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Conserved domains on  [gi|490774456|ref|WP_004636666|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [Ralstonia]

Protein Classification

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

aminodeoxychorismate/anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA), and anthranilate, an intermediate in the biosynthesis of L-tryptophan, respectively

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 7.13e-141

anthranilate synthase component II; Provisional


:

Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 389.87  E-value: 7.13e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 161 PVEGVQFHPESILSEHGHALLANFLK 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 7.13e-141

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 389.87  E-value: 7.13e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 161 PVEGVQFHPESILSEHGHALLANFLK 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-186 5.91e-140

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: 387.47  E-value: 5.91e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTLP 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*
gi 490774456 162 VEGVQFHPESILSEHGHALLANFLK 186
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLE 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 2.80e-115

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: 324.87  E-value: 2.80e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTLP 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 490774456 162 VEGVQFHPESILSEHGHALLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 7.15e-100

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: 286.30  E-value: 7.15e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456    1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDG-EIMGVRHKT 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*..
gi 490774456  160 LPVEGVQFHPESILSEHGHALLANFLK 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLH 187
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.14e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 226.74  E-value: 2.14e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456    3 LMLDNYDSFTYNIVQYFGELGQDVRTYRNDEiTIEEIEKLNPERICLSPGPCTPTEAGILVPALKH-FAGRVPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   82 HQAIADAFGGRVIRAQK-VMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGE-IMGVRHKT 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 490774456  160 LPVEGVQFHPESILSEHGHALLANFLKE 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
6-185 6.59e-61

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 187.55  E-value: 6.59e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   6 DNYDSFTYNIVQYFGELGQDVRT-YRNDEITIEEIEKLNPERICLSPGPCTPT---EAGILVPALKHFAGRVPILGVCLG 81
Cdd:NF041322   3 DNFDSFTYNLVEYVSEQREHAETtVLKNTASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVCLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIerETLPDCLEVTAWTEDGE---IMGVRHK 158
Cdd:NF041322  83 LEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGeelVMGIRHR 160

                        170       180
                 ....*....|....*....|....*..
gi 490774456 159 TLPVEGVQFHPESILSEHGHALLANFL 185
Cdd:NF041322 161 EHPIECVQFHPESVLTGVGHDVIENFL 187
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 7.13e-141

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 389.87  E-value: 7.13e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 161 PVEGVQFHPESILSEHGHALLANFLK 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-186 5.91e-140

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: 387.47  E-value: 5.91e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTLP 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*
gi 490774456 162 VEGVQFHPESILSEHGHALLANFLK 186
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLE 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 2.80e-115

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: 324.87  E-value: 2.80e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTLP 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 490774456 162 VEGVQFHPESILSEHGHALLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-185 1.15e-108

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 320.90  E-value: 1.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQD-VRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  80 LGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKT 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 160 LPVEGVQFHPESILSEHGHALLANFL 185
Cdd:PRK14607 161 HPIFGVQFHPESILTEEGKRILKNFL 186
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-186 2.04e-105

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 300.57  E-value: 2.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 161 PVEGVQFHPESILSEHGHALLANFLK 186
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFIR 186
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-186 1.68e-101

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 290.61  E-value: 1.68e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTE-DG---EIMGVR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSErGGemdEIMGIR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 490774456 157 HKTLPVEGVQFHPESILSEHGHALLANFLK 186
Cdd:PRK06774 161 HRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-186 1.98e-100

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 287.58  E-value: 1.98e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 161 PVEGVQFHPESILSEHGHALLANFLK 186
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLH 186
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-188 5.56e-100

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 286.77  E-value: 5.56e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTE--DG---EIMGV 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGsmdEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490774456 156 RHKTLPVEGVQFHPESILSEHGHALLANFLKER 188
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLART 193
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-186 7.15e-100

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: 286.30  E-value: 7.15e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456    1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDG-EIMGVRHKT 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*..
gi 490774456  160 LPVEGVQFHPESILSEHGHALLANFLK 186
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLH 187
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-185 9.17e-91

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 264.22  E-value: 9.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPE--RICLSPGPCTPTEAGILVPALKHFAG-RVPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQfdGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  79 CLGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHK 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|....*..
gi 490774456 159 TLPVEGVQFHPESILSEHGHALLANFL 185
Cdd:PRK07765 163 ELPIHGVQFHPESVLTEGGHRMLANWL 189
trpG CHL00101
anthranilate synthase component 2
 1-185 1.78e-89

