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Conserved domains on  [gi|1189717604|ref|WP_085770484|]
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aminodeoxychorismate/anthranilate synthase component II [Methylocystis bryophila]

Protein Classification

anthranilate synthase component II( domain architecture ID 11423509)

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

CATH:  3.40.50.880|3.60.120.10|3.40.50.880
EC:  4.1.3.27
Gene Ontology:  GO:0004049|GO:0000162
PubMed:  10387030|7495530|35816663
SCOP:  3001405|4002317|4003747

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 6-191 1.56e-126

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: 354.34  E-value: 1.56e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:COG0512     3 LIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLPVH 165
Cdd:COG0512    83 AIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELPIE 162

                         170       180
                  ....*....|....*....|....*.
gi 1189717604 166 GVQFHPESITSQHGHKILKNFLELAQ 191
Cdd:COG0512   163 GVQFHPESILTEHGHQLLANFLELAG 188
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 6-191 1.56e-126

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: 354.34  E-value: 1.56e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:COG0512     3 LIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLPVH 165
Cdd:COG0512    83 AIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELPIE 162

                         170       180
                  ....*....|....*....|....*.
gi 1189717604 166 GVQFHPESITSQHGHKILKNFLELAQ 191
Cdd:COG0512   163 GVQFHPESILTEHGHQLLANFLELAG 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 3-191 2.51e-119

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 335.95  E-value: 2.51e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCL 82
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  83 GHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSL 162
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*....
gi 1189717604 163 PVHGVQFHPESITSQHGHKILKNFLELAQ 191
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLELAR 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 6-187 2.74e-100

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: 287.89  E-value: 2.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:cd01743     3 LIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLPVH 165
Cdd:cd01743    83 AIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLPIY 162

                         170       180
                  ....*....|....*....|..
gi 1189717604 166 GVQFHPESITSQHGHKILKNFL 187
Cdd:cd01743   163 GVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 4-189 3.73e-82

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: 242.00  E-value: 3.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLG 83
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  84 HQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDG-LIMALSHVSL 162
Cdd:TIGR00566  82 HQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRDL 161

                         170       180
                  ....*....|....*....|....*..
gi 1189717604 163 PVHGVQFHPESITSQHGHKILKNFLEL 189
Cdd:TIGR00566 162 PLEGVQFHPESILSEQGHQLLANFLHR 188
GATase pfam00117
Glutamine amidotransferase class-I;
6-187 7.79e-70

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 210.94  E-value: 7.79e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDkISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACD-KIPIFGVCLGH 84
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  85 QAIGEAFGGEVVRAP-LPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDG-LIMALSHVSL 162
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDgTIMGIRHKKL 160

                         170       180
                  ....*....|....*....|....*
gi 1189717604 163 PVHGVQFHPESITSQHGHKILKNFL 187
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
7-190 7.89e-63

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 192.94  E-value: 7.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   7 IDNYDSFTFNLVHYFGE--LGAQVTVHRNdKISVEEVMAGSPDAIVLSPGPCTP---HEAGVCLDLIARACDKIPIFGVC 81
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkndRDVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  82 LGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVvkAETLPASLHVTATTPDG---LIMALS 158
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDHDgeeLVMGIR 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1189717604 159 HVSLPVHGVQFHPESITSQHGHKILKNFLELA 190
Cdd:NF041322  159 HREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
 
Name Accession Description Interval E-value
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 6-191 1.56e-126

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: 354.34  E-value: 1.56e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:COG0512     3 LIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLPVH 165
Cdd:COG0512    83 AIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELPIE 162

                         170       180
                  ....*....|....*....|....*.
gi 1189717604 166 GVQFHPESITSQHGHKILKNFLELAQ 191
Cdd:COG0512   163 GVQFHPESILTEHGHQLLANFLELAG 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 3-191 2.51e-119

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 335.95  E-value: 2.51e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCL 82
Cdd:PRK05670    1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  83 GHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSL 162
Cdd:PRK05670   81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                         170       180
                  ....*....|....*....|....*....
gi 1189717604 163 PVHGVQFHPESITSQHGHKILKNFLELAQ 191
Cdd:PRK05670  161 PIYGVQFHPESILTEHGHKLLENFLELAR 189
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 6-187 2.74e-100

