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Conserved domains on  [gi|446401410|ref|WP_000479265|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [Leptospira]

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 ...
 3-185 7.91e-122

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: 342.02  E-value: 7.91e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGH 82
Cdd:COG0512    2 LLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  83 QAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTKKh 162
Cdd:COG0512   82 QAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP- 160

                        170       180
                 ....*....|....*....|...
gi 446401410 163 LYGVQFHPESIMTGAGLDLIRNF 185
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANF 183
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 3-185 7.91e-122

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: 342.02  E-value: 7.91e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGH 82
Cdd:COG0512    2 LLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  83 QAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTKKh 162
Cdd:COG0512   82 QAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP- 160

                        170       180
                 ....*....|....*....|...
gi 446401410 163 LYGVQFHPESIMTGAGLDLIRNF 185
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANF 183
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-185 2.74e-117

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 330.55  E-value: 2.74e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTK 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*
gi 446401410 161 KhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:PRK05670 161 P-IYGVQFHPESILTEHGHKLLENF 184
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 3-185 3.77e-105

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: 299.45  E-value: 3.77e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGH 82
Cdd:cd01743    2 LLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  83 QAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTKKH 162
Cdd:cd01743   82 QAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLPI 161

                        170       180
                 ....*....|....*....|...
gi 446401410 163 lYGVQFHPESIMTGAGLDLIRNF 185
Cdd:cd01743  162 -YGVQFHPESILTEYGLRLLENF 183
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-185 1.08e-79

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: 235.45  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410    1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGV-IMGVRHKT 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 446401410  160 KKhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:TIGR00566 161 LP-LEGVQFHPESILSEQGHQLLANF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-185 1.32e-65

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 199.87  E-value: 1.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   5 IDNYDSFTYNLYQYFSQIGN--EIEVYRNdKITLDEIKHLSPKAIILSPGPGRPE---DSKVCLDVIRELGGKLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  80 LGHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLViqPESLPKELEIASKTPDG---VIMGVR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDHDgeeLVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 446401410 157 HKTkkH-LYGVQFHPESIMTGAGLDLIRNF 185
Cdd:NF041322 159 HRE--HpIECVQFHPESVLTGVGHDVIENF 186
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 2.23e-64

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 196.30  E-value: 2.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410    3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDkITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGG-KLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   82 HQAIGLVHGGKIVSAPSI-MHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGV-IMGVRHKT 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 446401410  160 KKhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:pfam00117 160 LP-IFGVQFHPESILTPHGPEILFNF 184
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 3-185 7.91e-122

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: 342.02  E-value: 7.91e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGH 82
Cdd:COG0512    2 LLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  83 QAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTKKh 162
Cdd:COG0512   82 QAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP- 160

                        170       180
                 ....*....|....*....|...
gi 446401410 163 LYGVQFHPESIMTGAGLDLIRNF 185
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANF 183
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-185 2.74e-117

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 330.55  E-value: 2.74e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTK 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*
gi 446401410 161 KhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:PRK05670 161 P-IYGVQFHPESILTEHGHKLLENF 184
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 3-185 3.77e-105

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: 299.45  E-value: 3.77e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGH 82
Cdd:cd01743    2 LLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  83 QAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTKKH 162
Cdd:cd01743   82 QAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLPI 161

                        170       180
                 ....*....|....*....|...
gi 446401410 163 lYGVQFHPESIMTGAGLDLIRNF 185
Cdd:cd01743  162 -YGVQFHPESILTEYGLRLLENF 183
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-192 1.34e-96

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 290.08  E-value: 1.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNE-IEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  80 LGHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKT 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446401410 160 kKHLYGVQFHPESIMTGAGLDLIRNFSSIVQEL 192
Cdd:PRK14607 161 -HPIFGVQFHPESILTEEGKRILKNFLNYQREE 192
trpG CHL00101
anthranilate synthase component 2
 1-185 4.65e-86

