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Conserved domains on  [gi|1391039412|ref|WP_109247617|]
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aminodeoxychorismate/anthranilate synthase component II [Shewanella algae]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 2-191 9.93e-113

anthranilate synthase component II; Provisional


:

Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 319.38  E-value: 9.93e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   2 KLYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPIL 81
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPD----AIVLSPGPGTPAEAGISLELIREFAGKVPIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  82 GICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTE-GMPMAIS 158
Cdd:PRK05670   77 GVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDResLPDCLEVTAWTDdGEIMGVR 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1391039412 159 HRCDAAVGFQFHPESILTTLGSTLLVQTLQYLT 191
Cdd:PRK05670  157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 2-191 9.93e-113

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 319.38  E-value: 9.93e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   2 KLYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPIL 81
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPD----AIVLSPGPGTPAEAGISLELIREFAGKVPIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  82 GICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTE-GMPMAIS 158
Cdd:PRK05670   77 GVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDResLPDCLEVTAWTDdGEIMGVR 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1391039412 159 HRCDAAVGFQFHPESILTTLGSTLLVQTLQYLT 191
Cdd:PRK05670  157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 5-183 1.50e-100

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: 288.47  E-value: 1.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAqlLAERMLAEPgqAALILSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:COG0512     3 LIDNYDSFTYNLVQYLGELGAEVVVVRNDEIT--LEEIEALAP--DGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTE-GMPMAISHRC 161
Cdd:COG0512    79 LGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRetLPDELEVTAWTEdGEIMGIRHRE 158

                         170       180
                  ....*....|....*....|..
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLL 183
Cdd:COG0512   159 LPIEGVQFHPESILTEHGHQLL 180
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 5-187 7.83e-87

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: 253.61  E-value: 7.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:cd01743     3 LIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPD----AIVISPGPGHPEDAGISLEIIRALAGKVPILGVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATKV--PDCLEVIATTE-GMPMAISHRC 161
Cdd:cd01743    79 LGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDplPDLLEVTASTEdGVIMALRHRD 158

                         170       180
                  ....*....|....*....|....*.
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLLVQTL 187
Cdd:cd01743   159 LPIYGVQFHPESILTEYGLRLLENFL 184
Anth_synII_Halo NF041322
anthranilate synthase component II;
7-179 1.67e-62

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 192.17  E-value: 1.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   7 DNFDSFTYNLVDQF--RSLGFEVLVYRNNVSaqlLAERMLAEPGqaALILSPGPGAP---REAGCMMELIALLAGKLPIL 81
Cdd:NF041322    3 DNFDSFTYNLVEYVseQREHAETTVLKNTAS---LAEVRAVDPD--AIVISPGPGHPkndRDVGVTADVLRELSPEVPTL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  82 GICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATKVPDCLEVIATT----EGMPMAI 157
Cdd:NF041322   78 GVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCFEVTATTdhdgEELVMGI 157

                         170       180
                  ....*....|....*....|..
gi 1391039412 158 SHRCDAAVGFQFHPESILTTLG 179
Cdd:NF041322  158 RHREHPIECVQFHPESVLTGVG 179
GATase pfam00117
Glutamine amidotransferase class-I;
5-183 2.25e-61

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 188.99  E-value: 2.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQllaERMLAEPgqAALILSPGPGAPREAGCMMELI-ALLAGKLPILGI 83
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAE---EILEENP--DGIILSGGPGSPGAAGGAIEAIrEARELKIPILGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  84 CLGHQALVEHYGGKVERAPQVV-HGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTE--GMPMAIS 158
Cdd:pfam00117  77 CLGHQLLALAFGGKVVKAKKFGhHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSEndGTIMGIR 156

                         170       180
                  ....*....|....*....|....*
gi 1391039412 159 HRCDAAVGFQFHPESILTTLGSTLL 183
Cdd:pfam00117 157 HKKLPIFGVQFHPESILTPHGPEIL 181
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-183 1.34e-58

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: 182.30  E-value: 1.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   3 LYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPILG 82
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPL----LIVISPGPCTPNEAGISLEAIRHFAGKLPILG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  83 ICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLV--ATKVPDCLEVIATTE--GMPMAIS 158
Cdd:TIGR00566  78 VCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVvePETLPTCFPVTAWEEenIEIMAIR 157

                         170       180
                  ....*....|....*....|....*
gi 1391039412 159 HRCDAAVGFQFHPESILTTLGSTLL 183
Cdd:TIGR00566 158 HRDLPLEGVQFHPESILSEQGHQLL 182
 
Name Accession Description Interval E-value
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 2-191 9.93e-113

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 319.38  E-value: 9.93e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   2 KLYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPIL 81
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPD----AIVLSPGPGTPAEAGISLELIREFAGKVPIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  82 GICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTE-GMPMAIS 158
Cdd:PRK05670   77 GVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDResLPDCLEVTAWTDdGEIMGVR 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1391039412 159 HRCDAAVGFQFHPESILTTLGSTLLVQTLQYLT 191
Cdd:PRK05670  157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 5-183 1.50e-100

