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Conserved domains on  [gi|740841868|ref|WP_038627121|]
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MULTISPECIES: aminodeoxychorismate/anthranilate synthase component II [Corynebacterium]

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 ...
 3-196 1.35e-119

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: 337.40  E-value: 1.35e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVvkQFDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEAL--APDGIVLSPGPGTPEEAGISLEVIRAFAGK---IPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:COG0512   76 GVCLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIR 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWLRLAGG 196
Cdd:COG0512  156 HRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 3-196 1.35e-119

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: 337.40  E-value: 1.35e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVvkQFDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEAL--APDGIVLSPGPGTPEEAGISLEVIRAFAGK---IPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:COG0512   76 GVCLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIR 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWLRLAGG 196
Cdd:COG0512  156 HRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
1-195 4.17e-117

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 332.40  E-value: 4.17e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   1 MQILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQDdpTP 80
Cdd:PRK07765   1 MRILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAAG--TP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  81 VLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMA 160
Cdd:PRK07765  79 LLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 740841868 161 MRHRDLPIHGVQYHPESVLTQYGHRMLVNWLRLAG 195
Cdd:PRK07765 159 VRHRELPIHGVQFHPESVLTEGGHRMLANWLTVCG 193
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 3-191 4.69e-99

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


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 285.58  E-value: 4.69e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDvvKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELEL--LNPDAIVISPGPGHPEDAGISLEIIRALAGK---VPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:cd01743   76 GVCLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALR 155

                        170       180
                 ....*....|....*....|....*....
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:cd01743  156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-193 8.81e-72

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: 216.58  E-value: 8.81e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868    3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFdaILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLL--IVISPGPCTPNEAGISLEAIRHFAGK---LPIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGM-LMAM 161
Cdd:TIGR00566  77 GVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 740841868  162 RHRDLPIHGVQYHPESVLTQYGHRMLVNWLRL 193
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase pfam00117
Glutamine amidotransferase class-I;
4-194 2.73e-67

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 205.16  E-value: 2.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868    4 LVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDvvkQFDAILLSPGPGEPSNAGWTEDIIRAVSRQDdpTPVLG 83
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEE---NPDGIILSGGPGSPGAAGGAIEAIREARELK--IPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   84 VCLGHQAIGEVFGAQVVRA-DELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGM-LMAM 161
Cdd:pfam00117  76 ICLGHQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 740841868  162 RHRDLPIHGVQYHPESVLTQYGHRMLVNWLRLA 194
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-194 6.31e-57

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 178.69  E-value: 6.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   5 VVDNYDSFVFNLVQYIGQLGET--VTVWRNDdARLRDVDDVvkQFDAILLSPGPGEPSNA---GWTEDIIRAVSRQddpT 79
Cdd:NF041322   1 FVDNFDSFTYNLVEYVSEQREHaeTTVLKNT-ASLAEVRAV--DPDAIVISPGPGHPKNDrdvGVTADVLRELSPE---V 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  80 PVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVdpKTLPEELIATAFTDSG--- 156
Cdd:NF041322  75 PTLGVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDgee 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 740841868 157 MLMAMRHRDLPIHGVQYHPESVLTQYGHRMLVNWLRLA 194
Cdd:NF041322 153 LVMGIRHREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 3-196 1.35e-119

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: 337.40  E-value: 1.35e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVvkQFDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEAL--APDGIVLSPGPGTPEEAGISLEVIRAFAGK---IPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:COG0512   76 GVCLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIR 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWLRLAGG 196
Cdd:COG0512  156 HRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
1-195 4.17e-117

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 332.40  E-value: 4.17e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   1 MQILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQDdpTP 80
Cdd:PRK07765   1 MRILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAAG--TP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  81 VLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMA 160
Cdd:PRK07765  79 LLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 740841868 161 MRHRDLPIHGVQYHPESVLTQYGHRMLVNWLRLAG 195
Cdd:PRK07765 159 VRHRELPIHGVQFHPESVLTEGGHRMLANWLTVCG 193
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 3-195 9.69e-105

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 300.12  E-value: 9.69e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKqfDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:PRK05670   2 ILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNP--DAIVLSPGPGTPAEAGISLELIREFAGK---VPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:PRK05670  77 GVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVR 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWLRLAG 195
Cdd:PRK05670 157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 3-191 4.69e-99