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 251.57  E-value: 4.65e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTK 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*
gi 446401410 161 KHLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:CHL00101 161 KMLRGIQFHPESLLTTHGQQILRNF 185
PLN02335 PLN02335
anthranilate synthase
 3-191 3.55e-85

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 250.48  E-value: 3.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGH 82
Cdd:PLN02335  22 IVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  83 QAIGLVHGGKIVSAPS-IMHGKISLVEHDGKD---IYKGISSPFVATRYHSLVIQPESLPK-ELEIASKTPDGVIMGVRH 157
Cdd:PLN02335 102 QCIGEAFGGKIVRSPFgVMHGKSSPVHYDEKGeegLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAARH 181

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446401410 158 KTKKHLYGVQFHPESIMTGAGLDLIRNFSSIVQE 191
Cdd:PLN02335 182 RKYKHIQGVQFHPESIITTEGKTIVRNFIKIIEK 215
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-185 5.74e-82

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 241.25  E-value: 5.74e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKTK 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180
                 ....*....|....*....|....*
gi 446401410 161 KhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:PRK07649 161 P-IEGVQFHPESIMTSHGKELLQNF 184
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-178 1.07e-80

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 238.80  E-value: 1.07e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   2 FLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKA--IILSPGPGRPEDSKVCLDVIREL-GGKLPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFdgVLLSPGPGTPERAGASIDMVRACaAAGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  79 CLGHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHK 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|
gi 446401410 159 TKKhLYGVQFHPESIMTGAG 178
Cdd:PRK07765 163 ELP-IHGVQFHPESVLTEGG 181
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-185 1.08e-79

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: 235.45  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410    1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGV-IMGVRHKT 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*.
gi 446401410  160 KKhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:TIGR00566 161 LP-LEGVQFHPESILSEQGHQLLANF 185
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-185 1.43e-79

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 235.20  E-value: 1.43e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKtK 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHR-Q 159

                        170       180
                 ....*....|....*....|....*
gi 446401410 161 KHLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:PRK08007 160 WDLEGVQFHPESILSEQGHQLLANF 184
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 2.80e-74

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 221.66  E-value: 2.80e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTP-DGV---IMGVR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSErGGEmdeIMGIR 160

                        170       180
                 ....*....|....*....|....*....
gi 446401410 157 HKTKKhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:PRK06774 161 HRTLP-LEGVQFHPESILSEQGHQLLDNF 188
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-185 1.08e-71

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 215.13  E-value: 1.08e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTP--DGV---IMGV 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGSmdeIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 446401410 156 RHKTKKhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:PRK08857 161 QHKTLP-IEAVQFHPESIKTEQGHQLLANF 189
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-185 1.32e-65

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 199.87  E-value: 1.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   5 IDNYDSFTYNLYQYFSQIGN--EIEVYRNdKITLDEIKHLSPKAIILSPGPGRPE---DSKVCLDVIRELGGKLPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEQREhaETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  80 LGHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLViqPESLPKELEIASKTPDG---VIMGVR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDHDgeeLVMGIR 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 446401410 157 HKTkkH-LYGVQFHPESIMTGAGLDLIRNF 185
Cdd:NF041322 159 HRE--HpIECVQFHPESVLTGVGHDVIENF 186
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 2.23e-64

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 196.30  E-value: 2.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410    3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDkITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGG-KLPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   82 HQAIGLVHGGKIVSAPSI-MHGKISLVEHDGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGV-IMGVRHKT 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFgHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 446401410  160 KKhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:pfam00117 160 LP-IFGVQFHPESILTPHGPEILFNF 184
PRK13566 PRK13566
anthranilate synthase component I;
3-184 1.50e-53

