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Conserved domains on  [gi|18395596|ref|NP_564225|]
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Glutamine amidotransferase type 1 family protein [Arabidopsis thaliana]

Protein Classification

anthranilate synthase beta subunit( domain architecture ID 10791323)

anthranilate synthase beta subunit (component II) is part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02335 PLN02335
anthranilate synthase
 1-222 3.38e-169

anthranilate synthase


:

Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 464.27  E-value: 3.38e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    1 MAESNSIPSVVINSSKQNGPIIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGI 80
Cdd:PLN02335   1 MAESNSIPSVVINSSKQNGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   81 SLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSMVHYDEKGEEGLFSGLSNPFIVGRYHSLVIEKDTF 160
Cdd:PLN02335  81 SLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYHSLVIEKDTF 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395596  161 PSDELEVTAWTEDGLVMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFIKIVEKKDSEKLT 222
Cdd:PLN02335 161 PSDELEVTAWTEDGLIMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFIKIIEKKESEKLT 222
 
Name Accession Description Interval E-value
PLN02335 PLN02335
anthranilate synthase
 1-222 3.38e-169

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 464.27  E-value: 3.38e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    1 MAESNSIPSVVINSSKQNGPIIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGI 80
Cdd:PLN02335   1 MAESNSIPSVVINSSKQNGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   81 SLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSMVHYDEKGEEGLFSGLSNPFIVGRYHSLVIEKDTF 160
Cdd:PLN02335  81 SLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYHSLVIEKDTF 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395596  161 PSDELEVTAWTEDGLVMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFIKIVEKKDSEKLT 222
Cdd:PLN02335 161 PSDELEVTAWTEDGLIMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFIKIIEKKESEKLT 222
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 21-215 1.08e-111

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: 317.36  E-value: 1.08e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:COG0512   1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596 101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:COG0512  81 HQAIGEAFGGKVVRAP-EPMHGKTSPITHDGS---GLFAGLPNPFTATRYHSLVVDRETLP-DELEVTAWTEDGEIMGIR 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18395596 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIKIVEK 215
Cdd:COG0512 156 HRELP-IEGVQFHPESILTEHGHQLLANFLELAGE 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 21-210 1.31e-96

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: 279.42  E-value: 1.31e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:cd01743   1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596 101 LQCIGEAFGGKIVRSPFgVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:cd01743  81 HQAIAEAFGGKVVRAPE-PMHGKTSEIHHDGS---GLFKGLPQPFTVGRYHSLVVDPDPLP-DLLEVTASTEDGVIMALR 155

                       170       180       190
                ....*....|....*....|....*....|
gi 18395596 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:cd01743 156 HRDLP-IYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
22-213 5.36e-66

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 201.70  E-value: 5.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    22 IVIDNYDSFTYNLCQYMGELQCHFEVYRNDElTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPL-VPLFGVCMG 100
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELkIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   101 LQCIGEAFGGKIVRSPFGVMHGKSSMVHYDekgEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDG-LVMAA 179
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFGHHGKNSPVGDD---GCGLFYGLPNVFIVRRYHSYAVDPDTLP-DGLEVTATSENDgTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 18395596   180 RHRKYKhIQGVQFHPESIITTEGKTIVRNFIKIV 213
Cdd:pfam00117 156 RHKKLP-IFGVQFHPESILTPHGPEILFNFFIKA 188
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 21-211 1.03e-65

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: 201.17  E-value: 1.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDG-LVMAA 179
Cdd:TIGR00566  82 HQAMGQAFGGDVVRAN-TVMHGKTSEIEHNGA---GIFRGLFNPLTATRYHSLVVEPETLP-TCFPVTAWEEENiEIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 18395596   180 RHRKyKHIQGVQFHPESIITTEGKTIVRNFIK 211
Cdd:TIGR00566 157 RHRD-LPLEGVQFHPESILSEQGHQLLANFLH 187
Anth_synII_Halo NF041322
anthranilate synthase component II;
23-210 6.79e-59

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 183.69  E-value: 6.79e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   23 VIDNYDSFTYNLCQYMGELQCHFE--VYRNDElTVEELKRKNPRGVLISPGPGTPQ---DSGISLQTVLELGPLVPLFGV 97
Cdd:NF041322   1 FVDNFDSFTYNLVEYVSEQREHAEttVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   98 CMGLQCIGEAFGGKIVRSPFGVmHGKSSMVHYDEkgeEGLFSGLSNPFIVGRYHSLVIekdTFPSDELEVTAWTEDG--- 174
Cdd:NF041322  80 CLGLEAAVYAYGGTVGRAPEPV-HGKAFPVDHDG---EGVFAGLEQGFQAGRYHSLVA---TEVPDCFEVTATTDHDgee 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 18395596  175 LVMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:NF041322 153 LVMGIRHREHP-IECVQFHPESVLTGVGHDVIENFL 187
 