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


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 285.58  E-value: 4.69e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDvvKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELEL--LNPDAIVISPGPGHPEDAGISLEIIRALAGK---VPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:cd01743   76 GVCLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALR 155

                        170       180
                 ....*....|....*....|....*....
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:cd01743  156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
3-192 3.60e-80

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 238.17  E-value: 3.60e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFdaILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:PRK07649   2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDF--LMISPGPCSPNEAGISMEVIRYFAGK---IPIF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:PRK07649  77 GVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIR 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWLR 192
Cdd:PRK07649 157 HKTLPIEGVQFHPESIMTSHGKELLQNFIR 186
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
3-191 6.75e-79

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 245.78  E-value: 6.75e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLG-ETVTVWRNDDARLRDVDDvvKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPV 81
Cdd:PRK14607   2 IILIDNYDSFTYNIYQYIGELGpEEIEVVRNDEITIEEIEA--LNPSHIVISPGPGRPEEAGISVEVIRHFSGK---VPI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  82 LGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAM 161
Cdd:PRK14607  77 LGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGI 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 740841868 162 RHRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:PRK14607 157 RHKEHPIFGVQFHPESILTEEGKRILKNFL 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-193 8.81e-72

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: 216.58  E-value: 8.81e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868    3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFdaILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLL--IVISPGPCTPNEAGISLEAIRHFAGK---LPIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGM-LMAM 161
Cdd:TIGR00566  77 GVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIeIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 740841868  162 RHRDLPIHGVQYHPESVLTQYGHRMLVNWLRL 193
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
3-191 1.16e-71

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 216.32  E-value: 1.16e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQfdAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:PRK08007   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQ--KIVISPGPCTPDEAGISLDVIRHYAGR---LPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:PRK08007  77 GVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIR 156

                        170       180
                 ....*....|....*....|....*....
gi 740841868 163 HRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:PRK08007 157 HRQWDLEGVQFHPESILSEQGHQLLANFL 185
trpG CHL00101
anthranilate synthase component 2
 3-193 1.05e-70

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 213.82  E-value: 1.05e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQfdAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVL 82
Cdd:CHL00101   2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIR--HIIISPGPGHPRDSGISLDVISSYAPY---IPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMR 162
Cdd:CHL00101  77 GVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACR 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 740841868 163 HRDLP-IHGVQYHPESVLTQYGHRMLVNWLRL 193
Cdd:CHL00101 157 HKKYKmLRGIQFHPESLLTTHGQQILRNFLSL 188
GATase pfam00117
Glutamine amidotransferase class-I;
4-194 2.73e-67

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 205.16  E-value: 2.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868    4 LVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDvvkQFDAILLSPGPGEPSNAGWTEDIIRAVSRQDdpTPVLG 83
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEE---NPDGIILSGGPGSPGAAGGAIEAIREARELK--IPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   84 VCLGHQAIGEVFGAQVVRA-DELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGM-LMAM 161
Cdd:pfam00117  76 ICLGHQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 740841868  162 RHRDLPIHGVQYHPESVLTQYGHRMLVNWLRLA 194
Cdd:pfam00117 156 RHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
PLN02335 PLN02335
anthranilate synthase
 3-193 3.65e-66

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 203.49  E-value: 3.65e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDdvVKQFDAILLSPGPGEPSNAGWTEDIIRAVSrqddPT-PV 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELK--RKNPRGVLISPGPGTPQDSGISLQTVLELG----PLvPL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  82 LGVCLGHQAIGEVFGAQVVRADE-LLHGKTSPVTHD---GTGVLADVPSPFIATRYHSLTVDPKTLPE-ELIATAFTDSG 156
Cdd:PLN02335  95 FGVCMGLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDG 174

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 740841868 157 MLMAMRHRDLP-IHGVQYHPESVLTQYGHRMLVNWLRL 193
Cdd:PLN02335 175 LIMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKI 212
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
3-192 3.77e-64

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 197.39  E-value: 3.77e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFdaILLSPGPGEPSNAGWTEDIIRAVSrqdDPTPVL 82
Cdd:PRK06774   2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSH--LVISPGPCTPNEAGISLAVIRHFA---DKLPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSG----ML 158
Cdd:PRK06774  77 GVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGgemdEI 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 740841868 159 MAMRHRDLPIHGVQYHPESVLTQYGHRMLVNWLR 192
Cdd:PRK06774 157 MGIRHRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
3-191 1.09e-60