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 181.27  E-value: 1.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKiTLDEIKHLSPKAIILSPGPGRPEDSKV--CLDVIRELGgkLPILGVCL 80
Cdd:PRK13566 530 LLVDHEDSFVHTLANYFRQTGAEVTTVRYGF-AEEMLDRVNPDLVVLSPGPGRPSDFDCkaTIDAALARN--LPIFGVCL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKD-IYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKT 159
Cdd:PRK13566 607 GLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHKT 686

                        170       180
                 ....*....|....*....|....*...
gi 446401410 160 KKhLYGVQFHPESIMT---GAGLDLIRN 184
Cdd:PRK13566 687 LP-VAAVQFHPESIMTlggDVGLRIIEN 713
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-191 1.26e-50

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 174.65  E-value: 1.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQI-GNEIEVYRNDKITLDEIKHL--SPKA---IILSPGPG---RPEDSKVCLDVIRELGgKL 73
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVYHYlyEEKAfdnIVISPGPGsptCPADIGICLRLLLECR-DI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  74 PILGVCLGHQAIGLVHGGKIVSAPSIMHGKISLVEHDG----KDIYKGISSPFVATRYHSLVIQPESLPKEL-------- 141
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGcrlfDDIPSGRNSGFKVVRYHSLVIDAESLPKELvpiawtss 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410 142 ------------------------------EIASKTPDG---------------VIMGVRHKTKKHlYGVQFHPESIMTG 176
Cdd:PLN02889 244 sdtlsflesqksglvpdayesqigqsgssdPFSSKLKNGtswpsshsermqngkILMGIMHSTRPH-YGLQFHPESIATC 322

                        250
                 ....*....|....*
gi 446401410 177 AGLDLIRNFSSIVQE 191
Cdd:PLN02889 323 YGRQIFKNFREITQD 337
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 3-182 6.12e-49

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 166.35  E-value: 6.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRND---KITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVC 79
Cdd:PRK09522   5 LLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGIC 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  80 LGHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYHSLViqPESLPKELEIASKTpDGVIMGVRHKT 159
Cdd:PRK09522  85 LGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINAHF-NGMVMAVRHDA 161

                        170       180
                 ....*....|....*....|...
gi 446401410 160 KKhLYGVQFHPESIMTGAGLDLI 182
Cdd:PRK09522 162 DR-VCGFQFHPESILTTQGARLL 183
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 3-192 1.76e-41

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: 148.11  E-value: 1.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410    3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRND--KITLDEIKhlsPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:TIGR01815 520 LLVDHEDSFVHTLANYLRQTGASVTTLRHShaEAAFDERR---PDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCL 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDI-YKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKT 159
Cdd:TIGR01815 597 GLQGMVEAFGGALDVLPEPVHGKASRIRVLGPDAlFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRR 676

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446401410  160 KKhLYGVQFHPESIMT---GAGLDLIRNfssIVQEL 192
Cdd:TIGR01815 677 LP-LAAVQFHPESIMTldgGAGLAMIGN---VVDRL 708
PRK06895 PRK06895
anthranilate synthase component II;
1-188 1.06e-36

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 126.01  E-value: 1.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKITLDEIKHLSpkAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKD-IYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHKT 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*....
gi 446401410 160 KKhLYGVQFHPESIMTGAGLDLIRNFSSI 188
Cdd:PRK06895 161 LP-IYGVQFHPESYISEFGEQILRNWLAI 188
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 3-188 6.44e-32

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


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 121.17  E-value: 6.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410    3 LLIDNYDSFTYNLYQYFSQ---IGNEIEVYRNDKITLDEIKHLSP-KAIILSPGPGRPEDSKVcLDVIREL-----GGKL 73
Cdd:TIGR01823   9 LFIDSYDSFTYNVVRLLEQqtdISVHVTTVHSDTFQDQLLELLPLfDAIVVGPGPGNPNNAQD-MGIISELwelanLDEV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   74 PILGVCLGHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSpFVATRYHSLVIQPESLPKELE--IASKTPDGV 151
Cdd:TIGR01823  88 PVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGIDTLLPlcLTEDEEGII 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 446401410  152 IMGVRHKTKKHlYGVQFHPESIMTGAG-LDLIRNFSSI 188
Cdd:TIGR01823 167 LMSAQTKKKPW-FGVQYHPESCCSELGsGKLVSNFLKL 203
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 3-178 1.21e-28