Name Accession Description Interval E-value
PLN02335 PLN02335
anthranilate synthase
 1-222 3.38e-169

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 464.27  E-value: 3.38e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    1 MAESNSIPSVVINSSKQNGPIIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGI 80
Cdd:PLN02335   1 MAESNSIPSVVINSSKQNGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   81 SLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSMVHYDEKGEEGLFSGLSNPFIVGRYHSLVIEKDTF 160
Cdd:PLN02335  81 SLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYHSLVIEKDTF 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395596  161 PSDELEVTAWTEDGLVMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFIKIVEKKDSEKLT 222
Cdd:PLN02335 161 PSDELEVTAWTEDGLIMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFIKIIEKKESEKLT 222
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 21-215 1.08e-111

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: 317.36  E-value: 1.08e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:COG0512   1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596 101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:COG0512  81 HQAIGEAFGGKVVRAP-EPMHGKTSPITHDGS---GLFAGLPNPFTATRYHSLVVDRETLP-DELEVTAWTEDGEIMGIR 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18395596 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIKIVEK 215
Cdd:COG0512 156 HRELP-IEGVQFHPESILTEHGHQLLANFLELAGE 189
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 21-213 9.32e-105

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 300.12  E-value: 9.32e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:PRK05670   2 ILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIVRSPFgVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:PRK05670  82 HQAIGEAFGGKVVRAKE-IMHGKTSPIEHDGS---GIFAGLPNPFTVTRYHSLVVDRESLP-DCLEVTAWTDDGEIMGVR 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 18395596  181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIKIV 213
Cdd:PRK05670 157 HKELP-IYGVQFHPESILTEHGHKLLENFLELA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 21-210 1.31e-96

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: 279.42  E-value: 1.31e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:cd01743   1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596 101 LQCIGEAFGGKIVRSPFgVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:cd01743  81 HQAIAEAFGGKVVRAPE-PMHGKTSEIHHDGS---GLFKGLPQPFTVGRYHSLVVDPDPLP-DLLEVTASTEDGVIMALR 155

                       170       180       190
                ....*....|....*....|....*....|
gi 18395596 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:cd01743 156 HRDLP-IYGVQFHPESILTEYGLRLLENFL 184
trpG CHL00101
anthranilate synthase component 2
 21-210 3.22e-85

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 250.80  E-value: 3.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:CHL00101   2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDekgEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:CHL00101  82 HQSIGYLFGGKIIKAP-KPMHGKTSKIYHN---HDDLFQGLPNPFTATRYHSLIIDPLNLP-SPLEITAWTEDGLIMACR 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 18395596  181 HRKYKHIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:CHL00101 157 HKKYKMLRGIQFHPESLLTTHGQQILRNFL 186
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
21-212 2.81e-84

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 259.65  E-value: 2.81e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGEL-QCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCM 99
Cdd:PRK14607   2 IILIDNYDSFTYNIYQYIGELgPEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  100 GLQCIGEAFGGKIVRSPFgVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPSDeLEVTAWTEDGLVMAA 179
Cdd:PRK14607  82 GHQAIGYAFGGKIVHAKR-ILHGKTSPIDHNGK---GLFRGIPNPTVATRYHSLVVEEASLPEC-LEVTAKSDDGEIMGI 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 18395596  180 RHRKYkHIQGVQFHPESIITTEGKTIVRNFIKI 212
Cdd:PRK14607 157 RHKEH-PIFGVQFHPESILTEEGKRILKNFLNY 188
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
21-210 1.14e-75

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 227.24  E-value: 1.14e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPR--GVLISPGPGTPQDSGISLQTVLEL-GPLVPLFGV 97
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQfdGVLLSPGPGTPERAGASIDMVRACaAAGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   98 CMGLQCIGEAFGGKIVRSPfGVMHGKSSMVHYDekgEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVM 177
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAP-ELLHGKTSSVHHT---GVGVLAGLPDPFTATRYHSLTILPETLP-AELEVTARTDSGVIM 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 18395596  178 AARHRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:PRK07765 158 AVRHRELP-IHGVQFHPESVLTEGGHRMLANWL 189
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
21-216 1.93e-75

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 226.22  E-value: 1.93e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:PRK07649   2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:PRK07649  82 HQSIAQVFGGEVVRAE-RLMHGKTSLMHHDGK---TIFSDIPNPFTATRYHSLIVKKETLP-DCLEVTSWTEEGEIMAIR 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 18395596  181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIKIVEKK 216
Cdd:PRK07649 157 HKTLP-IEGVQFHPESIMTSHGKELLQNFIRKYSPS 191
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
21-211 1.30e-68