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 188.55  E-value: 1.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFdaILLSPGPGEPSNAGWTEDIIRAVSrqdDPTPVL 82
Cdd:PRK08857   2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTH--LVISPGPCTPNEAGISLQAIEHFA---GKLPIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  83 GVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVDPKTLPE--ELIA-TAFTDSGM-- 157
Cdd:PRK08857  77 GVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPEcfELTAwTELEDGSMde 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 740841868 158 LMAMRHRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:PRK08857 157 IMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-194 6.31e-57

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 178.69  E-value: 6.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   5 VVDNYDSFVFNLVQYIGQLGET--VTVWRNDdARLRDVDDVvkQFDAILLSPGPGEPSNA---GWTEDIIRAVSRQddpT 79
Cdd:NF041322   1 FVDNFDSFTYNLVEYVSEQREHaeTTVLKNT-ASLAEVRAV--DPDAIVISPGPGHPKNDrdvGVTADVLRELSPE---V 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  80 PVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVdpKTLPEELIATAFTDSG--- 156
Cdd:NF041322  75 PTLGVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVA--TEVPDCFEVTATTDHDgee 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 740841868 157 MLMAMRHRDLPIHGVQYHPESVLTQYGHRMLVNWLRLA 194
Cdd:NF041322 153 LVMGIRHREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
PRK13566 PRK13566
anthranilate synthase component I;
1-194 1.31e-54

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 185.51  E-value: 1.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   1 MQILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDAR--LRDVDdvvkqFDAILLSPGPGEPSNAGWTEDIIRAVSRQddp 78
Cdd:PRK13566 527 KRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAEemLDRVN-----PDLVVLSPGPGRPSDFDCKATIDAALARN--- 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  79 TPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVT-HDGTGVLADVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGM 157
Cdd:PRK13566 599 LPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGV 678

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 740841868 158 LMAMRHRDLPIHGVQYHPESVLT---QYGHRMLVNWLRLA 194
Cdd:PRK13566 679 IMAIEHKTLPVAAVQFHPESIMTlggDVGLRIIENVVRLL 718
PRK06895 PRK06895
anthranilate synthase component II;
1-191 2.91e-46

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 151.81  E-value: 2.91e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   1 MQILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLrdvdDVVKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQDDptp 80
Cdd:PRK06895   2 TKLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDL----DEVENFSHILISPGPDVPRAYPQLFAMLERYHQHKS--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  81 VLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLAD-VPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLM 159
Cdd:PRK06895  75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLFDgLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVM 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 740841868 160 AMRHRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:PRK06895 155 AMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 3-190 9.11e-44

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 153.64  E-value: 9.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFDAIL-LSPGPGEPSNAGWTEDIIRavsRQDDPTPV 81
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLmLSPGPGVPSEAGCMPELLT---RLRGKLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  82 LGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTvdPKTLPEELIATAFTDsGMLMAM 161
Cdd:PRK09522  81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINAHFN-GMVMAV 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 740841868 162 RHRDLPIHGVQYHPESVLTQYGHRML---VNW 190
Cdd:PRK09522 158 RHDADRVCGFQFHPESILTTQGARLLeqtLAW 189
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 4-193 2.69e-40

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 146.53  E-value: 2.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   4 LVVDNYDSFVFNLVQYIGQL-GETVTVWRNDDARLRDVDDVV---KQFDAILLSPGPGEPSNAgwtEDI---IRAVSRQD 76
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWTWEEVYHYLyeeKAFDNIVISPGPGSPTCP---ADIgicLRLLLECR 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  77 DpTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVP----SPFIATRYHSLTVDPKTLPEELIATAF 152
Cdd:PLN02889 162 D-IPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAESLPKELVPIAW 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868 153 T-----------------------------------------------------DSGMLMAMRHRDLPIHGVQYHPESVL 179
Cdd:PLN02889 241 TsssdtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermqNGKILMGIMHSTRPHYGLQFHPESIA 320

                        250       260
                 ....*....|....*....|..
gi 740841868 180 TQYGHRMLVN--------WLRL 193
Cdd:PLN02889 321 TCYGRQIFKNfreitqdyWLRL 342
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 1-194 1.65e-33