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 105.70  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNdKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGH 82
Cdd:PRK05637   5 VLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  83 QAIGLVHGGKI-------------------VSAPsIMHGKISLVEHDGKDiYKGISSPFvaTRYHSLVIQpeSLPKELEI 143
Cdd:PRK05637  84 QALLEHHGGKVepcgpvhgttdnmiltdagVQSP-VFAGLATDVEPDHPE-IPGRKVPI--ARYHSLGCV--VAPDGMES 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446401410 144 ASKTPDG---VIMGVRHKTKKHLyGVQFHPESIMTGAG 178
Cdd:PRK05637 158 LGTCSSEigpVIMAAETTDGKAI-GLQFHPESVLSPTG 194
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 3-185 1.58e-28

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


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 105.09  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410    3 LLIDNYDSFTYNLYQYFSQIGNEIEVYRNDkITLDEIKHLSPKAIILSPGPG--RPEDSKVCLDVIRELGgkLPILGVCL 80
Cdd:TIGR00888   2 LVLDFGSQYTQLIARRLRELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSsvYAENAPRADEKIFELG--VPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   81 GHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYKGISSPFVATRYH-SLVIQpesLPKELEIASKTPDGVIMGVRHKT 159
Cdd:TIGR00888  79 GMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHgDKVKE---LPEGFKVLATSDNCPVAAMAHEE 155

                         170       180
                  ....*....|....*....|....*.
gi 446401410  160 KKhLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:TIGR00888 156 KP-IYGVQFHPEVTHTEYGNELLENF 180
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-192 1.88e-26

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 99.54  E-value: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   1 MFLLIDNYDSFTYNLYQYFSQIGNEIEVYRNDKiTLDEIKHLsPKAIILSPGPGRpEDSKVCLDVIRELggKLPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTT-PVEEIKAF-EDGLILSGGPDI-ERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  81 GHQAIGLVHGGKIVSA--PSIMHGKISLVEHDgkDIYKGISSPFVATRYHSLVIQpeSLPKELEIASKTPDGVIMGVRHK 158
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGeyGEYALVEVEILDED--DILKGLPPEIRVWASHADEVK--ELPDGFEILARSDICEVEAMKHK 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446401410 159 TkKHLYGVQFHPESIMTGAGLDLIRNFSSIVQEL 192
Cdd:PRK00758 152 E-KPIYGVQFHPEVAHTEYGEEIFKNFLEICGKY 184
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-172 1.90e-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: 99.11  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  13 YNLYQYFSQIGNEIEVYRNDKiTLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRE-LGGKLPILGVCLGHQAIGLVHGG 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKlLGKKIPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  92 KIVSAPSIMHGkislVEHDGKDIYKGISspFVATRYHSLVIQPESLPKELEIASKTP-DGVIMGVRHKTKKhLYGVQFHP 170
Cdd:cd01744   89 KTYKMKFGHRG----SNHPVKDLITGRV--YITSQNHGYAVDPDSLPGGLEVTHVNLnDGTVEGIRHKDLP-VFSVQFHP 161


                 ..
gi 446401410 171 ES 172
Cdd:cd01744  162 EA 163
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 27-185 1.81e-25