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: 288.47  E-value: 1.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAqlLAERMLAEPgqAALILSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:COG0512     3 LIDNYDSFTYNLVQYLGELGAEVVVVRNDEIT--LEEIEALAP--DGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTE-GMPMAISHRC 161
Cdd:COG0512    79 LGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRetLPDELEVTAWTEdGEIMGIRHRE 158

                         170       180
                  ....*....|....*....|..
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLL 183
Cdd:COG0512   159 LPIEGVQFHPESILTEHGHQLL 180
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 5-187 7.83e-87

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: 253.61  E-value: 7.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:cd01743     3 LIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPD----AIVISPGPGHPEDAGISLEIIRALAGKVPILGVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATKV--PDCLEVIATTE-GMPMAISHRC 161
Cdd:cd01743    79 LGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDplPDLLEVTASTEdGVIMALRHRD 158

                         170       180
                  ....*....|....*....|....*.
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLLVQTL 187
Cdd:cd01743   159 LPIYGVQFHPESILTEYGLRLLENFL 184
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 3-197 5.68e-82

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 252.64  E-value: 5.68e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   3 LYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERmLAEPGQAALILSPGPGAPREAGCMMELIALLAGKLPILG 82
Cdd:PRK09522    4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIER-LATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  83 ICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATKVPDCLEVIATTEGMPMAISHRCD 162
Cdd:PRK09522   83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHDAD 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1391039412 163 AAVGFQFHPESILTTLGSTLLVQTLQYLTMSREET 197
Cdd:PRK09522  163 RVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPT 197
Anth_synII_Halo NF041322
anthranilate synthase component II;
7-179 1.67e-62

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 192.17  E-value: 1.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   7 DNFDSFTYNLVDQF--RSLGFEVLVYRNNVSaqlLAERMLAEPGqaALILSPGPGAP---REAGCMMELIALLAGKLPIL 81
Cdd:NF041322    3 DNFDSFTYNLVEYVseQREHAETTVLKNTAS---LAEVRAVDPD--AIVISPGPGHPkndRDVGVTADVLRELSPEVPTL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  82 GICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATKVPDCLEVIATT----EGMPMAI 157
Cdd:NF041322   78 GVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCFEVTATTdhdgEELVMGI 157

                         170       180
                  ....*....|....*....|..
gi 1391039412 158 SHRCDAAVGFQFHPESILTTLG 179
Cdd:NF041322  158 RHREHPIECVQFHPESVLTGVG 179
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
2-197 2.33e-62

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 201.87  E-value: 2.33e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   2 KLYLLDNFDSFTYNLVDQFRSLGFE-VLVYRNNVSAQLLAERMlaEPgqAALILSPGPGAPREAGCMMELIALLAGKLPI 80
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEAL--NP--SHIVISPGPGRPEEAGISVEVIRHFSGKVPI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  81 LGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLV--ATKVPDCLEVIA-TTEGMPMAI 157
Cdd:PRK14607   77 LGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVveEASLPECLEVTAkSDDGEIMGI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1391039412 158 SHRCDAAVGFQFHPESILTTLGSTLLvqtLQYLTMSREET 197
Cdd:PRK14607  157 RHKEHPIFGVQFHPESILTEEGKRIL---KNFLNYQREEI 193
GATase pfam00117
Glutamine amidotransferase class-I;
5-183 2.25e-61

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 188.99  E-value: 2.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQllaERMLAEPgqAALILSPGPGAPREAGCMMELI-ALLAGKLPILGI 83
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAE---EILEENP--DGIILSGGPGSPGAAGGAIEAIrEARELKIPILGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  84 CLGHQALVEHYGGKVERAPQVV-HGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTE--GMPMAIS 158
Cdd:pfam00117  77 CLGHQLLALAFGGKVVKAKKFGhHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSEndGTIMGIR 156

                         170       180
                  ....*....|....*....|....*
gi 1391039412 159 HRCDAAVGFQFHPESILTTLGSTLL 183
Cdd:pfam00117 157 HKKLPIFGVQFHPESILTPHGPEIL 181
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-183 1.34e-58

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: 182.30  E-value: 1.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   3 LYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPILG 82
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPL----LIVISPGPCTPNEAGISLEAIRHFAGKLPILG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  83 ICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLV--ATKVPDCLEVIATTE--GMPMAIS 158
Cdd:TIGR00566  78 VCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVvePETLPTCFPVTAWEEenIEIMAIR 157

                         170       180
                  ....*....|....*....|....*
gi 1391039412 159 HRCDAAVGFQFHPESILTTLGSTLL 183
Cdd:TIGR00566 158 HRDLPLEGVQFHPESILSEQGHQLL 182
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
5-198 1.45e-58

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 182.31  E-value: 1.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:PRK07649    4 MIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPD----FLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIA-TTEGMPMAISHRC 161
Cdd:PRK07649   80 LGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKetLPDCLEVTSwTEEGEIMAIRHKT 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLLVQTLQylTMSREETC 198
Cdd:PRK07649  160 LPIEGVQFHPESIMTSHGKELLQNFIR--KYSPSVTS 194
trpG CHL00101
anthranilate synthase component 2
 5-191 3.72e-56