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: 126.94  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868    1 MQILVVDNYDSFVFNLVQYIGQLGE---TVTVWRNDDARLRDVDDVvKQFDAILLSPGPGEPSNAgwtED--IIRAV--S 73
Cdd:TIGR01823   6 LHVLFIDSYDSFTYNVVRLLEQQTDisvHVTTVHSDTFQDQLLELL-PLFDAIVVGPGPGNPNNA---QDmgIISELweL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   74 RQDDPTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVpSPFIATRYHSLTVDPKTlPEELIATAFT 153
Cdd:TIGR01823  82 ANLDEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLYANPEG-IDTLLPLCLT 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 740841868  154 DSG---MLMAMRHRDLPIHGVQYHPESVLTQYGHRMLV-NWLRLA 194
Cdd:TIGR01823 160 EDEegiILMSAQTKKKPWFGVQYHPESCCSELGSGKLVsNFLKLA 204
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 3-192 2.03e-27

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: 103.16  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868    3 ILVVDN---YDSFVFNLVQYIGQLGETVTvWRNDDARLRDVDDVvkqfdAILLSPGPgepsNAGWTEDIIRAVSRQDD-P 78
Cdd:TIGR00888   1 ILVLDFgsqYTQLIARRLRELGVYSELVP-NTTPLEEIREKNPK-----GIILSGGP----SSVYAENAPRADEKIFElG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   79 TPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVdpKTLPEELIATAFTDSGML 158
Cdd:TIGR00888  71 VPVLGICYGMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKV--KELPEGFKVLATSDNCPV 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 740841868  159 MAMRHRDLPIHGVQYHPESVLTQYGHRMLVNWLR 192
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
PRK00758 PRK00758
GMP synthase subunit A; Validated
 3-197 5.46e-27

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 101.85  E-value: 5.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFV---FNLVQYIGQLGETVTvwrNDdarlRDVDDVVKQFDAILLSPGPgEPSNAGWTEDIIRAVSrqddpT 79
Cdd:PRK00758   2 IVVVDNGGQYNhliHRTLRYLGVDAKIIP---NT----TPVEEIKAFEDGLILSGGP-DIERAGNCPEYLKELD-----V 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  80 PVLGVCLGHQAIGEVFGAQVVRADellHGKTSPVT-----HDGtgVLADVPSPFIATRYHSLTVdpKTLPEELIATAFTD 154
Cdd:PRK00758  69 PILGICLGHQLIAKAFGGEVGRGE---YGEYALVEveildEDD--ILKGLPPEIRVWASHADEV--KELPDGFEILARSD 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 740841868 155 SGMLMAMRHRDLPIHGVQYHPESVLTQYGHRMLVNWLRLAGGE 197
Cdd:PRK00758 142 ICEVEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFLEICGKY 184
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 3-183 7.26e-26

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 99.53  E-value: 7.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSFVFNLVQYIGQLGETVTVWRNDdarlRDVDDVVK-QFDAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPV 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRNT----VPVEEILAaNPDLICLSPGPGHPRDAGNMMALIDRTLGQ---IPL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  82 LGVCLGHQAIGEVFGAQvVRADELLHGKTSPVTHDGTGvladVPSPFIA--------------------TRYHSLTVdpK 141
Cdd:PRK05637  77 LGICLGFQALLEHHGGK-VEPCGPVHGTTDNMILTDAG----VQSPVFAglatdvepdhpeipgrkvpiARYHSLGC--V 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 740841868 142 TLPEELIATAFTDSGM---LMAMRHRDLPIHGVQYHPESVLTQYG 183
Cdd:PRK05637 150 VAPDGMESLGTCSSEIgpvIMAAETTDGKAIGLQFHPESVLSPTG 194
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 39-177 2.07e-24

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


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 94.87  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  39 DVDDVVK-QFDAILLSPGPGEPSNAGWTEDIIRAVSRQDdpTPVLGVCLGHQAIGEVFGAQVVRadelL----HGKTSPV 113
Cdd:cd01744   31 DAEEILKlDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLGHQLLALALGAKTYK----MkfghRGSNHPV 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740841868 114 THDGTGVLadvpspFIATRYHSLTVDPKTLPEELIATAFT-DSGMLMAMRHRDLPIHGVQYHPES 177
Cdd:cd01744  105 KDLITGRV------YITSQNHGYAVDPDSLPGGLEVTHVNlNDGTVEGIRHKDLPVFSVQFHPEA 163
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 80-191 1.94e-22

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: 89.90  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  80 PVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVdpKTLPEELIATAFTDSGMLM 159
Cdd:cd01742   72 PVLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEV--VKLPEGFKVIASSDNCPVA 149