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: 96.84  E-value: 1.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  27 EVYRNDkITLDEIKHLSPKAIILSPGPG--RPEDS-KVCLDVIrELGgkLPILGVCLGHQAIGLVHGGKIVSAPSIMHGK 103
Cdd:cd01742   26 EILPNT-TPLEEIKLKNPKGIILSGGPSsvYEEDApRVDPEIF-ELG--VPVLGICYGMQLIAKALGGKVERGDKREYGK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410 104 ISLVEHDGKDIYKGISSPFVATRYHSLVIqpESLPKELEIASKTPDGVIMGVRHKTKKhLYGVQFHPESIMTGAGLDLIR 183
Cdd:cd01742  102 AEIEIDDSSPLFEGLPDEQTVWMSHGDEV--VKLPEGFKVIASSDNCPVAAIANEEKK-IYGVQFHPEVTHTEKGKEILK 178


                 ..
gi 446401410 184 NF 185
Cdd:cd01742  179 NF 180
guaA PRK00074
GMP synthase; Reviewed
 27-185 9.70e-23

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 94.34  E-value: 9.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  27 EVYRNDkITLDEIKHLSPKAIILSPGPG--RPEDSKVCLDVIRELGgkLPILGVCLGHQAIGLVHGGKIVSAPSIMHGKI 104
Cdd:PRK00074  31 EIVPYD-ISAEEIRAFNPKGIILSGGPAsvYEEGAPRADPEIFELG--VPVLGICYGMQLMAHQLGGKVERAGKREYGRA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410 105 SLVEHDGKDIYKGISSPFVATRYHSLVIqpESLPKELEIASKTPDGVIMGVRHKtKKHLYGVQFHPESIMTGAGLDLIRN 184
Cdd:PRK00074 108 ELEVDNDSPLFKGLPEEQDVWMSHGDKV--TELPEGFKVIASTENCPIAAIANE-ERKFYGVQFHPEVTHTPQGKKLLEN 184


                 .
gi 446401410 185 F 185
Cdd:PRK00074 185 F 185
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
35-172 9.91e-23

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 93.22  E-value: 9.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  35 TLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIREL-GGKLPILGVCLGHQAIGLVHGGKIVSapsiMHgkislVEHDG-- 111
Cdd:PRK12564 210 TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELlEKKIPIFGICLGHQLLALALGAKTYK----MK-----FGHRGan 280

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446401410 112 ---KDIYKGISspFVATRYHSLVIQPESLPKELEIASKTP-DGVIMGVRHKTKKhLYGVQFHPES 172
Cdd:PRK12564 281 hpvKDLETGKV--EITSQNHGFAVDEDSLPANLEVTHVNLnDGTVEGLRHKDLP-AFSVQYHPEA 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 35-172 5.90e-22

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: 91.24  E-value: 5.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  35 TLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIREL-GGKLPILGVCLGHQAIGLVHGGKIVSapsiMHgkislVEHDG-- 111
Cdd:COG0505  209 SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELlGKGIPIFGICLGHQLLALALGAKTYK----LK-----FGHRGan 279

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446401410 112 ---KDIYKG---ISSPFvatryHSLVIQPESLPK-ELEIASKTP-DGVIMGVRHKTKKhLYGVQFHPES 172
Cdd:COG0505  280 hpvKDLETGrveITSQN-----HGFAVDEDSLPAtDLEVTHVNLnDGTVEGLRHKDLP-AFSVQYHPEA 342
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 35-171 4.37e-21

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 88.80  E-value: 4.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  35 TLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGHQAIGLVHGGKIVSAPsimhgkislVEHDG--- 111
Cdd:PRK12838 200 SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLP---------FGHRGanh 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446401410 112 --KDIYKG---ISSPFvatryHSLVIQPESL-PKELEIASKT-PDGVIMGVRHKTKKhLYGVQFHPE 171
Cdd:PRK12838 271 pvIDLTTGrvwMTSQN-----HGYVVDEDSLdGTPLSVRFFNvNDGSIEGLRHKKKP-VLSVQFHPE 331
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 35-172 1.48e-20

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


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 87.30  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   35 TLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGHQAIGLVHGGKIVSAPSIMHGkislVEHDGKDI 114
Cdd:TIGR01368 205 DAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRG----GNHPVKDL 280