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 208.62  E-value: 1.30e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:PRK08007   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDekgEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:PRK08007  82 HQAMAQAFGGKVVRAA-KVMHGKTSPITHN---GEGVFRGLANPLTVTRYHSLVVEPDSLP-ACFEVTAWSETREIMGIR 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 18395596  181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIK 211
Cdd:PRK08007 157 HRQWD-LEGVQFHPESILSEQGHQLLANFLH 186
GATase pfam00117
Glutamine amidotransferase class-I;
22-213 5.36e-66

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 201.70  E-value: 5.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    22 IVIDNYDSFTYNLCQYMGELQCHFEVYRNDElTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPL-VPLFGVCMG 100
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELkIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   101 LQCIGEAFGGKIVRSPFGVMHGKSSMVHYDekgEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDG-LVMAA 179
Cdd:pfam00117  80 HQLLALAFGGKVVKAKKFGHHGKNSPVGDD---GCGLFYGLPNVFIVRRYHSYAVDPDTLP-DGLEVTATSENDgTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 18395596   180 RHRKYKhIQGVQFHPESIITTEGKTIVRNFIKIV 213
Cdd:pfam00117 156 RHKKLP-IFGVQFHPESILTPHGPEILFNFFIKA 188
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
21-212 7.74e-66

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 201.63  E-value: 7.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:PRK06774   2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDekgEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTE-DGLV--- 176
Cdd:PRK06774  82 HQALGQAFGARVVRAR-QVMHGKTSAICHS---GQGVFRGLNQPLTVTRYHSLVIAADSLP-GCFELTAWSErGGEMdei 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 18395596  177 MAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKI 212
Cdd:PRK06774 157 MGIRHRTLP-LEGVQFHPESILSEQGHQLLDNFLKN 191
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 21-211 1.03e-65

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: 201.17  E-value: 1.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDG-LVMAA 179
Cdd:TIGR00566  82 HQAMGQAFGGDVVRAN-TVMHGKTSEIEHNGA---GIFRGLFNPLTATRYHSLVVEPETLP-TCFPVTAWEEENiEIMAI 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 18395596   180 RHRKyKHIQGVQFHPESIITTEGKTIVRNFIK 211
Cdd:TIGR00566 157 RHRD-LPLEGVQFHPESILSEQGHQLLANFLH 187
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
21-210 8.27e-62

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 191.24  E-value: 8.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:PRK08857   2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHYDEKgeeGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTE--DGL--- 175
Cdd:PRK08857  82 HQAIAQVFGGQVVRAR-QVMHGKTSPIRHTGR---SVFKGLNNPLTVTRYHSLVVKNDTLP-ECFELTAWTEleDGSmde 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 18395596  176 VMAARHrKYKHIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:PRK08857 157 IMGFQH-KTLPIEAVQFHPESIKTEQGHQLLANFL 190
Anth_synII_Halo NF041322
anthranilate synthase component II;
23-210 6.79e-59

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 183.69  E-value: 6.79e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   23 VIDNYDSFTYNLCQYMGELQCHFE--VYRNDElTVEELKRKNPRGVLISPGPGTPQ---DSGISLQTVLELGPLVPLFGV 97
Cdd:NF041322   1 FVDNFDSFTYNLVEYVSEQREHAEttVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   98 CMGLQCIGEAFGGKIVRSPFGVmHGKSSMVHYDEkgeEGLFSGLSNPFIVGRYHSLVIekdTFPSDELEVTAWTEDG--- 174
Cdd:NF041322  80 CLGLEAAVYAYGGTVGRAPEPV-HGKAFPVDHDG---EGVFAGLEQGFQAGRYHSLVA---TEVPDCFEVTATTDHDgee 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 18395596  175 LVMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:NF041322 153 LVMGIRHREHP-IECVQFHPESVLTGVGHDVIENFL 187
PRK13566 PRK13566
anthranilate synthase component I;
21-208 6.70e-50

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 172.41  E-value: 6.70e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDeLTVEELKRKNPRGVLISPGPGTPQDSGIS--LQTVLELGplVPLFGVC 98
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPSDFDCKatIDAALARN--LPIFGVC 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   99 MGLQCIGEAFGGKI--VRSPfgvMHGKSSMVHYdeKGEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLV 176
Cdd:PRK13566 606 LGLQAIVEAFGGELgqLAYP---MHGKPSRIRV--RGPGRLFSGLPEEFTVGRYHSLFADPETLP-DELLVTAETEDGVI 679

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 18395596  177 MAARHRKYKhIQGVQFHPESIITTEGK---TIVRN 208
Cdd:PRK13566 680 MAIEHKTLP-VAAVQFHPESIMTLGGDvglRIIEN 713
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 21-202 1.22e-38

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 139.78  E-value: 1.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRND---ELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGV 97
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   98 CMGLQCIGEAFGGKIVRSPfGVMHGKSSMVHYDekgEEGLFSGLSNPFIVGRYHSLVieKDTFPsDELEVTAwTEDGLVM 177
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAG-EILHGKASSIEHD---GQAMFAGLTNPLPVARYHSLV--GSNIP-AGLTINA-HFNGMVM 155