                         90       100       110
                 ....*....|....*....|....*....|..
gi 740841868 160 AMRHRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:cd01742  150 AIANEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 48-177 1.96e-19

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: 84.99  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   48 DAILLSPGPGEPSNAgwtEDIIRAVSRQDDPTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLadvpsp 127
Cdd:TIGR01368 215 DGIFLSNGPGDPAAV---EPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRV------ 285

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 740841868  128 FIATRYHSLTVDPKTLP-EELIATaFTD--SGMLMAMRHRDLPIHGVQYHPES 177
Cdd:TIGR01368 286 EITSQNHGYAVDPDSLPaGDLEVT-HVNlnDGTVEGIRHKDLPVFSVQYHPEA 337
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
48-177 1.77e-18

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 82.43  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  48 DAILLSPGPGEPSNAGWTEDIIRAVsrQDDPTPVLGVCLGHQAIGEVFGAQVVRadelL----HGKTSPVTHDGTG-Vla 122
Cdd:PRK12564 220 DGVFLSNGPGDPAALDYAIEMIREL--LEKKIPIFGICLGHQLLALALGAKTYK----MkfghRGANHPVKDLETGkV-- 291

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 740841868 123 dvpspFIATRYHSLTVDPKTLPEELIAT---AFTDSgmLMAMRHRDLPIHGVQYHPES 177
Cdd:PRK12564 292 -----EITSQNHGFAVDEDSLPANLEVThvnLNDGT--VEGLRHKDLPAFSVQYHPEA 342
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 3-197 1.97e-18

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: 80.38  E-value: 1.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVD---NYDSFVFNLVQYIGQLGETVTVWRNDDARLRDVDDVVKQFDAILLSPGPgepsnAGWTED---------IIR 70
Cdd:COG0518    2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRVYAGEILPYDPDLEDPDGLILSGGP-----MSVYDEdpwledepaLIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  71 AVSRQDdpTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTsPVT-HDGTGVLADVPSPFIATRYHSLTVDpkTLPEELIA 149
Cdd:COG0518   77 EAFELG--KPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTVWMSHGDTVT--ELPEGAEV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 740841868 150 TAFTDSGMLMAMRHRDlPIHGVQYHPESVltqygHRMLVNWLRLAGGE 197
Cdd:COG0518  152 LASSDNCPNQAFRYGR-RVYGVQFHPEVT-----HTMMEAWLEERADE 193
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 34-176 5.19e-18

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 81.09  E-value: 5.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  34 DARLRDVDDVvkQFDAILLSPGPGEPSNAgwtEDIIRAVSRQDDPTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPV 113
Cdd:PRK12838 198 DTSLEEIKNL--NPDGIVLSNGPGDPKEL---QPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPV 272

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740841868 114 THDGTGVLadvpspFIATRYHSLTVDPKTLPEELIATAFTD--SGMLMAMRHRDLPIHGVQYHPE 176
Cdd:PRK12838 273 IDLTTGRV------WMTSQNHGYVVDEDSLDGTPLSVRFFNvnDGSIEGLRHKKKPVLSVQFHPE 331
guaA PRK00074
GMP synthase; Reviewed
 80-192 1.10e-16

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 78.17  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  80 PVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLADVPSPFIATRYHSLTVdpKTLPEELIATAFTDSGMLM 159
Cdd:PRK00074  77 PVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKV--TELPEGFKVIASTENCPIA 154

                         90       100       110
                 ....*....|....*....|....*....|...
gi 740841868 160 AMRHRDLPIHGVQYHPESVLTQYGHRMLVNWLR 192
Cdd:PRK00074 155 AIANEERKFYGVQFHPEVTHTPQGKKLLENFVF 187
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 48-177 4.38e-15

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: 72.75  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  48 DAILLSPGPGEPSNAGWTEDIIRAVsrQDDPTPVLGVCLGHQAIGEVFGAQVVRadelL----HGKTSPVTHDGTG-Vla 122
Cdd:COG0505  219 DGVFLSNGPGDPAALDYAIETIREL--LGKGIPIFGICLGHQLLALALGAKTYK----LkfghRGANHPVKDLETGrV-- 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 740841868 123 dvpspFIATRYHSLTVDPKTLPE-ELIAT---AFTDSgmLMAMRHRDLPIHGVQYHPES 177
Cdd:COG0505  291 -----EITSQNHGFAVDEDSLPAtDLEVThvnLNDGT--VEGLRHKDLPAFSVQYHPEA 342
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 48-177 1.98e-13