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  115 YKGisSPFVATRYHSLVIQPESLPK-ELEIASKTP-DGVIMGVRHKTKKhLYGVQFHPES 172
Cdd:TIGR01368 281 ITG--RVEITSQNHGYAVDPDSLPAgDLEVTHVNLnDGTVEGIRHKDLP-VFSVQYHPEA 337
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 26-171 3.22e-19

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 81.53  E-value: 3.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  26 IEVYRND----KITLDEikhlsPKAIILSPGP-------GRPEDSKVCLDVIRELGgkLPILGVCLGHQAIGLVHGGKIV 94
Cdd:COG0518   32 LRVYAGEilpyDPDLED-----PDGLILSGGPmsvydedPWLEDEPALIREAFELG--KPVLGICYGAQLLAHALGGKVE 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446401410  95 SAPS--IMHGKISLVEHDgkDIYKGISSPFVAtrYHSLVIQPESLPKELEIASKTPDGVIMGVRHktKKHLYGVQFHPE 171
Cdd:COG0518  105 PGPGreIGWAPVELTEAD--PLFAGLPDEFTV--WMSHGDTVTELPEGAEVLASSDNCPNQAFRY--GRRVYGVQFHPE 177
PLN02347 PLN02347
GMP synthetase
 36-185 1.17e-16

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 77.03  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  36 LDEIKHLSPKAIILSPGP------GRPEDSKVCLDVIRElgGKLPILGVCLGHQAIGLVHGGKIVSAPSIMHGKISLVEH 109
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446401410 110 DGKDIYKGISSPFVATRYHSLVIQPESLPKELEIASKTPDGVIMGVRHkTKKHLYGVQFHPESIMTGAGLDLIRNF 185
Cdd:PLN02347 124 CGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIEN-RERRIYGLQYHPEVTHSPKGMETLRHF 198
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 8-172 1.37e-13

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 68.08  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   8 YD-SFTYNLYQYFSQIGNEIEVYRNDKITLDEIKhLSPKAIILSPGPGRPEDSKVCLDVIRELGGKLPILGVCLGHQAIG 86
Cdd:PLN02771 246 YDfGIKHNILRRLASYGCKITVVPSTWPASEALK-MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLG 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  87 LVHGGKIVsapsimhgKISLVEHDGKDIYKGISSPFV--ATRYHSLVIQPESLPKELEIAS-KTPDGVIMGVRHKTkKHL 163
Cdd:PLN02771 325 QALGGKTF--------KMKFGHHGGNHPVRNNRTGRVeiSAQNHNYAVDPASLPEGVEVTHvNLNDGSCAGLAFPA-LNV 395


                 ....*....
gi 446401410 164 YGVQFHPES 172
Cdd:PLN02771 396 MSLQYHPEA 404
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-172 2.26e-11

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 61.35  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  13 YNLYQYFSQIGNEIEVYrNDKITLDEIKHLSPKAIILSPGPGRPEDSKVCLDVIRE-LGGKLPILGVCLGHQAIGLVHGG 91
Cdd:CHL00197 204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKlLKYNIPIFGICMGHQILSLALEA 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  92 KI---------VSAPSIMHGKISlvehdgkdiykgisspfVATRYHSLVIQPESLPKELEIAS--KTPDGVIMGVRHkTK 160
Cdd:CHL00197 283 KTfklkfghrgLNHPSGLNQQVE-----------------ITSQNHGFAVNLESLAKNKFYIThfNLNDGTVAGISH-SP 344

                        170
                 ....*....|..
gi 446401410 161 KHLYGVQFHPES 172
Cdd:CHL00197 345 KPYFSVQYHPEA 356
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 72-185 1.23e-10