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: 287.89  E-value: 2.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:cd01743     3 LIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLPVH 165
Cdd:cd01743    83 AIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLPIY 162

                         170       180
                  ....*....|....*....|..
gi 1189717604 166 GVQFHPESITSQHGHKILKNFL 187
Cdd:cd01743   163 GVQFHPESILTEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
3-202 1.86e-93

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 282.38  E-value: 1.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLIDNYDSFTFNLVHYFGELGA-QVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVC 81
Cdd:PRK14607    1 MIILIDNYDSFTYNIYQYIGELGPeEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  82 LGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVS 161
Cdd:PRK14607   81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1189717604 162 LPVHGVQFHPESITSQHGHKILKNFLELAQVWNDSRPRGKK 202
Cdd:PRK14607  161 HPIFGVQFHPESILTEEGKRILKNFLNYQREEIDIKSYLKK 201
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
4-188 4.15e-90

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 262.43  E-value: 4.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLG 83
Cdd:PRK07649    2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  84 HQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLP 163
Cdd:PRK07649   82 HQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTLP 161

                         170       180
                  ....*....|....*....|....*
gi 1189717604 164 VHGVQFHPESITSQHGHKILKNFLE 188
Cdd:PRK07649  162 IEGVQFHPESIMTSHGKELLQNFIR 186
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-188 2.46e-87

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 256.13  E-value: 2.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   2 AKVTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSP--DAIVLSPGPCTPHEAGVCLDLIaRAC--DKIPI 77
Cdd:PRK07765    1 MRILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAqfDGVLLSPGPGTPERAGASIDMV-RACaaAGTPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  78 FGVCLGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMAL 157
Cdd:PRK07765   80 LGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAV 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1189717604 158 SHVSLPVHGVQFHPESITSQHGHKILKNFLE 188
Cdd:PRK07765  160 RHRELPIHGVQFHPESVLTEGGHRMLANWLT 190
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 4-189 3.73e-82

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: 242.00  E-value: 3.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLG 83
Cdd:TIGR00566   2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  84 HQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDG-LIMALSHVSL 162
Cdd:TIGR00566  82 HQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRDL 161

                         170       180
                  ....*....|....*....|....*..
gi 1189717604 163 PVHGVQFHPESITSQHGHKILKNFLEL 189
Cdd:TIGR00566 162 PLEGVQFHPESILSEQGHQLLANFLHR 188
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
6-188 1.24e-79

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 235.91  E-value: 1.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:PRK06774    4 LIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTA-TTPDGL---IMALSHVS 161
Cdd:PRK06774   84 ALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAwSERGGEmdeIMGIRHRT 163

                         170       180
                  ....*....|....*....|....*..
gi 1189717604 162 LPVHGVQFHPESITSQHGHKILKNFLE 188
Cdd:PRK06774  164 LPLEGVQFHPESILSEQGHQLLDNFLK 190
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
6-187 4.35e-77

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 229.38  E-value: 4.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:PRK08857    4 MIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTP--DGL---IMALSHV 160
Cdd:PRK08857   84 AIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGSmdeIMGFQHK 163

                         170       180
                  ....*....|....*....|....*..
gi 1189717604 161 SLPVHGVQFHPESITSQHGHKILKNFL 187
Cdd:PRK08857  164 TLPIEAVQFHPESIKTEQGHQLLANFL 190
trpG CHL00101
anthranilate synthase component 2
 6-189 1.18e-76

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 228.08  E-value: 1.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQ 85
Cdd:CHL00101    4 IIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  86 AIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLP-V 164
Cdd:CHL00101   84 SIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKYKmL 163

                         170       180
                  ....*....|....*....|....*
gi 1189717604 165 HGVQFHPESITSQHGHKILKNFLEL 189
Cdd:CHL00101  164 RGIQFHPESLLTTHGQQILRNFLSL 188
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
4-187 1.25e-76

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 228.26  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLG 83
Cdd:PRK08007    2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  84 HQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLP 163
Cdd:PRK08007   82 HQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQWD 161

                         170       180
                  ....*....|....*....|....
gi 1189717604 164 VHGVQFHPESITSQHGHKILKNFL 187
Cdd:PRK08007  162 LEGVQFHPESILSEQGHQLLANFL 185
PLN02335 PLN02335
anthranilate synthase
 4-189 9.62e-74