                        170       180
                 ....*....|....*....|....*
gi 18395596  178 AARHRKyKHIQGVQFHPESIITTEG 202
Cdd:PRK09522 156 AVRHDA-DRVCGFQFHPESILTTQG 179
PRK06895 PRK06895
anthranilate synthase component II;
21-212 2.77e-32

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 115.60  E-value: 2.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDELTVEELKrkNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:PRK06895   4 LLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVE--NFSHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIVRSPfGVMHGKSSMVHydEKGEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDELEVTAWTEDGLVMAAR 180
Cdd:PRK06895  82 HQTLCEFFGGELYNLN-NVRHGQQRPLK--VRSNSPLFDGLPEEFNIGLYHSWAVSEENFP-TPLEITAVCDENVVMAMQ 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 18395596  181 HrKYKHIQGVQFHPESIITTEGKTIVRNFIKI 212
Cdd:PRK06895 158 H-KTLPIYGVQFHPESYISEFGEQILRNWLAI 188
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 21-211 5.40e-30

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 110.32  E-value: 5.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNdELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  101 LQCIGEAFGGKIvrSPFGVMHGKSS-MVHYDEKGEEGLFSGLS------NPFI------VGRYHSLVIekdTFPSDELEV 167
Cdd:PRK05637  83 FQALLEHHGGKV--EPCGPVHGTTDnMILTDAGVQSPVFAGLAtdvepdHPEIpgrkvpIARYHSLGC---VVAPDGMES 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 18395596  168 TAWTEDGL---VMAARHRKYKHIqGVQFHPESIITTEGKTIVRNFIK 211
Cdd:PRK05637 158 LGTCSSEIgpvIMAAETTDGKAI-GLQFHPESVLSPTGPIILSRCVE 203
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 22-214 1.25e-29

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 115.72  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   22 IVIDNYDSFTYNLCQYMGELQ-CHFEVYRNDELTVEEL-----KRKNPRGVLISPGPGTP---QDSGISLQTVLELGPlV 92
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIVNgVPPVVVRNDEWTWEEVyhylyEEKAFDNIVISPGPGSPtcpADIGICLRLLLECRD-I 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   93 PLFGVCMGLQCIGEAFGGKIVRSPFGVmHGKSSMVHYDEKGeegLF----SGLSNPFIVGRYHSLVIEKDTFPSdELEVT 168
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPV-HGRLSEIEHNGCR---LFddipSGRNSGFKVVRYHSLVIDAESLPK-ELVPI 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  169 AWT--------------------------------------EDG---------------LVMAARHRKYKHIqGVQFHPE 195
Cdd:PLN02889 239 AWTsssdtlsflesqksglvpdayesqigqsgssdpfssklKNGtswpsshsermqngkILMGIMHSTRPHY-GLQFHPE 317

                        250
                 ....*....|....*....
gi 18395596  196 SIITTEGKTIVRNFIKIVE 214
Cdd:PLN02889 318 SIATCYGRQIFKNFREITQ 336
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 21-213 9.58e-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: 101.24  E-value: 9.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDElTVEELKRKNPRGVLISPGPG--TPQDSGISLQTVLELGplVPLFGVC 98
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSsvYAENAPRADEKIFELG--VPVLGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    99 MGLQCIGEAFGGKIVRSPFGvMHGKSSmVHYDEKGEegLFSGLSNPFIVGRYHSlviEKDTFPSDELEVTAWTEDGLVMA 178
Cdd:TIGR00888  78 YGMQLMAKQLGGEVGRAEKR-EYGKAE-LEILDEDD--LFRGLPDESTVWMSHG---DKVKELPEGFKVLATSDNCPVAA 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 18395596   179 ARHRKyKHIQGVQFHPESIITTEGKTIVRNFIKIV 213
Cdd:TIGR00888 151 MAHEE-KPIYGVQFHPEVTHTEYGNELLENFVYDV 184
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 21-212 2.41e-24

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: 100.37  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    21 IIVIDNYDSFTYNLCQYM---GELQCHFEVYRNDELT---VEELKRKNprGVLISPGPGTP---QDSGIsLQTVLELGPL 91
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQdqlLELLPLFD--AIVVGPGPGNPnnaQDMGI-ISELWELANL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    92 --VPLFGVCMGLQCIGEAFGGKIVRSPFgVMHGKSSMVHYDEKGeegLFSGLSNpFIVGRYHSLVIEKDtfPSDELEVTA 169
Cdd:TIGR01823  85 deVPVLGICLGFQSLCLAQGADISRLPT-PKHGQVYEMHTNDAA---IFCGLFS-VKSTRYHSLYANPE--GIDTLLPLC 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 18395596   170 WTEDG---LVMAARHRKYKHIqGVQFHPESIITTEGK-TIVRNFIKI 212
Cdd:TIGR01823 158 LTEDEegiILMSAQTKKKPWF-GVQYHPESCCSELGSgKLVSNFLKL 203
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 21-210 9.75e-24