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: 57.64  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  72 KLPILGVCLGHQAIGLVHGGKIVSAPS---IMHGKISLVEHDGKDI-YKGISSPFVAtrYHSLVIQPESLPKELEIASKT 147
Cdd:cd01741   81 GKPVLGICLGHQLLARALGGKVGRNPKgweIGWFPVTLTEAGKADPlFAGLPDEFPV--FHWHGDTVVELPPGAVLLASS 158

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446401410 148 PDGVIMGVRhkTKKHLYGVQFHPESIMtgagldlIRNF 185
Cdd:cd01741  159 EACPNQAFR--YGDRALGLQFHPEERL-------LRNF 187
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 72-171 4.17e-10

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: 57.10  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  72 KLPILGVCLGHQAIGLVHGGKIVSA-PSIMHGKIslvEHDGKDIYKGISspfvatryHSLVIQPES-------------- 136
Cdd:COG2071   96 GKPVLGICRGMQLLNVALGGTLYQDlPDQVPGAL---DHRQPAPRYAPR--------HTVEIEPGSrlarilgeeeirvn 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446401410 137 ---------LPKELEIASKTPDGVIMGVRHKTKKHLYGVQFHPE 171
Cdd:COG2071  165 slhhqavkrLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPE 208
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 4.94e-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: 54.53  E-value: 4.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFT---YNLYQYFSQIGNEIEVYRNDKITL-DEIKHLSPKAIILSPGPGRPEDSKVCLDVIREL----GGKLP 74
Cdd:cd01653    2 AVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVeSDVDLDDYDGLILPGGPGTPDDLARDEALLALLreaaAAGKP 81

                         90
                 ....*....|.
gi 446401410  75 ILGVCLGHQAI 85
Cdd:cd01653   82 ILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 9.69e-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: 53.36  E-value: 9.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   3 LLIDNYDSFT---YNLYQYFSQIGNEIEVYRNDKITLD-EIKHLSPKAIILSPGPGRPEDSKVCLDVIREL----GGKLP 74
Cdd:cd03128    2 AVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLAWDEALLALLreaaAAGKP 81

                         90
                 ....*....|.
gi 446401410  75 ILGVCLGHQAI 85
Cdd:cd03128   82 VLGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 72-171 2.48e-09

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 54.12  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  72 KLPILGVCLGHQAIGLVHGGKIVsaPSIMhgkislvehdgkdiykgISSpfvatrYHSLVIqpESLPKELEIASKTPDGV 151
Cdd:cd01745  100 GKPILGICRGMQLLNVALGGTLY--QDIR-----------------VNS------LHHQAI--KRLADGLRVEARAPDGV 152

                         90       100
                 ....*....|....*....|
gi 446401410 152 IMGVRHKTKKHLYGVQFHPE 171
Cdd:cd01745  153 IEAIESPDRPFVLGVQWHPE 172
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 66-171 1.42e-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: 52.64  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   66 IRE-LGGKLPILGVCLGHQAIGLVHGGKIVSAPSIMHGKISLVEHDGKDIYkgisspfvATRyHSLVIQPES-------- 136
Cdd:pfam07722  98 IRAaLARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREHCQVAPY--------APS-HAVNVEPGSllasllgs 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446401410  137 ---------------LPKELEIASKTPDGVIMGVRHKT-KKHLYGVQFHPE 171
Cdd:pfam07722 169 eefrvnslhhqaidrLAPGLRVEAVAPDGTIEAIESPNaKGFALGVQWHPE 219
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 64-185 1.26e-06