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 176.08  E-value: 3.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNN----VSAQLLAERmlaepgqaALILSPGPGAPREAGCMMELIALLAGKLPI 80
Cdd:CHL00101    4 IIDNYDSFTYNLVQSLGELNSDVLVCRNDeidlSKIKNLNIR--------HIIISPGPGHPRDSGISLDVISSYAPYIPI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  81 LGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATKV--PDCLEVIA-TTEGMPMAI 157
Cdd:CHL00101   76 LGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLnlPSPLEITAwTEDGLIMAC 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1391039412 158 SHRCDAAV-GFQFHPESILTTLGSTLLVQTLQYLT 191
Cdd:CHL00101  156 RHKKYKMLrGIQFHPESLLTTHGQQILRNFLSLSS 190
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
3-189 1.63e-55

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 174.28  E-value: 1.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   3 LYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNvsaqllaERMLAEPGQAA---LILSPGPGAPREAGCMMELIALLAGKLP 79
Cdd:PRK06774    2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRND-------ELQLTDIEQLApshLVISPGPCTPNEAGISLAVIRHFADKLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  80 ILGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLV--ATKVPDCLEVIATTE-----G 152
Cdd:PRK06774   75 ILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLViaADSLPGCFELTAWSErggemD 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1391039412 153 MPMAISHRCDAAVGFQFHPESILTTLGSTLLVQTLQY 189
Cdd:PRK06774  155 EIMGIRHRTLPLEGVQFHPESILSEQGHQLLDNFLKN 191
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
5-188 4.30e-55

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 173.18  E-value: 4.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNvsAQLLAERMLAEPGQaaLILSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:PRK08007    4 LIDNYDSFTWNLYQYFCELGADVLVKRND--ALTLADIDALKPQK--IVISPGPCTPDEAGISLDVIRHYAGRLPILGVC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVA--TKVPDCLEVIATTE-GMPMAISHRC 161
Cdd:PRK08007   80 LGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVepDSLPACFEVTAWSEtREIMGIRHRQ 159

                         170       180
                  ....*....|....*....|....*..
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLLVQTLQ 188
Cdd:PRK08007  160 WDLEGVQFHPESILSEQGHQLLANFLH 186
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
1-189 1.34e-54

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 172.93  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   1 MKLYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNvsaqllaERMLAEPGQAA-----LILSPGPGAPREAGCMMELI-ALL 74
Cdd:PRK07765    1 MRILVVDNYDSFVFNLVQYLGQLGVEAEVWRND-------DPRLADEAAVAaqfdgVLLSPGPGTPERAGASIDMVrACA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  75 AGKLPILGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVA--TKVPDCLEVIATTE- 151
Cdd:PRK07765   74 AAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTIlpETLPAELEVTARTDs 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1391039412 152 GMPMAISHRCDAAVGFQFHPESILTTLGSTLLVQTLQY 189
Cdd:PRK07765  154 GVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWLTV 191
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
3-188 3.11e-54

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 171.21  E-value: 3.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   3 LYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNvSAQLLAERMLAEpgqAALILSPGPGAPREAGCMMELIALLAGKLPILG 82
Cdd:PRK08857    2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRND-EIDIDGIEALNP---THLVISPGPCTPNEAGISLQAIEHFAGKLPILG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  83 ICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATK--VPDCLEVIATTEGMP------ 154
Cdd:PRK08857   78 VCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNdtLPECFELTAWTELEDgsmdei 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1391039412 155 MAISHRCDAAVGFQFHPESILTTLGSTLLVQTLQ 188
Cdd:PRK08857  158 MGFQHKTLPIEAVQFHPESIKTEQGHQLLANFLA 191
PRK13566 PRK13566
anthranilate synthase component I;
1-180 3.74e-50

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 172.41  E-value: 3.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   1 MKLYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVsaqllAERMLAEPGQAALILSPGPGAPREAGCMMELIALLAGKLPI 80
Cdd:PRK13566  527 KRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGF-----AEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPI 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  81 LGICLGHQALVEHYGGKVERAPQVVHGKASPVEHN-CDGLFTNLPSPLPVARYHSLVAT--KVPDCLEVIATTE-GMPMA 156
Cdd:PRK13566  602 FGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRgPGRLFSGLPEEFTVGRYHSLFADpeTLPDELLVTAETEdGVIMA 681

                         170       180
                  ....*....|....*....|....
gi 1391039412 157 ISHRCDAAVGFQFHPESILTTLGS 180
Cdd:PRK13566  682 IEHKTLPVAAVQFHPESIMTLGGD 705
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 5-190 5.07e-49

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 158.47  E-value: 5.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQllaERMLAEPgqAALILSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:PRK05637    6 LIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVE---EILAANP--DLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVErAPQVVHGKASPVEHNCDG----LFTNLPSP------------LPVARYHSLVATKVPDCLEVIA 148
Cdd:PRK05637   81 LGFQALLEHHGGKVE-PCGPVHGTTDNMILTDAGvqspVFAGLATDvepdhpeipgrkVPIARYHSLGCVVAPDGMESLG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1391039412 149 TTEG----MPMAISHRCDAAVGFQFHPESILTTLGSTLLVQTLQYL 190
Cdd:PRK05637  160 TCSSeigpVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQL 205
PLN02335 PLN02335
anthranilate synthase
 5-183 8.90e-49