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: 93.37  E-value: 9.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  21 IIVIDNYDSFTYNLCQYMGELQCHFEVYRNDElTVEELKRKNPRGVLISPGPGTPQDSGISL--QTVLELGplVPLFGVC 98
Cdd:cd01742   1 ILILDFGSQYTHLIARRVRELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRvdPEIFELG--VPVLGIC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  99 MGLQCIGEAFGGKIVRSP---FGVMhgKSSMVHYDEkgeegLFSGLSNPFIVGRYHSLVIEKdtfPSDELEVTAWTEDGL 175
Cdd:cd01742  78 YGMQLIAKALGGKVERGDkreYGKA--EIEIDDSSP-----LFEGLPDEQTVWMSHGDEVVK---LPEGFKVIASSDNCP 147

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18395596 176 VMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:cd01742 148 VAAIANEEKK-IYGVQFHPEVTHTEKGKEILKNFL 181
guaA PRK00074
GMP synthase; Reviewed
 40-210 1.25e-20

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 89.34  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   40 ELQCHFEVYRNDElTVEELKRKNPRGVLISPGP------GTPQ-DSGIslqtvLELGplVPLFGVCMGLQCIGEAFGGKI 112
Cdd:PRK00074  25 ELGVYSEIVPYDI-SAEEIRAFNPKGIILSGGPasvyeeGAPRaDPEI-----FELG--VPVLGICYGMQLMAHQLGGKV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  113 VRSP---FGvmhgkSSMVHYDEKGEegLFSGLSNPFIVGRYHSLVIEKdtfPSDELEVTAWTEDGLVMAARHRKyKHIQG 189
Cdd:PRK00074  97 ERAGkreYG-----RAELEVDNDSP--LFKGLPEEQDVWMSHGDKVTE---LPEGFKVIASTENCPIAAIANEE-RKFYG 165

                        170       180
                 ....*....|....*....|.
gi 18395596  190 VQFHPESIITTEGKTIVRNFI 210
Cdd:PRK00074 166 VQFHPEVTHTPQGKKLLENFV 186
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 20-195 1.09e-19

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


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 83.84  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  20 PIIVID---NYDSFTYNLCQYMGELQCHFEVYR--NDELTVEELKRKNPRGVLISPGPGTPQDSGISL-------QTVLE 87
Cdd:COG0518   1 KILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLedepaliREAFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  88 LGplVPLFGVCMGLQCIGEAFGGKIVRSP---FGVMHgkssmVHYDEKGEegLFSGLSNPFIVGRYHSlviekDTFpsDE 164
Cdd:COG0518  81 LG--KPVLGICYGAQLLAHALGGKVEPGPgreIGWAP-----VELTEADP--LFAGLPDEFTVWMSHG-----DTV--TE 144

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18395596 165 L----EVTAWTEDGLVMAARHRkyKHIQGVQFHPE 195
Cdd:COG0518 145 LpegaEVLASSDNCPNQAFRYG--RRVYGVQFHPE 177
PRK00758 PRK00758
GMP synthase subunit A; Validated
 20-215 1.13e-19

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 82.59  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   20 PIIVIDNYDSFTYNLCQYMGELQCHFEVYRNDeLTVEELKrKNPRGVLISPGPgTPQDSGISLQTVLELGplVPLFGVCM 99
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIK-AFEDGLILSGGP-DIERAGNCPEYLKELD--VPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  100 GLQCIGEAFGGKIVRSPfgvmHGKSSMVHYDEKGEEGLFSGLSNPFIVGRYHslvieKD--TFPSDELEVTAWTEDGLVM 177
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGE----YGEYALVEVEILDEDDILKGLPPEIRVWASH-----ADevKELPDGFEILARSDICEVE 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 18395596  178 AARHrKYKHIQGVQFHPESIITTEGKTIVRNFIKIVEK 215
Cdd:PRK00758 147 AMKH-KEKPIYGVQFHPEVAHTEYGEEIFKNFLEICGK 183
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 54-196 1.95e-18

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: 79.08  E-value: 1.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  54 TVEELKRKNPRGVLISPGPGTPQDSGISLQTVLE-LGPLVPLFGVCMGLQCIGEAFGGKIVRSPFG-------VMHGKSS 125
Cdd:cd01744  31 DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKlLGKKIPIFGICLGHQLLALALGAKTYKMKFGhrgsnhpVKDLITG 110

