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1125431596 138 PPVLNVTATADDGEIMAVAHVRHP--VIGLQFHPE 170
Cdd:pfam07722 185 APGLRVEAVAPDGTIEAIESPNAKgfALGVQWHPE 219
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 1.78e-07

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: 47.58  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSF---VHNLARYVRELGEE-TVVRRHDATSFEEIEQLRPSHIIISPGPCSPGEAGISTD----VVRRFGATT 73
Cdd:cd03128     1 VAVLLFGGSEeleLASPLDALREAGAEvDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEAllalLREAAAAGK 80

                          90
                  ....*....|..
gi 1125431596  74 PILGVCLGHQCI 85
Cdd:cd03128    81 PVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-108 2.71e-07

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: 47.59  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDNYDSF---VHNLARYVRELGEE-TVVRRHDATSFEEIEQLRPSHIIISPGPCSPGE----AGISTDVVRRFGATT 73
Cdd:cd01653     1 VAVLLFPGFEeleLASPLDALREAGAEvDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDlardEALLALLREAAAAGK 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1125431596  74 PILGVCLGHQCIgaAYGAAIVRAGRPVHGKASRIF 108
Cdd:cd01653    81 PILGICLGAQLL--VLGVQFHPEAIDGAEAGARLL 113
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 74-170 4.19e-06

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: 45.64  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  74 PILGVCLGHQCIGAAYGAAIvragrpvhgkasrifhdgraifaglpnpFQAAR---YHSLAIARrgMPPVLNVTATADDG 150
Cdd:cd01745   102 PILGICRGMQLLNVALGGTL----------------------------YQDIRvnsLHHQAIKR--LADGLRVEARAPDG 151

                          90       100
                  ....*....|....*....|.
gi 1125431596 151 EIMAVAHV-RHPVIGLQFHPE 170
Cdd:cd01745   152 VIEAIESPdRPFVLGVQWHPE 172
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-185 1.28e-05

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 44.41  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596   2 ILLIDnYDSF-VHNLARYVRELGEETVVRRHDatsfEEIEQlrpSHIIISPGPCSPGEA-------GISTDVVRRFGATT 73
Cdd:cd01748     1 IAIID-YGMGnLRSVANALERLGAEVIITSDP----EEILS---ADKLILPGVGAFGDAmanlrerGLIEALKEAIASGK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  74 PILGVCLGHQ-------------CIGAaYGAAIVR----AGRPV-H-GKASRIFHDGRAIFAGLPNpfQAARY--HSLAI 132
Cdd:cd01748    73 PFLGICLGMQllfesseegggtkGLGL-IPGKVVRfpasEGLKVpHmGWNQLEITKESPLFKGIPD--GSYFYfvHSYYA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1125431596 133 ArrgMPPVLNVTATADDGEIMAVAHVRHPVIGLQFHPE-SvlTEHGYRLLDRFL 185
Cdd:cd01748   150 P---PDDPDYILATTDYGGKFPAAVEKDNIFGTQFHPEkS--GKAGLKLLKNFL 198
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 71-185 2.61e-04

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


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 40.39  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  71 ATTPILGVCLGHQCI-------GAAYGAAIVRaGRPVHGKASRIFHDG---------RAIFAGLPNpfqAARY---HSLA 131
Cdd:TIGR01855  70 LGKPVLGICLGMQLLferseegGGVPGLGLIK-GNVVKLEARKVPHMGwnevhpvkeSPLLNGIDE---GAYFyfvHSYY 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1125431596 132 iarrgMPP-VLNVTATADDGEIMAVAHVRHPVIGLQFHPESVlTEHGYRLLDRFL 185
Cdd:TIGR01855 146 -----AVCeEEAVLAYADYGEKFPAAVQKGNIFGTQFHPEKS-GKTGLKLLENFL 194
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 70-170 5.23e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 36.86  E-value: 5.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  70 GATTPILGVCLGHQCIGAAYG--AAIVRAGRPVHGKASRIFHDGR--AIFAGLPNPFQAARYHSLAIARrgMPPVLNVTA 145
Cdd:PRK09065   86 AAGMPLLGICYGHQLLAHALGgeVGYNPAGRESGTVTVELHPAAAddPLFAGLPAQFPAHLTHLQSVLR--LPPGAVVLA 163

                          90       100
                  ....*....|....*....|....*
gi 1125431596 146 TADDGEIMAVAHVRHpVIGLQFHPE 170
Cdd:PRK09065  164 RSAQDPHQAFRYGPH-AWGVQFHPE 187
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 58-170 5.25e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 36.84  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431596  58 EAGISTDVVRRFGATTPILGVCLGHQCIGAAYGAAIVRA-GRPVHGKASRIFHDGRA--IFAGLPNPFQAARYHSLAIAR 134
Cdd:PRK07567   79 EAELSGLLDEVVARDFPFLGACYGVGTLGHHQGGVVDRTyGEPVGAVTVSLTDAGRAdpLLAGLPDTFTAFVGHKEAVSA 158

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1125431596 135 rgMPPVLNVTATADDGEIMAVaHVRHPVIGLQFHPE 170
Cdd:PRK07567  159 --LPPGAVLLATSPTCPVQMF-RVGENVYATQFHPE 191
 
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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