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 68.47  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  48 DAILLSPGPGEPSNAGWTEDIIRAVSRQddpTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLAdvpsp 127
Cdd:PLN02771 283 DGVLFSNGPGDPSAVPYAVETVKELLGK---VPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVE----- 354

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 740841868 128 fIATRYHSLTVDPKTLPEELIATAFT-DSGMLMAMRHRDLPIHGVQYHPES 177
Cdd:PLN02771 355 -ISAQNHNYAVDPASLPEGVEVTHVNlNDGSCAGLAFPALNVMSLQYHPEA 404
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-98 1.20e-12

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: 62.23  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSF---VFNLVQYIGQLGETVTVWRNDDARLRDVDDVvKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQ-DDP 78
Cdd:cd01653    1 VAVLLFPGFEeleLASPLDALREAGAEVDVVSPDGGPVESDVDL-DDYDGLILPGGPGTPDDLARDEALLALLREAaAAG 79

                         90       100
                 ....*....|....*....|
gi 740841868  79 TPVLGVCLGHQAIgeVFGAQ 98
Cdd:cd01653   80 KPILGICLGAQLL--VLGVQ 97
PLN02347 PLN02347
GMP synthetase
 49-191 1.88e-12

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 65.86  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  49 AILLSPGP------GEPSNAGWTEDIIravsrQDDPTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTGVLA 122
Cdd:PLN02347  56 VVILSGGPhsvhveGAPTVPEGFFDYC-----RERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFG 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740841868 123 DVPSPFIATRYHSLTVDPKTLPEELIATAFTDSGMLMAMRHRDLPIHGVQYHPESVLTQYGHRMLVNWL 191
Cdd:PLN02347 131 DLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-91 2.55e-11

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: 57.98  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   3 ILVVDNYDSF---VFNLVQYIGQLGETVTVWRNDDARLRDVDDVvKQFDAILLSPGPGEPSNAGWTEDIIRAVSRQ-DDP 78
Cdd:cd03128    1 VAVLLFGGSEeleLASPLDALREAGAEVDVVSPDGGPVESDVDL-DDYDGLILPGGPGTPDDLAWDEALLALLREAaAAG 79

                         90
                 ....*....|...
gi 740841868  79 TPVLGVCLGHQAI 91
Cdd:cd03128   80 KPVLGICLGAQLL 92
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 47-191 5.27e-11

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 59.57  E-value: 5.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  47 FDAILLSPGPGEPSNAG--WTEDIIRAVSRQ-DDPTPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVTHDGTG---- 119
Cdd:cd01741   47 YDGLVILGGPMSVDEDDypWLKKLKELIRQAlAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadp 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740841868 120 VLADVPSPFIATRYHSLTVDpkTLPE--ELIATAFTDSgmLMAMRHRDLpIHGVQYHPEsvltqygHRMLVNWL 191
Cdd:cd01741  127 LFAGLPDEFPVFHWHGDTVV--ELPPgaVLLASSEACP--NQAFRYGDR-ALGLQFHPE-------ERLLRNFL 188
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 1-177 1.72e-09

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 56.73  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   1 MQILVVDNydSFVFNLVQYIGQLGETVTVWRNDDarlrDVDDVVK-QFDAILLSPGPGEPSNagwTEDIIRAVSR-QDDP 78
Cdd:CHL00197 193 LKIIVIDF--GVKYNILRRLKSFGCSITVVPATS----PYQDILSyQPDGILLSNGPGDPSA---IHYGIKTVKKlLKYN 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  79 TPVLGVCLGHQAIGEVFGAQVVRADELLHGKTSPVthdGTGVLADVPSpfiatRYHSLTVDPKTLPEELI-ATAFT-DSG 156
Cdd:CHL00197 264 IPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPS---GLNQQVEITS-----QNHGFAVNLESLAKNKFyITHFNlNDG 335

                        170       180
                 ....*....|....*....|.
gi 740841868 157 MLMAMRHRDLPIHGVQYHPES 177
Cdd:CHL00197 336 TVAGISHSPKPYFSVQYHPEA 356
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 39-176 2.06e-07