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395596 126 MVhydekgeeglfsglsnpFIVGRYHSLVIEKDTFPSDeLEVTAWT-EDGLVMAARHRKYKhIQGVQFHPES 196
Cdd:cd01744 111 RV-----------------YITSQNHGYAVDPDSLPGG-LEVTHVNlNDGTVEGIRHKDLP-VFSVQFHPEA 163
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 56-196 8.71e-17

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: 77.67  E-value: 8.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    56 EELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSMVHYDEKGee 135
Cdd:TIGR01368 207 EEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFG-HRGGNHPVKDLITG-- 283

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395596   136 glfsglsNPFIVGRYHSLVIEKDTFPSDELEVTAWT-EDGLVMAARHrKYKHIQGVQFHPES 196
Cdd:TIGR01368 284 -------RVEITSQNHGYAVDPDSLPAGDLEVTHVNlNDGTVEGIRH-KDLPVFSVQYHPEA 337
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 54-195 1.93e-16

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 76.85  E-value: 1.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   54 TVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSMVhYDekg 133
Cdd:PRK12838 200 SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFG-HRGANHPV-ID--- 274

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395596  134 eegLFSGlsNPFIVGRYHSLVIEKDTFPSDELEVTAWT-EDGLVMAARHRKYKhIQGVQFHPE 195
Cdd:PRK12838 275 ---LTTG--RVWMTSQNHGYVVDEDSLDGTPLSVRFFNvNDGSIEGLRHKKKP-VLSVQFHPE 331
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 13-196 1.40e-14

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 71.55  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   13 NSSKQNGPIIVIDNYD-SFTYNLCQYMGELQCHFEVYRNDELTVEELKRKnPRGVLISPGPGTPQDSGISLQTVLELGPL 91
Cdd:PLN02771 232 NTNSRDGESYHVIAYDfGIKHNILRRLASYGCKITVVPSTWPASEALKMK-PDGVLFSNGPGDPSAVPYAVETVKELLGK 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   92 VPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSMVHYDEKGEEGlfsglsnpfIVGRYHSLVIEKDTFPSDeLEVTAWT 171
Cdd:PLN02771 311 VPVFGICMGHQLLGQALGGKTFKMKFG-HHGGNHPVRNNRTGRVE---------ISAQNHNYAVDPASLPEG-VEVTHVN 379

                        170       180
                 ....*....|....*....|....*
gi 18395596  172 EDGLVMAARHRKYKHIQGVQFHPES 196
Cdd:PLN02771 380 LNDGSCAGLAFPALNVMSLQYHPEA 404
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 54-196 2.06e-14

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: 70.82  E-value: 2.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  54 TVEELKRKNPRGVLISPGPGTPQDSGISLQTVLEL-GPLVPLFGVCMGLQCIGEAFGGKIVRSPFG-------VMH---G 122
Cdd:COG0505 209 SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELlGKGIPIFGICLGHQLLALALGAKTYKLKFGhrganhpVKDletG 288

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18395596 123 K---SSMvhydekgeeglfsglsNpfivgryHSLVIEKDTFPSDELEVTaw-teDGLVMAARHRKYKhIQGVQFHPES 196
Cdd:COG0505 289 RveiTSQ----------------N-------HGFAVDEDSLPATDLEVThvnlnDGTVEGLRHKDLP-AFSVQYHPEA 342
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 82-210 5.04e-14

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: 67.66  E-value: 5.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  82 LQTVLELGplVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSMVHYDEKGEEGLFSGLSNPFIVGRYHslvieKDTFp 161
Cdd:cd01741  74 IRQALAAG--KPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWH-----GDTV- 145

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18395596 162 sDEL----EVTAWTEDGLVMAARHRkyKHIQGVQFHPEsiittegKTIVRNFI 210
Cdd:cd01741 146 -VELppgaVLLASSEACPNQAFRYG--DRALGLQFHPE-------ERLLRNFL 188
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
54-196 5.62e-14

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 69.72  E-value: 5.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   54 TVEELKRKNPRGVLISPGPGTPQ--DSGISL-QTVLELGplVPLFGVCMGLQCIGEAFGGKIVRSPFG-------VMHGK 123
Cdd:PRK12564 210 TAEEILALNPDGVFLSNGPGDPAalDYAIEMiRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGhrganhpVKDLE 287

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395596  124 SSMVhydekgeeglfsglsnpFIVGRYHSLVIEKDTFPsDELEVTAW-TEDGLVMAARHRKYKhIQGVQFHPES 196
Cdd:PRK12564 288 TGKV-----------------EITSQNHGFAVDEDSLP-ANLEVTHVnLNDGTVEGLRHKDLP-AFSVQYHPEA 342
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 21-196 1.96e-11