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 260.05  E-value: 1.78e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 161 P-VEGVQFHPESILSEHGHALLANFL 185
Cdd:CHL00101 161 KmLRGIQFHPESLLTTHGQQILRNFL 186
PLN02335 PLN02335
anthranilate synthase
 2-186 5.29e-80

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 237.39  E-value: 5.29e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRVIRAQ-KVMHGKVSTI---ENTGVGVFANLPRHFKVTRYHSLAIERETLP-DCLEVTAWTEDGEIMGVR 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPfGVMHGKSSPVhydEKGEEGLFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTEDGLIMAAR 180

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490774456 157 HKTLP-VEGVQFHPESILSEHGHALLANFLK 186
Cdd:PLN02335 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIK 211
GATase pfam00117
Glutamine amidotransferase class-I;
3-187 2.14e-76

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 226.74  E-value: 2.14e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456    3 LMLDNYDSFTYNIVQYFGELGQDVRTYRNDEiTIEEIEKLNPERICLSPGPCTPTEAGILVPALKH-FAGRVPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   82 HQAIADAFGGRVIRAQK-VMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGE-IMGVRHKT 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*...
gi 490774456  160 LPVEGVQFHPESILSEHGHALLANFLKE 187
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
6-185 6.59e-61

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 187.55  E-value: 6.59e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   6 DNYDSFTYNIVQYFGELGQDVRT-YRNDEITIEEIEKLNPERICLSPGPCTPT---EAGILVPALKHFAGRVPILGVCLG 81
Cdd:NF041322   3 DNFDSFTYNLVEYVSEQREHAETtVLKNTASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVCLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIerETLPDCLEVTAWTEDGE---IMGVRHK 158
Cdd:NF041322  83 LEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDGeelVMGIRHR 160

                        170       180
                 ....*....|....*....|....*..
gi 490774456 159 TLPVEGVQFHPESILSEHGHALLANFL 185
Cdd:NF041322 161 EHPIECVQFHPESVLTGVGHDVIENFL 187
PRK13566 PRK13566
anthranilate synthase component I;
2-183 1.70e-57

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 191.67  E-value: 1.70e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEiTIEEIEKLNPERICLSPGPCTPTEAGI--LVPALkhFAGRVPILGVC 79
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGF-AEEMLDRVNPDLVVLSPGPGRPSDFDCkaTIDAA--LARNLPIFGVC 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  80 LGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVG-VFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHK 158
Cdd:PRK13566 606 LGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEHK 685

                        170       180
                 ....*....|....*....|....*...
gi 490774456 159 TLPVEGVQFHPESILS---EHGHALLAN 183
Cdd:PRK13566 686 TLPVAAVQFHPESIMTlggDVGLRIIEN 713
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-185 2.36e-50

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 169.82  E-value: 2.36e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRND---EITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  79 CLGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAieRETLPDCLEVTAwTEDGEIMGVRHK 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160

                        170       180
                 ....*....|....*....|....*..
gi 490774456 159 TLPVEGVQFHPESILSEHGHALLANFL 185
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTL 187
PRK06895 PRK06895
anthranilate synthase component II;
1-185 4.62e-47

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 152.58  E-value: 4.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEITIEEIEklNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVE--NFSHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVST-IENTGVGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKT 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPlKVRSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*.
gi 490774456 160 LPVEGVQFHPESILSEHGHALLANFL 185
Cdd:PRK06895 161 LPIYGVQFHPESYISEFGEQILRNWL 186
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 2-182 7.32e-42

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: 148.88  E-value: 7.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456    2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDeITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:TIGR01815 519 ILLVDHEDSFVHTLANYLRQTGASVTTLRHS-HAEAAFDERRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVCLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   82 HQAIADAFGGRVIRAQKVMHGKVSTIENTGVGV-FANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:TIGR01815 598 LQGMVEAFGGALDVLPEPVHGKASRIRVLGPDAlFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHRRL 677

                         170       180
                  ....*....|....*....|..
gi 490774456  161 PVEGVQFHPESILSEHGHALLA 182
Cdd:TIGR01815 678 PLAAVQFHPESIMTLDGGAGLA 699
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 5.67e-40