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 49.95  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   39 DVDDVVKQFDAILLSPGP--------GEPSNAG---------WTEDIIRAVSRQDdpTPVLGVCLG------------HQ 89
Cdd:pfam07722  51 DAAAILDRLDGLLLTGGPnvdphfygEEPSESGgpydpardaYELALIRAALARG--KPILGICRGfqllnvalggtlYQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   90 AIGEVFGAQVVRADE--LLHGKTSPVTHDGTGVLADVPSP--FIATRYHSLTVDpkTLPEELIATAFTDSGMLMAMRHRD 165
Cdd:pfam07722 129 DIQEQPGFTDHREHCqvAPYAPSHAVNVEPGSLLASLLGSeeFRVNSLHHQAID--RLAPGLRVEAVAPDGTIEAIESPN 206

                         170
                  ....*....|...
gi 740841868  166 LP--IHGVQYHPE 176
Cdd:pfam07722 207 AKgfALGVQWHPE 219
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 39-176 3.94e-07

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: 49.01  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  39 DVDDVVKQFDAILLSPGP--------GEPSNAGWTED---------IIRAVSRQDdpTPVLGVCLGHQAIGEVFG----- 96
Cdd:COG2071   42 DLDELLDRLDGLVLTGGAdvdpalygEEPHPELGPIDperdafelaLIRAALERG--KPVLGICRGMQLLNVALGgtlyq 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  97 -AQVVRADELLHGKTSP---VTHD-----GTgVLADV--PSPFIATRYHSLTVdpKTLPEELIATAFTDSGMLMAMRHRD 165
Cdd:COG2071  120 dLPDQVPGALDHRQPAPryaPRHTveiepGS-RLARIlgEEEIRVNSLHHQAV--KRLGPGLRVSARAPDGVIEAIESPG 196

                        170
                 ....*....|..
gi 740841868 166 LP-IHGVQYHPE 176
Cdd:COG2071  197 APfVLGVQWHPE 208
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 39-176 2.11e-06

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 46.41  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  39 DVDDVVKQFDAILLSPGP--------GEPSNAGWTED---------IIRAVSRQDdpTPVLGVCLGHQAIGEVFGA---Q 98
Cdd:cd01745   46 DLEQYLELLDGLLLTGGGdvdpplygEEPHPELGPIDperdafelaLLRAALERG--KPILGICRGMQLLNVALGGtlyQ 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740841868  99 VVRadellhgktspvthdgtgvladVPSpfiatrYHSLTVdpKTLPEELIATAFTDSGMLMAMRHRDLP-IHGVQYHPE 176
Cdd:cd01745  124 DIR----------------------VNS------LHHQAI--KRLADGLRVEARAPDGVIEAIESPDRPfVLGVQWHPE 172
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 21-176 3.04e-05

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 43.41  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  21 GQLGETVTVWRND-DARLRDVDDvvkqFDAILLSpgpGEPS----NAGW---TEDIIRAVSRQDdpTPVLGVCLGHQAIG 92
Cdd:PRK09065  32 GLAEQPVVVVRVFaGEPLPAPDD----FAGVIIT---GSWAmvtdRLDWserTADWLRQAAAAG--MPLLGICYGHQLLA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  93 EVFGAQVvrADELLhGK---TSPVT-HDGTG---VLADVPSPFIATRYHSLTVdpKTLPEELIATAFTDSGMLMAMRHRD 165
Cdd:PRK09065 103 HALGGEV--GYNPA-GResgTVTVElHPAAAddpLFAGLPAQFPAHLTHLQSV--LRLPPGAVVLARSAQDPHQAFRYGP 177