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: 46.72  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  64 DVIREL--GGKlPILGVCLGHQA-------IGLVHG-----GKIVSAPSIMHGKI------SLVEHDGKDIYKGISSP-- 121
Cdd:cd01748   62 EALKEAiaSGK-PFLGICLGMQLlfesseeGGGTKGlglipGKVVRFPASEGLKVphmgwnQLEITKESPLFKGIPDGsy 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410 122 --FVatryHSLVIQPESlpkELEIASKTPDGVIM--GVRhktKKHLYGVQFHPE-SimtG-AGLDLIRNF 185
Cdd:cd01748  141 fyFV----HSYYAPPDD---PDYILATTDYGGKFpaAVE---KDNIFGTQFHPEkS---GkAGLKLLKNF 197
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 64-191 3.47e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 45.51  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  64 DVIRELG--GKlPILGVCLGHQAI-------GLVHG-----GKIVSAPSIMHGKI------SLVEHDGKDIYKGISSP-- 121
Cdd:PRK13141  63 EVIKEAVasGK-PLLGICLGMQLLfesseefGETEGlgllpGRVRRFPPEEGLKVphmgwnQLELKKESPLLKGIPDGay 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446401410 122 --FVatryHSLVIQPEslPKELEIASKTPDGVIMGVRHKtkKHLYGVQFHPE-SimtG-AGLDLIRNFSSIVQE 191
Cdd:PRK13141 142 vyFV----HSYYADPC--DEEYVAATTDYGVEFPAAVGK--DNVFGAQFHPEkS---GdVGLKILKNFVEMVEE 204
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 46-185 9.42e-05

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: 41.54  E-value: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410   46 AIILsPGPGRPEDskvCLDVIRELG----------GKLPILGVCLGHQAIGLvHG--GKIVSAPSIMHGKISLVE----- 108
Cdd:TIGR01855  39 KLIL-PGVGAFGA---AMARLRENGldlfvelvvrLGKPVLGICLGMQLLFE-RSeeGGGVPGLGLIKGNVVKLEarkvp 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  109 HDGKD---------IYKGISSP----FVatryHSLVIQPEslpkeleiasktPDGVIMGVRHKTK-------KHLYGVQF 168
Cdd:TIGR01855 114 HMGWNevhpvkespLLNGIDEGayfyFV----HSYYAVCE------------EEAVLAYADYGEKfpaavqkGNIFGTQF 177

                         170
                  ....*....|....*..
gi 446401410  169 HPESIMTgAGLDLIRNF 185
Cdd:TIGR01855 178 HPEKSGK-TGLKLLENF 193
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 33-185 7.79e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 38.70  E-value: 7.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  33 KITLDEIKHLSPKAIILsPGPGRPEDSKVCLDVIREL------GGKlPILGVCLGHQAI-------GLVHG-----GKIV 94
Cdd:PRK13143  28 VITSDPEEILDADGIVL-PGVGAFGAAMENLSPLRDVileaarSGK-PFLGICLGMQLLfesseegGGVRGlglfpGRVV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  95 SAPSIMHgkislVEHDG-------KD--IYKGISSPFVatrY--HSLVIQPEslpkELEIASKTPDGVIMGVRHKTKKHL 163
Cdd:PRK13143 106 RFPAGVK-----VPHMGwntvkvvKDcpLFEGIDGEYV---YfvHSYYAYPD----DEDYVVATTDYGIEFPAAVCNDNV 173

                        170       180
                 ....*....|....*....|...
gi 446401410 164 YGVQFHPESimTG-AGLDLIRNF 185
Cdd:PRK13143 174 FGTQFHPEK--SGeTGLKILENF 194
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 64-185 2.30e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 37.14  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401410  64 DVIRELggKLPILGVCLGHQAIGLV---HGGkiVSAPSIMHGKISLVE-------H---------DGKDIYKGISSP--- 121
Cdd:PRK13170  64 DLIKAC--TQPVLGICLGMQLLGERseeSGG--VDCLGIIDGPVKKMTdfglplpHmgwnqvtpqAGHPLFQGIEDGsyf 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446401410 122 -FVatryHSLVIQPEslpkELEIASKT---PDGVIMGvrhktKKHLYGVQFHPE-SIMTGAglDLIRNF 185
Cdd:PRK13170 140 yFV----HSYAMPVN----EYTIAQCNygePFSAAIQ-----KDNFFGVQFHPErSGAAGA--QLLKNF 193
 
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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