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 221.98  E-value: 9.62e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLG 83
Cdd:PLN02335   21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  84 HQAIGEAFGGEVVRAPLPI-HGKMATILHS---GETIFRGIDGPFQATRYHSLVVKAETLPA-SLHVTATTPDGLIMALS 158
Cdd:PLN02335  101 LQCIGEAFGGKIVRSPFGVmHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1189717604 159 HVSLP-VHGVQFHPESITSQHGHKILKNFLEL 189
Cdd:PLN02335  181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIKI 212
GATase pfam00117
Glutamine amidotransferase class-I;
6-187 7.79e-70

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 210.94  E-value: 7.79e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLVHYFGELGAQVTVHRNDkISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACD-KIPIFGVCLGH 84
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  85 QAIGEAFGGEVVRAP-LPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDG-LIMALSHVSL 162
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDgTIMGIRHKKL 160

                         170       180
                  ....*....|....*....|....*
gi 1189717604 163 PVHGVQFHPESITSQHGHKILKNFL 187
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFF 185
PRK13566 PRK13566
anthranilate synthase component I;
3-191 1.67e-63

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 208.62  E-value: 1.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKisVEEVMAG-SPDAIVLSPGPCTPHEAGvCLDLIARACDK-IPIFGV 80
Cdd:PRK13566  528 RVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGF--AEEMLDRvNPDLVVLSPGPGRPSDFD-CKATIDAALARnLPIFGV 604

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  81 CLGHQAIGEAFGGEVVRAPLPIHGKMATI-LHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSH 159
Cdd:PRK13566  605 CLGLQAIVEAFGGELGQLAYPMHGKPSRIrVRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEH 684

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1189717604 160 VSLPVHGVQFHPESITS---QHGHKILKNFLELAQ 191
Cdd:PRK13566  685 KTLPVAAVQFHPESIMTlggDVGLRIIENVVRLLA 719
Anth_synII_Halo NF041322
anthranilate synthase component II;
7-190 7.89e-63

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 192.94  E-value: 7.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   7 IDNYDSFTFNLVHYFGE--LGAQVTVHRNdKISVEEVMAGSPDAIVLSPGPCTP---HEAGVCLDLIARACDKIPIFGVC 81
Cdd:NF041322    2 VDNFDSFTYNLVEYVSEqrEHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPkndRDVGVTADVLRELSPEVPTLGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  82 LGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVvkAETLPASLHVTATTPDG---LIMALS 158
Cdd:NF041322   81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDHDgeeLVMGIR 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1189717604 159 HVSLPVHGVQFHPESITSQHGHKILKNFLELA 190
Cdd:NF041322  159 HREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 1-191 2.57e-46

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 159.81  E-value: 2.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   1 MAKVTLIDNYDSFTFNLVHYFGELGAQVTVHRND---KISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPI 77
Cdd:PRK09522    1 MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  78 FGVCLGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVvkAETLPASLHVTATTpDGLIMAL 157
Cdd:PRK09522   81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINAHF-NGMVMAV 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1189717604 158 SHVSLPVHGVQFHPESITSQHGHKILKNFLELAQ 191
Cdd:PRK09522  158 RHDADRVCGFQFHPESILTTQGARLLEQTLAWAQ 191
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 6-198 8.49e-45

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 158.47  E-value: 8.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   6 LIDNYDSFTFNLvhyFGEL----GAQVTVHRNDKISVEEVM-----AGSPDAIVLSPGPCTPHEA---GVCLDLIaRACD 73
Cdd:PLN02889   86 LIDNYDSYTYNI---YQELsivnGVPPVVVRNDEWTWEEVYhylyeEKAFDNIVISPGPGSPTCPadiGICLRLL-LECR 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  74 KIPIFGVCLGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGI-DGP---FQATRYHSLVVKAETLPASLHVTATT 149
Cdd:PLN02889  162 DIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIpSGRnsgFKVVRYHSLVIDAESLPKELVPIAWT 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604 150 -----------------PDG------------------------------------LIMALSHVSLPVHGVQFHPESITS 176
Cdd:PLN02889  242 sssdtlsflesqksglvPDAyesqigqsgssdpfssklkngtswpsshsermqngkILMGIMHSTRPHYGLQFHPESIAT 321