                        170
                 ....*....|.
gi 740841868 166 lPIHGVQYHPE 176
Cdd:PRK09065 178 -HAWGVQFHPE 187
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-176 1.06e-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: 41.56  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   1 MQILVVD----NYDSfVFNLVQYigqLGETVTVWrnDDArlrdvdDVVKQFDAILLsPGPGEPSNA-------GWTEDII 69
Cdd:COG0118    1 MMIAIIDygmgNLRS-VAKALER---LGAEVVVT--SDP------DEIRAADRLVL-PGVGAFGDAmenlrerGLDEAIR 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  70 RAVSRQddpTPVLGVCLGHQAIGE------------VFGAQVVRadelLHGKTSPVTH---------DGTGVLADVPSpf 128
Cdd:COG0118   68 EAVAGG---KPVLGICLGMQLLFErseengdteglgLIPGEVVR----FPASDLKVPHmgwntveiaKDHPLFAGIPD-- 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 740841868 129 iATRY---HSLTVDPkTLPEELIATA-----FTdsgmlmAMRHRDlPIHGVQYHPE 176
Cdd:COG0118  139 -GEYFyfvHSYYVPP-DDPEDVVATTdygvpFT------AAVERG-NVFGTQFHPE 185
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 66-192 7.15e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 39.38  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  66 EDIIRAVSRQDdpTPVLGVCLGHQAIGEvFGAQVVRADEL--LHGKTSPVTHDGTG----------VLADVPSPFIA--- 130
Cdd:PRK13146  67 EAVIEAVLAAG--RPFLGICVGMQLLFE-RGLEHGDTPGLglIPGEVVRFQPDGPAlkvphmgwntVDQTRDHPLFAgip 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740841868 131 --TRY---HSLTVDPKTlPEELIATA-----FTdsgmlmAMRHRDlPIHGVQYHPE-SvlTQYGHRMLVNWLR 192
Cdd:PRK13146 144 dgARFyfvHSYYAQPAN-PADVVAWTdyggpFT------AAVARD-NLFATQFHPEkS--QDAGLALLRNFLA 206
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 39-176 2.52e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 37.92  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  39 DVDDVVKQFDAILLSPGPGEpsnAGWtEDIIRAVS--RQDDpTPVLGVCLGHQ-AIGE----VFGAQ------------- 98
Cdd:cd01746   48 NAEEALKGADGILVPGGFGI---RGV-EGKILAIKyaRENN-IPFLGICLGMQlAVIEfarnVLGLPdanstefdpdtph 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  99 -VVRADELLHGKTS----------PVT-HDGTGVLADVPSPFIATRY-HSLTVDPKTLPE----ELIATAFTDSGMLM-A 160
Cdd:cd01746  123 pVVDLMPEQKGVKDlggtmrlgayPVIlKPGTLAHKYYGKDEVEERHrHRYEVNPEYVDEleeaGLRFSGTDPDGGLVeI 202

                        170
                 ....*....|....*..
gi 740841868 161 MRHRDLPIH-GVQYHPE 176
Cdd:cd01746  203 VELPDHPFFvGTQFHPE 219
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 41-193 4.44e-03

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: 36.92  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868   41 DDVVKQFDAILLsPGPGEPSNA------GWTEDIIRAVSRQDdpTPVLGVCLGHQAIGE------------VFGAQVVRA 102
Cdd:TIGR01855  31 SKEAELADKLIL-PGVGAFGAAmarlreNGLDLFVELVVRLG--KPVLGICLGMQLLFErseegggvpglgLIKGNVVKL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  103 dellhgKTSPVTHDG---TGVLADVPSP--FIATRY----HSLTVDpktlPEELIATAFTDSG-MLMAMRHRDlPIHGVQ 172
Cdd:TIGR01855 108 ------EARKVPHMGwneVHPVKESPLLngIDEGAYfyfvHSYYAV----CEEEAVLAYADYGeKFPAAVQKG-NIFGTQ 176

                         170       180
                  ....*....|....*....|.
gi 740841868  173 YHPESVlTQYGHRMLVNWLRL 193
Cdd:TIGR01855 177 FHPEKS-GKTGLKLLENFLEL 196
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 13-193 6.31e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 36.36  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  13 VFNLVQYIGQLgetVTVWRNDdarlRDVDDVVKqfdaiLLSPGPG-------EPSNAGWTEDIIRAVSRQDdpTPVLGVC 85
Cdd:PRK13152  15 VAKAFEKIGAI---NFIAKNP----KDLQKADK-----LLLPGVGsfkeamkNLKELGFIEALKEQVLVQK--KPILGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841868  86 LGHQAI---GEVFG---------AQVVRADELLHGKTSPVTHDGTGVLADVP--------SPFIATryHSLTVDPKtlpe 145
Cdd:PRK13152  81 LGMQLFlerGYEGGvceglgfieGEVVKFEEDLNLKIPHMGWNELEILKQSPlyqgipekSDFYFV--HSFYVKCK---- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 740841868 146 ELIATAFTDSGMLMAMRHRDLPIHGVQYHPESVlTQYGHRMLVNWLRL 193
Cdd:PRK13152 155 DEFVSAKAQYGHKFVASLQKDNIFATQFHPEKS-QNLGLKLLENFARL 201
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 81-104 8.59e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 36.10  E-value: 8.59e-03
                         10        20
                 ....*....|....*....|....
gi 740841868  81 VLGVCLGHQAIGEVFGAQVVRADE 104
Cdd:PRK08250  87 VIGVCLGAQLIGEALGAKYEHSPE 110
 
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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