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 144.22  E-value: 5.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   3 LMLDNYDSFTYNIVQYFGEL-GQDVRTYRNDEITIEEI-----EKLNPERICLSPGPCTPTEA---GILVPALKHfAGRV 73
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPTCPadiGICLRLLLE-CRDI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  74 PILGVCLGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLP----RHFKVTRYHSLAIERETLPDCLEVTAWT-- 147
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAESLPKELVPIAWTss 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456 148 --------------------------------------------------EDGEI-MGVRHKTLPVEGVQFHPESILSEH 176
Cdd:PLN02889 244 sdtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermQNGKIlMGIMHSTRPHYGLQFHPESIATCY 323


                 ....*...
gi 490774456 177 GHALLANF 184
Cdd:PLN02889 324 GRQIFKNF 331
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-185 1.55e-35

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: 122.64  E-value: 1.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   3 LMLDNYDSFTYNIVQYFGELGQDVRTYRNDeITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLGH 82
Cdd:cd01742    2 LILDFGSQYTHLIARRVRELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  83 QAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLPRHFKVTRYHSLAIERetLPDCLEVTAWTEDGEIMGVRHKTLPV 162
Cdd:cd01742   81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDNCPVAAIANEEKKI 158

                        170       180
                 ....*....|....*....|...
gi 490774456 163 EGVQFHPESILSEHGHALLANFL 185
Cdd:cd01742  159 YGVQFHPEVTHTEKGKEILKNFL 181
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-186 1.93e-35

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: 122.81  E-value: 1.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456    2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNDEiTIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   82 HQAIADAFGGRVIRAQKVMHGKVST-IENTGVgVFANLPRHFKVTRYHSLAIERetLPDCLEVTAWTEDGEIMGVRHKTL 160
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAELeILDEDD-LFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDNCPVAAMAHEEK 156

                         170       180
                  ....*....|....*....|....*.
gi 490774456  161 PVEGVQFHPESILSEHGHALLANFLK 186
Cdd:TIGR00888 157 PIYGVQFHPEVTHTEYGNELLENFVY 182
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-181 7.76e-34

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 119.18  E-value: 7.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYRNdEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  82 HQAIADAFGGRViRAQKVMHGKVS--TIENTGVG--VFANLP------------RHFKVTRYHSLAIerETLPDCLEV-- 143
Cdd:PRK05637  83 FQALLEHHGGKV-EPCGPVHGTTDnmILTDAGVQspVFAGLAtdvepdhpeipgRKVPIARYHSLGC--VVAPDGMESlg 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490774456 144 TAWTEDGE-IMGVRHKTLPVEGVQFHPESILSEHGHALL 181
Cdd:PRK05637 160 TCSSEIGPvIMAAETTDGKAIGLQFHPESVLSPTGPIIL 198
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-186 1.45e-31

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 112.64  E-value: 1.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   1 MLLMLDNYDSFTYNIVQYFGELGQDVRTYRNDeITIEEIEKlNPERICLSPGPcTPTEAGILVPALKHFagRVPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKA-FEDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  81 GHQAIADAFGGRVIRAQKVMHGKVsTI----ENTgvgVFANLPRHFKVTRYHslAIERETLPDCLEVTAWTEDGEIMGVR 156
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALV-EVeildEDD---ILKGLPPEIRVWASH--ADEVKELPDGFEILARSDICEVEAMK 149

                        170       180       190
                 ....*....|....*....|....*....|
gi 490774456 157 HKTLPVEGVQFHPESILSEHGHALLANFLK 186
Cdd:PRK00758 150 HKEKPIYGVQFHPEVAHTEYGEEIFKNFLE 179
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-186 1.29e-28

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


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 111.54  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456    2 LLMLDNYDSFTYNIVQYF---GELGQDVRTYRNDEITIEEIEKLNP-ERICLSPGPCTPTEA---GILVPALK-HFAGRV 73
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQDQLLELLPLfDAIVVGPGPGNPNNAqdmGIISELWElANLDEV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   74 PILGVCLGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGVFANLpRHFKVTRYHSLAIERETlPDCLEVTAWTEDGE-- 151
Cdd:TIGR01823  88 PVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLYANPEG-IDTLLPLCLTEDEEgi 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 490774456  152 -IMGVRHKTLPVEGVQFHPESILSEHGHA-LLANFLK 186
Cdd:TIGR01823 166 iLMSAQTKKKPWFGVQYHPESCCSELGSGkLVSNFLK 202
guaA PRK00074
GMP synthase; Reviewed
 33-187 1.54e-27