                         250       260
                  ....*....|....*....|...
gi 1189717604 177 QHGHKILKNFLELAQ-VWNDSRP 198
Cdd:PLN02889  322 CYGRQIFKNFREITQdYWLRLRS 344
PRK06895 PRK06895
anthranilate synthase component II;
1-189 8.92e-45

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 147.19  E-value: 8.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   1 MAKVTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKISVEEVMAGSpdAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGV 80
Cdd:PRK06895    1 ATKLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  81 CLGHQAIGEAFGGEVVRAPLPIHGKMAT-ILHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSH 159
Cdd:PRK06895   79 CLGHQTLCEFFGGELYNLNNVRHGQQRPlKVRSNSPLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQH 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1189717604 160 VSLPVHGVQFHPESITSQHGHKILKNFLEL 189
Cdd:PRK06895  159 KTLPIYGVQFHPESYISEFGEQILRNWLAI 188
TrpE-clade3 TIGR01815
anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of ...
 3-179 4.50e-43

anthranilate synthase, alpha proteobacterial clade; This model represents a small clade of anthranilate synthases from alpha proteobacteria and Nostoc (a cyanobacterium). This enzyme is the first step in the pathway for the biosynthesis of tryprophan from chorismate. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130874 [Multi-domain]  Cd Length: 717  Bit Score: 153.12  E-value: 4.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLIDNYDSFTFNLVHYFGELGAQVTVHRNDkiSVEEVMAG-SPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVC 81
Cdd:TIGR01815 518 RILLVDHEDSFVHTLANYLRQTGASVTTLRHS--HAEAAFDErRPDLVVLSPGPGRPADFDVAGTIDAALARGLPVFGVC 595

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  82 LGHQAIGEAFGGEVVRAPLPIHGKMATI-LHSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHV 160
Cdd:TIGR01815 596 LGLQGMVEAFGGALDVLPEPVHGKASRIrVLGPDALFAGLPERLTVGRYHSLFARRDRLPAELTVTAESADGLIMAIEHR 675

                         170
                  ....*....|....*....
gi 1189717604 161 SLPVHGVQFHPESITSQHG 179
Cdd:TIGR01815 676 RLPLAAVQFHPESIMTLDG 694
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 1-183 1.12e-35

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 124.57  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   1 MAKVTLIDNYDSFTFNLVHYFGELGAQVTVHRNdKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGV 80
Cdd:PRK05637    1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  81 CLGHQAIGEAFGGEvVRAPLPIHGK--MATILHSGET--IFRGI------DGP------FQATRYHSLvvKAETLPASLH 144
Cdd:PRK05637   80 CLGFQALLEHHGGK-VEPCGPVHGTtdNMILTDAGVQspVFAGLatdvepDHPeipgrkVPIARYHSL--GCVVAPDGME 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1189717604 145 VTATTPDGL---IMALSHVSLPVHGVQFHPESITSQHGHKIL 183
Cdd:PRK05637  157 SLGTCSSEIgpvIMAAETTDGKAIGLQFHPESVLSPTGPIIL 198
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 4-202 3.28e-35

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: 130.80  E-value: 3.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFTFNLVHYF---GELGAQVTVHRNDKIS---VEEVMAGspDAIVLSPGPCTPHEA---GVCLDLIARA-CD 73
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQdqlLELLPLF--DAIVVGPGPGNPNNAqdmGIISELWELAnLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  74 KIPIFGVCLGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGpFQATRYHSLVVKAETlPASLHVTATTPDG- 152
Cdd:TIGR01823  86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEG-IDTLLPLCLTEDEe 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1189717604 153 --LIMALSHVSLPVHGVQFHPESITSQHGH-KILKNFLELAQVWNDSRPRGKK 202
Cdd:TIGR01823 164 giILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKLAFINNVKTGRWEK 216
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 23-187 3.95e-30