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 158.42  E-value: 8.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSLGFEVLVYRNNvsaQLLAERMLAEPGQAALIlSPGPGAPREAGCMMELIALLAGKLPILGIC 84
Cdd:PLN02335   23 VIDNYDSFTYNLCQYMGELGCHFEVYRND---ELTVEELKRKNPRGVLI-SPGPGTPQDSGISLQTVLELGPLVPLFGVC 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  85 LGHQALVEHYGGKVERAPQ-VVHGKASPVEHN---CDGLFTNLPSPLPVARYHSLVATK--VP-DCLEVIATTE-GMPMA 156
Cdd:PLN02335   99 MGLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKdtFPsDELEVTAWTEdGLIMA 178

                         170       180
                  ....*....|....*....|....*...
gi 1391039412 157 ISHRCDAAV-GFQFHPESILTTLGSTLL 183
Cdd:PLN02335  179 ARHRKYKHIqGVQFHPESIITTEGKTIV 206
PRK06895 PRK06895
anthranilate synthase component II;
1-188 2.99e-32

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 114.83  E-value: 2.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   1 MKLYLLDNFDSFTYNLVDQFRSLGFEVLVyrnnVSAQLLAERMLAEpgQAALILSPGPGAPREAGCMMELIALLAGKLPI 80
Cdd:PRK06895    2 TKLLIINNHDSFTFNLVDLIRKLGVPMQV----VNVEDLDLDEVEN--FSHILISPGPDVPRAYPQLFAMLERYHQHKSI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  81 LGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDG-LFTNLPSPLPVARYHSLVATK--VPDCLEVIAT-TEGMPMA 156
Cdd:PRK06895   76 LGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEenFPTPLEITAVcDENVVMA 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1391039412 157 ISHRCDAAVGFQFHPESILTTLGSTLLVQTLQ 188
Cdd:PRK06895  156 MQHKTLPIYGVQFHPESYISEFGEQILRNWLA 187
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 3-183 2.96e-28

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


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 104.70  E-value: 2.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   3 LYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERmlaEPgqAALILSPGPGAPREAGCMMELIALLAGKLPILG 82
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREK---NP--KGIILSGGPSSVYAENAPRADEKIFELGVPVLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  83 ICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLPSPLPVARYHSLVATKVPDCLEVIATTEGMPM-AISHRC 161
Cdd:TIGR00888  76 ICYGMQLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVaAMAHEE 155

                         170       180
                  ....*....|....*....|..
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLL 183
Cdd:TIGR00888 156 KPIYGVQFHPEVTHTEYGNELL 177
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 5-193 6.83e-27

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


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 106.91  E-value: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVD---QFRSLGFEVL-VYRNNVSAQLLAERMLAEpgqaALILSPGPGAPREA---GCMMELIAL-LAG 76
Cdd:TIGR01823  10 FIDSYDSFTYNVVRlleQQTDISVHVTtVHSDTFQDQLLELLPLFD----AIVVGPGPGNPNNAqdmGIISELWELaNLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  77 KLPILGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLpSPLPVARYHSLVATKVP-DCLEVIATTEG--- 152
Cdd:TIGR01823  86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLYANPEGiDTLLPLCLTEDeeg 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1391039412 153 -MPMAISHRCDAAVGFQFHPESILTTLGSTLLVQtlQYLTMS 193
Cdd:TIGR01823 165 iILMSAQTKKKPWFGVQYHPESCCSELGSGKLVS--NFLKLA 204
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 7-172 2.00e-25

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: 98.09  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   7 DNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERMLAEPgqAALILSPGP-GAPREAGCMMELIAL----LAGKLPIL 81
Cdd:COG0518     9 PFGGQYPGLIARRLREAGIELDVLRVYAGEILPYDPDLEDP--DGLILSGGPmSVYDEDPWLEDEPALireaFELGKPVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  82 GICLGHQALVEHYGGKVERAPQVVHGKAsPVE-HNCDGLFTNLPSPLPVARYHSLVATKVPDCLEVIATTEGMP-MAISH 159
Cdd:COG0518    87 GICYGAQLLAHALGGKVEPGPGREIGWA-PVElTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCPnQAFRY 165

                         170
                  ....*....|...
gi 1391039412 160 RcDAAVGFQFHPE 172
Cdd:COG0518   166 G-RRVYGVQFHPE 177
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 5-182 3.66e-25

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 101.85  E-value: 3.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   5 LLDNFDSFTYNLVDQFRSL-GFEVLVYRNN------VSAQLLAERMLAEpgqaaLILSPGPGAPREA---GCMMELIaLL 74
Cdd:PLN02889   86 LIDNYDSYTYNIYQELSIVnGVPPVVVRNDewtweeVYHYLYEEKAFDN-----IVISPGPGSPTCPadiGICLRLL-LE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  75 AGKLPILGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNLP----SPLPVARYHSLV--ATKVPDCLEVIA 148
Cdd:PLN02889  160 CRDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVidAESLPKELVPIA 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412 149 TT-------------------------------------------------EGMP-----MAISHRCDAAVGFQFHPESI 174
Cdd:PLN02889  240 WTsssdtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsERMQngkilMGIMHSTRPHYGLQFHPESI 319