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 107.83  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  33 EITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLGHQAIADAFGGRVIRAQKVMHGKVSTIENTGV 112
Cdd:PRK00074  36 DISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDS 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490774456 113 GVFANLPRHFKVTRYHSLAIERetLPDCLEVTAWTEDGEIMGVRHKTLPVEGVQFHPESILSEHGHALLANFLKE 187
Cdd:PRK00074 116 PLFKGLPEEQDVWMSHGDKVTE--LPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVFD 188
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 1.34e-25

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: 96.80  E-value: 1.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  13 YNIVQYFGELGQDVRTYRNDEiTIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGR-VPILGVCLGHQAIADAFGG 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  92 RVIRaqkvMHgkvstIENTGvgvfANLP-------RHFKVTRYHSLAIERETLPDCLEVTAWT-EDGEIMGVRHKTLPVE 163
Cdd:cd01744   89 KTYK----MK-----FGHRG----SNHPvkdlitgRVYITSQNHGYAVDPDSLPGGLEVTHVNlNDGTVEGIRHKDLPVF 155


                 ....*...
gi 490774456 164 GVQFHPES 171
Cdd:cd01744  156 SVQFHPEA 163
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-187 1.71e-23

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: 92.70  E-value: 1.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   2 LLMLDNYDSFTYNIVQYFGELGQDVRTYR--NDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKH-----FAGRVP 74
Cdd:COG0518    5 LDHDPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPAlireaFELGKP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  75 ILGVCLGHQAIADAFGGRVIRAQKVMHGK--VSTIENTgvGVFANLPRHFKVTRYHSLAIERetLPDCLEVTAWTEDGEI 152
Cdd:COG0518   85 VLGICYGAQLLAHALGGKVEPGPGREIGWapVELTEAD--PLFAGLPDEFTVWMSHGDTVTE--LPEGAEVLASSDNCPN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490774456 153 MGVRHKTlPVEGVQFHPE------------------------------SILSEHGHALLANFLKE 187
Cdd:COG0518  161 QAFRYGR-RVYGVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 35-170 4.10e-21

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 88.80  E-value: 4.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  35 TIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLGHQAIADAFGGRVIRAQKVMHGkvstientgvgv 114
Cdd:PRK12838 200 SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRG------------ 267

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490774456 115 fANLP-------RHFKVTRYHSLAIERETLPDCLEVTAWTE--DGEIMGVRHKTLPVEGVQFHPE 170
Cdd:PRK12838 268 -ANHPvidlttgRVWMTSQNHGYVVDEDSLDGTPLSVRFFNvnDGSIEGLRHKKKPVLSVQFHPE 331
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
35-171 3.61e-20

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 85.90  E-value: 3.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  35 TIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGR-VPILGVCLGHQAIADAFGGRVIRaqkvMH------------ 101
Cdd:PRK12564 210 TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKkIPIFGICLGHQLLALALGAKTYK----MKfghrganhpvkd 285

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490774456 102 ---GKVS-TIENtgvgvfanlprhfkvtryHSLAIERETLPDCLEVTAW-TEDGEIMGVRHKTLPVEGVQFHPES 171
Cdd:PRK12564 286 letGKVEiTSQN------------------HGFAVDEDSLPANLEVTHVnLNDGTVEGLRHKDLPAFSVQYHPEA 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 35-171 6.77e-20

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: 85.46  E-value: 6.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  35 TIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGR-VPILGVCLGHQAIADAFGGRVIRaqkvMH------------ 101
Cdd:COG0505  209 SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYK----LKfghrganhpvkd 284

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490774456 102 ---GKVS-TIENtgvgvfanlprhfkvtryHSLAIERETLPD-CLEVTaw-teDGEIMGVRHKTLPVEGVQFHPES 171
Cdd:COG0505  285 letGRVEiTSQN------------------HGFAVDEDSLPAtDLEVThvnlnDGTVEGLRHKDLPAFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 36-185 1.99e-18

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 82.04  E-value: 1.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  36 IEEIEKLNPERICLSPGPCTPTEAGI-LVPA--LKHFAGR-VPILGVCLGHQAIADAFGGRVIRAQKVMHGKVSTIENTG 111
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPHSVHVEGApTVPEgfFDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490774456 112 VGVFANLPRHFKVTRYHSLAIERETLPDCLEVTAWTEDGEIMGVRHKTLPVEGVQFHPESILSEHGHALLANFL 185
Cdd:PLN02347 126 SQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 38-176 2.80e-16