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 62.51  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   21 IIVIDNydSFTYNLCQYMGELQCHFEVYrNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLE-LGPLVPLFGVCM 99
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKlLKYNIPIFGICM 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  100 GLQCIGEAFGGKIVRSPFGvMHGKSSMVHYDEKGEeglfsglsnpfIVGRYHSLVIEKDTFPSDELEVTAWT-EDGLVMA 178
Cdd:CHL00197 272 GHQILSLALEAKTFKLKFG-HRGLNHPSGLNQQVE-----------ITSQNHGFAVNLESLAKNKFYITHFNlNDGTVAG 339

                        170
                 ....*....|....*...
gi 18395596  179 ARHRKYKHIQgVQFHPES 196
Cdd:CHL00197 340 ISHSPKPYFS-VQYHPEA 356
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 92-195 2.14e-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: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 60.67  E-value: 2.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  92 VPLFGVCMGLQCIGEAFGGKIVRspfgvmhgkssmvhyDEKgeeglfsglsnpfiVGRYHSLVIEKdtfPSDELEVTAWT 171
Cdd:cd01745 101 KPILGICRGMQLLNVALGGTLYQ---------------DIR--------------VNSLHHQAIKR---LADGLRVEARA 148

                        90       100
                ....*....|....*....|....
gi 18395596 172 EDGLVMAARHRKYKHIQGVQFHPE 195
Cdd:cd01745 149 PDGVIEAIESPDRPFVLGVQWHPE 172
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 92-195 1.16e-10

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: 58.81  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    92 VPLFGVCMGLQCIGEAFGG----KIVRSPFGVMHGKSSMVHYD--------EKGeeGLFSGL--SNPFIVGRYHSLVIEK 157
Cdd:pfam07722 106 KPILGICRGFQLLNVALGGtlyqDIQEQPGFTDHREHCQVAPYapshavnvEPG--SLLASLlgSEEFRVNSLHHQAIDR 183

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 18395596   158 dtfPSDELEVTAWTEDGLVMAARHRKYKH-IQGVQFHPE 195
Cdd:pfam07722 184 ---LAPGLRVEAVAPDGTIEAIESPNAKGfALGVQWHPE 219
PLN02347 PLN02347
GMP synthetase
 13-210 3.83e-10

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 58.93  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   13 NSSKQNGPIIVIDNYDS-FTYNLCQYMGELQCHFEVYRNDeLTVEELKRKNPRGVLISPGP------GTPQDSGISLQTV 85
Cdd:PLN02347   4 EAAKSYLDVVLILDYGSqYTHLITRRVRELGVYSLLLSGT-ASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   86 LELGplVPLFGVCMGLQCIGEAFGGKiVRSPFGVMHGKSSMvhyDEKGEEGLFSGLSNPFIVGRYHSLVIEKDTFPsDEL 165
Cdd:PLN02347  83 RERG--VPVLGICYGMQLIVQKLGGE-VKPGEKQEYGRMEI---RVVCGSQLFGDLPSGETQTVWMSHGDEAVKLP-EGF 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18395596  166 EVTAWTEDGLVMAARHRKyKHIQGVQFHPESIITTEGKTIVRNFI 210
Cdd:PLN02347 156 EVVAKSVQGAVVAIENRE-RRIYGLQYHPEVTHSPKGMETLRHFL 199
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 82-195 7.51e-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: 56.72  E-value: 7.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  82 LQTVLELGplVPLFGVCMGLQCIGEAFGGKIV-----RSPFGVMHGKSSMVHYDEKG----EEGLFSGL--SNPFIVGRY 150
Cdd:COG2071  89 IRAALERG--KPVLGICRGMQLLNVALGGTLYqdlpdQVPGALDHRQPAPRYAPRHTveiePGSRLARIlgEEEIRVNSL 166

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18395596 151 HSLVIEKdtfPSDELEVTAWTEDGLVMAARHRKYKHIQGVQFHPE 195
Cdd:COG2071 167 HHQAVKR---LGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPE 208
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 21-104 2.12e-07

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 47.58  E-value: 2.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  21 IIVIDNYDSFT---YNLCQYMGELQCHFEVYRNDELTVE-ELKRKNPRGVLISPGPGTPQDSGIS------LQTVLELGp 90
Cdd:cd03128   1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLAWDeallalLREAAAAG- 79

                        90
                ....*....|....
gi 18395596  91 lVPLFGVCMGLQCI 104
Cdd:cd03128  80 -KPVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 21-104 4.12e-07

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 47.21  E-value: 4.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596  21 IIVIDNYDSFT---YNLCQYMGELQCHFEVYRNDELTVE-ELKRKNPRGVLISPGPGTPQDSGIS------LQTVLELGp 90
Cdd:cd01653   1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLARDeallalLREAAAAG- 79

                        90
                ....*....|....
gi 18395596  91 lVPLFGVCMGLQCI 104
Cdd:cd01653  80 -KPILGICLGAQLL 92
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 66-210 1.96e-06