                  ....*...
gi 1391039412 175 LTTLGSTL 182
Cdd:PLN02889  320 ATCYGRQI 327
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 4-183 5.70e-25

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


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 95.68  E-value: 5.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   4 YLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAERmlaepGQAALILSPGPGAPREAGCMMELIALLAGKLPILGI 83
Cdd:cd01742     2 LILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLK-----NPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  84 CLGHQALVEHYGGKVERAPQVVHGKASP-VEHNCDgLFTNLPSPLPVARYHSLVATKVPDCLEVIATTEGMPM-AISHRC 161
Cdd:cd01742    77 CYGMQLIAKALGGKVERGDKREYGKAEIeIDDSSP-LFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVaAIANEE 155

                         170       180
                  ....*....|....*....|..
gi 1391039412 162 DAAVGFQFHPESILTTLGSTLL 183
Cdd:cd01742   156 KKIYGVQFHPEVTHTEKGKEIL 177
guaA PRK00074
GMP synthase; Reviewed
 50-183 2.57e-22

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 93.57  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  50 AALILSPGP------GAPReagCMMELIALlagKLPILGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDGLFTNL 123
Cdd:PRK00074   48 KGIILSGGPasvyeeGAPR---ADPEIFEL---GVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGL 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391039412 124 PSPLPVARYHSLVATKVPDCLEVIATTEGMPMA-ISHRCDAAVGFQFHPESILTTLGSTLL 183
Cdd:PRK00074  122 PEEQDVWMSHGDKVTELPEGFKVIASTENCPIAaIANEERKFYGVQFHPEVTHTPQGKKLL 182
PRK00758 PRK00758
GMP synthase subunit A; Validated
 2-172 9.22e-19

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 79.51  E-value: 9.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   2 KLYLLDNFDSFTYNLVDQFRSLGFEVLVYRNNVSAQLLAErmlaepGQAALILSPGPGAPREAGCmmELIaLLAGKLPIL 81
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKA------FEDGLILSGGPDIERAGNC--PEY-LKELDVPIL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  82 GICLGHQALVEHYGGKVERAPqvvHGKASPVEHNC---DGLFTNLPSPLPVARYHSLVATKVPDCLEVIATTEGMPM-AI 157
Cdd:PRK00758   72 GICLGHQLIAKAFGGEVGRGE---YGEYALVEVEIldeDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVeAM 148

                         170
                  ....*....|....*
gi 1391039412 158 SHRCDAAVGFQFHPE 172
Cdd:PRK00758  149 KHKEKPIYGVQFHPE 163
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 68-172 2.50e-15

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 70.74  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  68 MELI-ALLAGKLPILGICLGHQALVEHYGGKVERAPQVVHGKASPVEHNCDG----LFTNLPSPLPVARYHSLVATKVPD 142
Cdd:cd01741    71 KELIrQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadpLFAGLPDEFPVFHWHGDTVVELPP 150

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1391039412 143 CLEVIATTEGMP---MAIShrcDAAVGFQFHPE 172
Cdd:cd01741   151 GAVLLASSEACPnqaFRYG---DRALGLQFHPE 180
PLN02347 PLN02347
GMP synthetase
 51-183 3.18e-14

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 70.10  E-value: 3.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  51 ALILSPGP------GAPREAGCMMELIAllAGKLPILGICLGHQALVEHYGGKVERAPQVVHGKAsPVEHNCD-GLFTNL 123
Cdd:PLN02347   56 VVILSGGPhsvhveGAPTVPEGFFDYCR--ERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRM-EIRVVCGsQLFGDL 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391039412 124 PSPLPVARY--HSLVATKVPDCLEVIATTE-GMPMAISHRCDAAVGFQFHPESILTTLGSTLL 183
Cdd:PLN02347  133 PSGETQTVWmsHGDEAVKLPEGFEVVAKSVqGAVVAIENRERRIYGLQYHPEVTHSPKGMETL 195
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 14-173 7.26e-11

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: 58.28  E-value: 7.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  14 YNLVDQFRSLGFEVLVYRNNVSAQllaERMLAEPgqAALILSPGPGAPREAG-CMMELIALLAGKLPILGICLGHQALVE 92
Cdd:cd01744    10 HNILRELLKRGCEVTVVPYNTDAE---EILKLDP--DGIFLSNGPGDPALLDeAIKTVRKLLGKKIPIFGICLGHQLLAL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  93 HYGGKVERAPQVVHGKASPVEHNCDG--LFTnlpsplpvARYH--SLVATKVPDCLEV------IATTEGmpmaISHRCD 162
Cdd:cd01744    85 ALGAKTYKMKFGHRGSNHPVKDLITGrvYIT--------SQNHgyAVDPDSLPGGLEVthvnlnDGTVEG----IRHKDL 152