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 75.79  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  38 EIEKLNPERICLSPGPCTPTEAGILVPALKHFAGRVPILGVCLGHQAIADAFGGRVIRAQKVMHGKVSTIENtgvgvfaN 117
Cdd:PLN02771 276 EALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRN-------N 348

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490774456 118 LPRHFKVT-RYHSLAIERETLPDCLEVTAWT-EDGEIMGVRHKTLPVEGVQFHPESILSEH 176
Cdd:PLN02771 349 RTGRVEISaQNHNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVMSLQYHPEASPGPH 409
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 69-185 5.09e-16

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: 72.28  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  69 FAGRVPILGVCLGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVG----VFANLPRHFKVTRYHSLAIERetLPDCLEVT 144
Cdd:cd01741   78 LAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadpLFAGLPDEFPVFHWHGDTVVE--LPPGAVLL 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490774456 145 AWTEDGEIMGVRhKTLPVEGVQFHPEsilsehgHALLANFL 185
Cdd:cd01741  156 ASSEACPNQAFR-YGDRALGLQFHPE-------ERLLRNFL 188
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 72-170 1.70e-15

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: 70.68  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  72 RVPILGVCLGHQAIADAFGGrviraqkvmhgkvstientgvgvfaNLPRHFKVTRYHSLAIERetLPDCLEVTAWTEDGE 151
Cdd:cd01745  100 GKPILGICRGMQLLNVALGG-------------------------TLYQDIRVNSLHHQAIKR--LADGLRVEARAPDGV 152

                         90       100
                 ....*....|....*....|
gi 490774456 152 IMGVRHKTLP-VEGVQFHPE 170
Cdd:cd01745  153 IEAIESPDRPfVLGVQWHPE 172
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 13-171 4.14e-14

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 69.44  E-value: 4.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  13 YNIVQYFGELGQDVrTYRNDEITIEEIEKLNPERICLSPGPCTPTEAGILVPALKHFAGR-VPILGVCLGHQAIADAFGG 91
Cdd:CHL00197 204 YNILRRLKSFGCSI-TVVPATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYnIPIFGICMGHQILSLALEA 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  92 RVIrAQKVMHgkvstienTGVGVFANLPRHFKVT-RYHSLAIERETL-PDCLEVTAWT-EDGEIMGVRHKTLPVEGVQFH 168
Cdd:CHL00197 283 KTF-KLKFGH--------RGLNHPSGLNQQVEITsQNHGFAVNLESLaKNKFYITHFNlNDGTVAGISHSPKPYFSVQYH 353


                 ...
gi 490774456 169 PES 171
Cdd:CHL00197 354 PEA 356
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 72-170 1.94e-11

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: 60.35  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   72 RVPILGVCLGHQAIADAFGGRV---IRAQKVMHGKVSTIENTGV-----------GVFANLP--RHFKVTRYHSLAIERe 135
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLyqdIQEQPGFTDHREHCQVAPYapshavnvepgSLLASLLgsEEFRVNSLHHQAIDR- 183

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 490774456  136 tLPDCLEVTAWTEDGEIMGVRHKTLP--VEGVQFHPE 170
Cdd:pfam07722 184 -LAPGLRVEAVAPDGTIEAIESPNAKgfALGVQWHPE 219
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 72-170 2.51e-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: 57.49  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  72 RVPILGVCLGHQAIADAFGGRVI-------------RAQKVMHGKVSTIE-NTGvGVFANL--PRHFKVTRYHSLAIERe 135
Cdd:COG2071   96 GKPVLGICRGMQLLNVALGGTLYqdlpdqvpgaldhRQPAPRYAPRHTVEiEPG-SRLARIlgEEEIRVNSLHHQAVKR- 173

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490774456 136 tLPDCLEVTAWTEDGEIMGVRHKTLP-VEGVQFHPE 170
Cdd:COG2071  174 -LGPGLRVSARAPDGVIEAIESPGAPfVLGVQWHPE 208
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 2.51e-08

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: 49.90  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   3 LMLDNYDSFT---YNIVQYFGELGQDVRTYRNDEITIEEIEKL-NPERICLSPGPCTPTEAGILVPAL----KHFAGRVP 74
Cdd:cd01653    2 AVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLARDEALLallrEAAAAGKP 81

                         90
                 ....*....|.
gi 490774456  75 ILGVCLGHQAI 85
Cdd:cd01653   82 ILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-85 2.57e-08