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


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 46.55  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596    66 VLISPGPGTPQD-------SGISLQTVLELGPLVPLFGVCMGLQCIGEA------------FGGKIVR-SPFGVMHGKSS 125
Cdd:TIGR01855  39 KLILPGVGAFGAamarlreNGLDLFVELVVRLGKPVLGICLGMQLLFERseegggvpglglIKGNVVKlEARKVPHMGWN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   126 MVHydEKGEEGLFSGLSNPFIVGRYHSLVIEkdtfPSDElEVTAWTEDGLVMAARHRKyKHIQGVQFHPESIITTeGKTI 205
Cdd:TIGR01855 119 EVH--PVKESPLLNGIDEGAYFYFVHSYYAV----CEEE-AVLAYADYGEKFPAAVQK-GNIFGTQFHPEKSGKT-GLKL 189


                  ....*
gi 18395596   206 VRNFI 210
Cdd:TIGR01855 190 LENFL 194
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 92-195 2.57e-05

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 43.80  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   92 VPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSMVHYDEKGEEGLFSGLSNpfivgryhslviekdTFP---SDELEVT 168
Cdd:PRK09065  89 MPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPA---------------QFPahlTHLQSVL 153

                         90       100       110
                 ....*....|....*....|....*....|....
gi 18395596  169 AWTEDGLVMAA----RH---RKYKHIQGVQFHPE 195
Cdd:PRK09065 154 RLPPGAVVLARsaqdPHqafRYGPHAWGVQFHPE 187
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 92-195 2.46e-04

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 41.04  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   92 VPLFGVCMGLQCIGEAFGGKIVRSPFGV-------------MHGKSSMVHYDEKGEEGLFSGL---SNPFIVGRYHSlvi 155
Cdd:PRK11366 108 IPIFAICRGLQELVVATGGSLHRKLCEQpellehredpelpVEQQYAPSHEVQVEEGGLLSALlpeCSNFWVNSLHG--- 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18395596  156 EKDTFPSDELEVTAWTEDGLVMAARHRKYKHIQGVQFHPE 195
Cdd:PRK11366 185 QGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPE 224
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 93-216 1.06e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 38.57  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   93 PLFGVCMGLQCI---GEAFG---------GKIVRSPFG----VMH-GKSSMVHydeKGEEGLFSGLSNpfivGRY----H 151
Cdd:PRK13141  74 PLLGICLGMQLLfesSEEFGeteglgllpGRVRRFPPEeglkVPHmGWNQLEL---KKESPLLKGIPD----GAYvyfvH 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18395596  152 SLVIEkdtfPSDELEVTAWTEDGLVMAARHRKyKHIQGVQFHPE-SiitteGKT---IVRNFIKIVEKK 216
Cdd:PRK13141 147 SYYAD----PCDEEYVAATTDYGVEFPAAVGK-DNVFGAQFHPEkS-----GDVglkILKNFVEMVEEC 205
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 92-213 1.33e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 38.31  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   92 VPLFGVCMGLQCIGEA------------FGGKIVRSPFG--VMHGKSSMVHYDEKGEegLFSGLSNPFIvgrY--HSLVI 155
Cdd:PRK13143  72 KPFLGICLGMQLLFESseegggvrglglFPGRVVRFPAGvkVPHMGWNTVKVVKDCP--LFEGIDGEYV---YfvHSYYA 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18395596  156 EkdtfPSDELEVTAWTEDGLVMAARHRKyKHIQGVQFHPESIITTeGKTIVRNFIKIV 213
Cdd:PRK13143 147 Y----PDDEDYVVATTDYGIEFPAAVCN-DNVFGTQFHPEKSGET-GLKILENFVELI 198
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 96-151 3.32e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 37.64  E-value: 3.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18395596   96 GVCMGLQCIGEAFGGKIVRSPFGVMhGKSSMVHYDEKGEEGLFSGLSNPFIVGRYH 151
Cdd:PRK08250  89 GVCLGAQLIGEALGAKYEHSPEKEI-GYFPITLTEAGLKDPLLSHFGSTLTVGHWH 143
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 92-212 8.40e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 36.00  E-value: 8.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395596   92 VPLFGVCMGLQCIGEA-----------FGGKIVR---SPFGVMHgkssM----VHYdeKGEEGLFSGLSNpfivGRY--- 150
Cdd:PRK13181  73 QPVLGICLGMQLLFESseegnvkglglIPGDVKRfrsEPLKVPQ----MgwnsVKP--LKESPLFKGIEE----GSYfyf 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395596  151 -HSLVIEkdtfPSDELEVTAWTEDGLVMAARHRKyKHIQGVQFHPE--SIItteGKTIVRNFIKI 212
Cdd:PRK13181 143 vHSYYVP----CEDPEDVLATTEYGVPFCSAVAK-DNIYAVQFHPEksGKA---GLKLLKNFAEL 199
 
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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