                         170
                  ....*....|.
gi 1391039412 163 AAVGFQFHPES 173
Cdd:cd01744   153 PVFSVQFHPEA 163
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 7-91 1.54e-10

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 56.07  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   7 DNFDSFTYNLVDQFRSLGFEVLVyrnnVSAQLLAERMLAEPGQA-ALILSPGPGAPREAGCMMELIALL----AGKLPIL 81
Cdd:cd01653     8 GFEELELASPLDALREAGAEVDV----VSPDGGPVESDVDLDDYdGLILPGGPGTPDDLARDEALLALLreaaAAGKPIL 83

                          90
                  ....*....|
gi 1391039412  82 GICLGHQALV 91
Cdd:cd01653    84 GICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 7-90 1.15e-09

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 53.36  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   7 DNFDSFTYNLVDQFRSLGFEVLVyrnnVSAQLLAERMLAEPGQA-ALILSPGPGAPREAGCMMELIALL----AGKLPIL 81
Cdd:cd03128     8 GSEELELASPLDALREAGAEVDV----VSPDGGPVESDVDLDDYdGLILPGGPGTPDDLAWDEALLALLreaaAAGKPVL 83


                  ....*....
gi 1391039412  82 GICLGHQAL 90
Cdd:cd03128    84 GICLGAQLL 92
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 14-173 1.30e-09

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 56.53  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  14 YNLVDQFRSLGFEVLVYRNNVSAqllAERMLAEPGqaALILSPGPGAPREAGCMMELIALLAGKLPILGICLGHQALVEH 93
Cdd:PLN02771  252 HNILRRLASYGCKITVVPSTWPA---SEALKMKPD--GVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQA 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  94 YGGKVERAPQVVHGKASPVEHNCDGLFTnlpsplPVARYHSLVA--TKVPDCLEV--IATTEGMPMAISHRCDAAVGFQF 169
Cdd:PLN02771  327 LGGKTFKMKFGHHGGNHPVRNNRTGRVE------ISAQNHNYAVdpASLPEGVEVthVNLNDGSCAGLAFPALNVMSLQY 400


                  ....
gi 1391039412 170 HPES 173
Cdd:PLN02771  401 HPEA 404
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
14-99 2.04e-09

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 55.85  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  14 YNLVDQFRSLGFEVLVyrnnVSAQLLAERMLA-EPGqaALILSPGPGAPREAGCMMELI-ALLAGKLPILGICLGHQALV 91
Cdd:PRK12564  189 RNILRELAERGCRVTV----VPATTTAEEILAlNPD--GVFLSNGPGDPAALDYAIEMIrELLEKKIPIFGICLGHQLLA 262


                  ....*...
gi 1391039412  92 EHYGGKVE 99
Cdd:PRK12564  263 LALGAKTY 270
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 14-173 4.18e-09

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: 54.94  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  14 YNLVDQFRSLGFEVLVYRNNVSAQllaERMLAEPGqaALILSPGPGAPREAGCMMELIALLAGKLPILGICLGHQALVEH 93
Cdd:TIGR01368 184 RNILRRLVKRGCEVTVVPYDTDAE---EIKKYNPD--GIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALA 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  94 YGGKVERAPQVVHGKASPVEHNCDG--LFTnlpsplpvARYHSLV---ATKVPDCLEVI------ATTEGmpmaISHRCD 162
Cdd:TIGR01368 259 FGAKTYKMKFGHRGGNHPVKDLITGrvEIT--------SQNHGYAvdpDSLPAGDLEVThvnlndGTVEG----IRHKDL 326

                         170
                  ....*....|.
gi 1391039412 163 AAVGFQFHPES 173
Cdd:TIGR01368 327 PVFSVQYHPEA 337
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 14-90 4.84e-09

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: 54.64  E-value: 4.84e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391039412  14 YNLVDQFRSLGFEVLVyrnnVSAQLLAERMLA-EPgqAALILSPGPGAPREAGCMMELI-ALLAGKLPILGICLGHQAL 90
Cdd:COG0505   188 RNILRELAERGCRVTV----VPATTSAEEILAlNP--DGVFLSNGPGDPAALDYAIETIrELLGKGIPIFGICLGHQLL 260
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 52-185 5.08e-09

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 54.20  E-value: 5.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  52 LILSPGPGAPRE---------AGCMMELI--ALLAGKLpILGICLGHQALVEHYGGKVERAPQVVHGKAsPVEHNCDGL- 119
Cdd:PRK08250   49 LIVMGGPQSPRTtreecpyfdSKAEQRLInqAIKAGKA-VIGVCLGAQLIGEALGAKYEHSPEKEIGYF-PITLTEAGLk 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391039412 120 ---FTNLPSPLPVARYHSLVATKVPDClEVIATTEGMPMAISHRCDAAVGFQFHPESILTTLgsTLLVQ 185
Cdd:PRK08250  127 dplLSHFGSTLTVGHWHNDMPGLTDQA-KVLATSEGCPRQIVQYSNLVYGFQCHMEFTVEAV--ELLIA 192
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 51-172 5.45e-09