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 49.51  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   3 LMLDNYDSFT---YNIVQYFGELGQDVRTYRNDEITIEEIEKL-NPERICLSPGPCTPTEAGILVPAL----KHFAGRVP 74
Cdd:cd03128    2 AVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLdDYDGLILPGGPGTPDDLAWDEALLallrEAAAAGKP 81

                         90
                 ....*....|.
gi 490774456  75 ILGVCLGHQAI 85
Cdd:cd03128   82 VLGICLGAQLL 92
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 62-186 1.79e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 49.40  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  62 LVPALKHFA---GRvPILGVCLGHQAIADA------------FGGRVIR------AQKVMHGKVSTIENTGVG-VFANLP 119
Cdd:PRK13146  65 LGEAVIEAVlaaGR-PFLGICVGMQLLFERglehgdtpglglIPGEVVRfqpdgpALKVPHMGWNTVDQTRDHpLFAGIP 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490774456 120 --RHFkvtrY--HSLAIERETLPDCLevtAWTEDGEIMgvrhkTLPVE-----GVQFHPE-SilSEHGHALLANFLK 186
Cdd:PRK13146 144 dgARF----YfvHSYYAQPANPADVV---AWTDYGGPF-----TAAVArdnlfATQFHPEkS--QDAGLALLRNFLA 206
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 73-170 2.39e-07

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 49.19  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  73 VPILGVCLGHQAIADAFGGRVIRAQKVMHGKVSTIENTGVGV----FANLPRHFKVTRYHSLAIERetLPDCLEVTAWTE 148
Cdd:PRK09065  89 MPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAAddplFAGLPAQFPAHLTHLQSVLR--LPPGAVVLARSA 166

                         90       100
                 ....*....|....*....|....
gi 490774456 149 -DG-EIMGVRHKTLpveGVQFHPE 170
Cdd:PRK09065 167 qDPhQAFRYGPHAW---GVQFHPE 187
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 62-185 2.18e-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: 45.95  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  62 LVPALKHFAG-RVPILGVCLGHQAIADA------------FGGRVIRAQKVMHGKV---------STIENTgvgVFANLP 119
Cdd:cd01748   60 LIEALKEAIAsGKPFLGICLGMQLLFESseegggtkglglIPGKVVRFPASEGLKVphmgwnqleITKESP---LFKGIP 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490774456 120 RHFKVtrY--HSLAIEretLPDCLEVTAWTEDGEIM--GVRHKTlpVEGVQFHPE-SilSEHGHALLANFL 185
Cdd:cd01748  137 DGSYF--YfvHSYYAP---PDDPDYILATTDYGGKFpaAVEKDN--IFGTQFHPEkS--GKAGLKLLKNFL 198
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 58-185 6.19e-06

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


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 44.62  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456   58 EAGILVPALKHFAGRVPILGVCLGHQAIADA------------FGGRVIR--AQKVMH-GKVSTIENTGVGVFANLPRHF 122
Cdd:TIGR01855  57 ENGLDLFVELVVRLGKPVLGICLGMQLLFERseegggvpglglIKGNVVKleARKVPHmGWNEVHPVKESPLLNGIDEGA 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490774456  123 KVTRYHSLAIERETlpdcLEVTAWTEDGEIM--GVRHKTlpVEGVQFHPE-SilSEHGHALLANFL 185
Cdd:TIGR01855 137 YFYFVHSYYAVCEE----EAVLAYADYGEKFpaAVQKGN--IFGTQFHPEkS--GKTGLKLLENFL 194
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 62-182 1.62e-04

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 40.79  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490774456  62 LVPALK-HFAGRVPILGVCLGHQAIADA------------FGGRVIR----AQKVMH-G--KVSTIENTGVgvFANLP-- 119
Cdd:COG0118   62 LDEAIReAVAGGKPVLGICLGMQLLFERseengdteglglIPGEVVRfpasDLKVPHmGwnTVEIAKDHPL--FAGIPdg 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490774456 120 RHFkvtrY--HSLAIERETLPDcleVTAWTEDGE--IMGVRHKtlPVEGVQFHPE-SilSEHGHALLA 182
Cdd:COG0118  140 EYF----YfvHSYYVPPDDPED---VVATTDYGVpfTAAVERG--NVFGTQFHPEkS--GAAGLRLLK 196
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 70-93 4.65e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 36.46  E-value: 4.65e-03
                         10        20
                 ....*....|....*....|....
gi 490774456  70 AGRVPILGVCLGHQAIADAFGGRV 93
Cdd:PRK07053  81 AAGLPTLGICLGAQLIARALGARV 104
 
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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