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 53.60  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  51 ALILsPGPGAPREAgcMMELIAL----------LAGKlPILGICLGHQALVEH---YG---------GKVERAP------ 102
Cdd:PRK13141   40 GVIL-PGVGAFPDA--MANLRERgldevikeavASGK-PLLGICLGMQLLFESseeFGeteglgllpGRVRRFPpeeglk 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412 103 -------QVVHGKASPvehncdgLFTNLPSPLPVarY--HSLVAtKVPDCLEVIATTE-GMPMAISHRCDAAVGFQFHPE 172
Cdd:PRK13141  116 vphmgwnQLELKKESP-------LLKGIPDGAYV--YfvHSYYA-DPCDEEYVAATTDyGVEFPAAVGKDNVFGAQFHPE 185
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 20-172 7.03e-09

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


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 53.27  E-value: 7.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  20 FRSLGFEVLVYRNNvsaqllAERMLAEpgqaALILsPGPGAPREAgcmME----------LIALLAGKLPILGICLGHQA 89
Cdd:cd01748    18 LERLGAEVIITSDP------EEILSAD----KLIL-PGVGAFGDA---MAnlrerglieaLKEAIASGKPFLGICLGMQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  90 LVEH------------YGGKVERAP-------------QVVHGKASPvehncdgLFTNLPsplPVARY---HSLVATkVP 141
Cdd:cd01748    84 LFESseegggtkglglIPGKVVRFPaseglkvphmgwnQLEITKESP-------LFKGIP---DGSYFyfvHSYYAP-PD 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1391039412 142 DCLEVIATTE-GMPMAISHRCDAAVGFQFHPE 172
Cdd:cd01748   153 DPDYILATTDyGGKFPAAVEKDNIFGTQFHPE 184
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 51-112 3.76e-08

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 52.20  E-value: 3.76e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391039412  51 ALILSPGPGAPREAGCMMELIALLAGKLPILGICLGHQALVEHYGGKVERAPQVVHGKASPV 112
Cdd:PRK12838  211 GIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPV 272
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 51-172 1.13e-07

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: 49.65  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  51 ALILsPGPGAPREagCMMELIAL---------LAGKLPILGICLGHQALVEH---YG---------GKVERAP------- 102
Cdd:COG0118    41 RLVL-PGVGAFGD--AMENLRERgldeaireaVAGGKPVLGICLGMQLLFERseeNGdteglglipGEVVRFPasdlkvp 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391039412 103 -----QVVHGKASPvehncdgLFTNLPSPlpvARY---HSLVAtKVPDCLEVIATTE-GMPMAISHRCDAAVGFQFHPE 172
Cdd:COG0118   118 hmgwnTVEIAKDHP-------LFAGIPDG---EYFyfvHSYYV-PPDDPEDVVATTDyGVPFTAAVERGNVFGTQFHPE 185
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 68-172 3.53e-07

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: 48.34  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  68 MELI-ALLAGKLPILGICLGHQALVEHYGGKVERAPQVvhgkaspvehNCdglftnlpsplpvarYHSLVATKVPDCLEV 146
Cdd:cd01745    90 LALLrAALERGKPILGICRGMQLLNVALGGTLYQDIRV----------NS---------------LHHQAIKRLADGLRV 144

                          90       100
                  ....*....|....*....|....*...
gi 1391039412 147 IATTE-GMPMAISHRCDA-AVGFQFHPE 172
Cdd:cd01745   145 EARAPdGVIEAIESPDRPfVLGVQWHPE 172
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 73-172 5.47e-07

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 48.42  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  73 LLAGKLPILGICLGHQALVEHYGGKVERAPQvvhGKAS---PVE-HNC---DGLFTNLPSPLPVARYHSLVATKVPDCLE 145
Cdd:PRK09065   84 AAAAGMPLLGICYGHQLLAHALGGEVGYNPA---GRESgtvTVElHPAaadDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                          90       100
                  ....*....|....*....|....*..
gi 1391039412 146 VIATTEGMPMAISHRCDAAVGFQFHPE 172
Cdd:PRK09065  161 VLARSAQDPHQAFRYGPHAWGVQFHPE 187
PRK05665 PRK05665
amidotransferase; Provisional
 70-174 8.42e-07

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 47.88  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  70 LIALLAGKLPILGICLGHQALVEHYGGKVERAPQ-----VVHGKASPVEHNCDGLFTNLpsPLPVAryHSLVATKVPDCL 144
Cdd:PRK05665   84 LLKLYERGDKLLGVCFGHQLLALLLGGKAERASQgwgvgIHRYQLAAHAPWMSPAVTEL--TLLIS--HQDQVTALPEGA 159

                          90       100       110
                  ....*....|....*....|....*....|
gi 1391039412 145 EVIATTEGMPMAISHRCDAAVGFQFHPESI 174
Cdd:PRK05665  160 TVIASSDFCPFAAYHIGDQVLCFQGHPEFV 189
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 48-172 1.65e-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: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  48 GQAALILSPGPGA-------PREAGCMMELIALLAGKLPILGICLGHQALVEH------------YGGKVERApqvvhgK 108
Cdd:TIGR01855  35 ELADKLILPGVGAfgaamarLRENGLDLFVELVVRLGKPVLGICLGMQLLFERseegggvpglglIKGNVVKL------E 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391039412 109 ASPVEH-NCDGLFTNLPSPLP-----VARY---HSLVAtkVPDCLEVIATTE-GMPMAISHRCDAAVGFQFHPE 172
Cdd:TIGR01855 109 ARKVPHmGWNEVHPVKESPLLngideGAYFyfvHSYYA--VCEEEAVLAYADyGEKFPAAVQKGNIFGTQFHPE 180
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 48-172 6.09e-06

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: 45.33  E-value: 6.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  48 GQAALILSPGPGAPREAGCMMELIALLAGKLPILGICLGHQALVEHYGG----KVERAPQVVH----------GKASPVE 113
Cdd:pfam07722  76 GEEPSESGGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGtlyqDIQEQPGFTDhrehcqvapyAPSHAVN 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391039412 114 HNCDGLFTNLPSP--LPVARYHSLVATKVPDCLEVIATTE-GMPMAISHRcDA---AVGFQFHPE 172
Cdd:pfam07722 156 VEPGSLLASLLGSeeFRVNSLHHQAIDRLAPGLRVEAVAPdGTIEAIESP-NAkgfALGVQWHPE 219
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 14-97 2.55e-05

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 44.02  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  14 YNLVDQFRSLGFEVLVYRNNVSAQLLaerMLAEPGqaALILSPGPGAPREAG-CMMELIALLAGKLPILGICLGHQALVE 92
Cdd:CHL00197  204 YNILRRLKSFGCSITVVPATSPYQDI---LSYQPD--GILLSNGPGDPSAIHyGIKTVKKLLKYNIPIFGICMGHQILSL 278


                  ....*
gi 1391039412  93 HYGGK 97
Cdd:CHL00197  279 ALEAK 283
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 56-172 1.51e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 40.92  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  56 PGPGAprEAGCMMEL-----------IALLAGKlPILGICLGHQAL----VEH--------YGGKVERAP---------- 102
Cdd:PRK13146   48 PGVGA--FADCMRGLravglgeavieAVLAAGR-PFLGICVGMQLLfergLEHgdtpglglIPGEVVRFQpdgpalkvph 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412 103 ----QVVHGKASPvehncdgLFTNLPsplPVARY---HSL-VATKVPDclEVIATTE-GMPM-AISHRcDAAVGFQFHPE 172
Cdd:PRK13146  125 mgwnTVDQTRDHP-------LFAGIP---DGARFyfvHSYyAQPANPA--DVVAWTDyGGPFtAAVAR-DNLFATQFHPE 191
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 71-172 3.62e-04

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 39.94  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  71 IALLAGKlPILGICLGHQALVEHYGGKVERAPQvvhGKAS----PVEHNCDGLfTNLPSPLPVARYHSlVATKVPDCLEV 146
Cdd:PRK06490   81 VPLKENK-PFLGICLGAQMLARHLGARVAPHPD---GRVEigyyPLRPTEAGR-ALMHWPEMVYHWHR-EGFDLPAGAEL 154

                          90       100
                  ....*....|....*....|....*.
gi 1391039412 147 IATTEGMPMAISHRCDAAVGFQFHPE 172
Cdd:PRK06490  155 LATGDDFPNQAFRYGDNAWGLQFHPE 180
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 69-172 2.26e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 37.62  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  69 ELIALLAGKL----PILGICLGHQALVEHYGGKVERAPQV----------VHGKASPVEHNCDGlftnlpspLPVARYHS 134
Cdd:PRK07053   71 PEIALLRQRLaaglPTLGICLGAQLIARALGARVYPGGQKeigwapltltDAGRASPLRHLGAG--------TPVLHWHG 142

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1391039412 135 LVATkVPDCLEVIATTEGMPMAISHRCDAAVGFQFHPE 172
Cdd:PRK07053  143 DTFD-LPEGATLLASTPACRHQAFAWGNHVLALQFHPE 179
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-172 7.69e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 35.99  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412   1 MKLYLLD----NFDSFTYnlvdQFRSLGFEVLVYRNnVSAQLLAERmlaepgqaaLILsPGPGAPREAgcmM------EL 70
Cdd:PRK13170    1 MNVVIIDtgcaNLSSVKF----AIERLGYEPVVSRD-PDVILAADK---------LFL-PGVGTAQAA---MdqlrerEL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391039412  71 IALLAG-KLPILGICLGHQALV----EHYG--------GKVERAP------------QVVHGKASPvehncdgLFTNLPS 125
Cdd:PRK13170   63 IDLIKAcTQPVLGICLGMQLLGerseESGGvdclgiidGPVKKMTdfglplphmgwnQVTPQAGHP-------LFQGIED 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1391039412 126 PLPVARYHSLvatKVPDCLEVIATTE-GMPMAISHRCDAAVGFQFHPE 172
Cdd:PRK13170  136 GSYFYFVHSY---AMPVNEYTIAQCNyGEPFSAAIQKDNFFGVQFHPE 180
 
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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