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: 109.16  E-value: 3.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  23 ELGAQVTVHRNDkISVEEVMAGSPDAIVLSPGPCTPHEAG---VCLDLIARacdKIPIFGVCLGHQAIGEAFGGEVVRAP 99
Cdd:cd01742    20 ELGVYSEILPNT-TPLEEIKLKNPKGIILSGGPSSVYEEDaprVDPEIFEL---GVPVLGICYGMQLIAKALGGKVERGD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604 100 LPIHGK-MATILHSGEtIFRGIDGPFQATRYHSLVVkaETLPASLHVTATTPDGLIMALSHVSLPVHGVQFHPESITSQH 178
Cdd:cd01742    96 KREYGKaEIEIDDSSP-LFEGLPDEQTVWMSHGDEV--VKLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEK 172


                  ....*....
gi 1189717604 179 GHKILKNFL 187
Cdd:cd01742   173 GKEILKNFL 181
PRK00758 PRK00758
GMP synthase subunit A; Validated
 3-191 4.44e-30

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 109.17  E-value: 4.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLIDNYDSFTFNLVHYFGELGAQVTVHRNDKiSVEEVMAGsPDAIVLSPGPcTPHEAGVCLDLIARAcdKIPIFGVCL 82
Cdd:PRK00758    1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTT-PVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  83 GHQAIGEAFGGEVVRAPLPIHGKM-ATILHSgETIFRGIDGPFQATRYHSLVVKaeTLPASLHVTATTPDGLIMALSHVS 161
Cdd:PRK00758   76 GHQLIAKAFGGEVGRGEYGEYALVeVEILDE-DDILKGLPPEIRVWASHADEVK--ELPDGFEILARSDICEVEAMKHKE 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1189717604 162 LPVHGVQFHPESITSQHGHKILKNFLELAQ 191
Cdd:PRK00758  153 KPIYGVQFHPEVAHTEYGEEIFKNFLEICG 182
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 23-188 6.97e-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: 103.55  E-value: 6.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  23 ELGAQVTVHRNDkISVEEVMAGSPDAIVLSPGPCTPHEAGvCLDLIARACD-KIPIFGVCLGHQAIGEAFGGEVVRAPLP 101
Cdd:TIGR00888  20 ELGVYSELVPNT-TPLEEIREKNPKGIILSGGPSSVYAEN-APRADEKIFElGVPVLGICYGMQLMAKQLGGEVGRAEKR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604 102 IHGKMAT-ILHSGEtIFRGIDGPFQATRYHSLVVKAetLPASLHVTATTPDGLIMALSHVSLPVHGVQFHPESITSQHGH 180
Cdd:TIGR00888  98 EYGKAELeILDEDD-LFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDNCPVAAMAHEEKPIYGVQFHPEVTHTEYGN 174


                  ....*...
gi 1189717604 181 KILKNFLE 188
Cdd:TIGR00888 175 ELLENFVY 182
guaA PRK00074
GMP synthase; Reviewed
 23-187 2.47e-27

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 107.83  E-value: 2.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  23 ELGAQVTVHRNDkISVEEVMAGSPDAIVLSPGPCTPHEAGvcldliARACDK------IPIFGVCLGHQAIGEAFGGEVV 96
Cdd:PRK00074   25 ELGVYSEIVPYD-ISAEEIRAFNPKGIILSGGPASVYEEG------APRADPeifelgVPVLGICYGMQLMAHQLGGKVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  97 RAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVkaETLPASLHVTATTPDGLIMALSHVSLPVHGVQFHPESITS 176
Cdd:PRK00074   98 RAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKV--TELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHT 175

                         170
                  ....*....|.
gi 1189717604 177 QHGHKILKNFL 187
Cdd:PRK00074  176 PQGKKLLENFV 186
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 3-190 3.06e-24

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: 95.01  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLIDNYDSFTF---NLVHYFGELGAQVTVHR--NDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCL----DLIARACD 73
Cdd:COG0518     1 KILILDHDPFGGQypgLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLedepALIREAFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  74 -KIPIFGVCLGHQAIGEAFGGEVVRAPLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVkaETLPASLHVTATTPDG 152
Cdd:COG0518    81 lGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTV--TELPEGAEVLASSDNC 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189717604 153 LIMALSHvSLPVHGVQFHPE------------------------------SITSQHGHKILKNFLELA 190
Cdd:COG0518   159 PNQAFRY-GRRVYGVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLREI 225
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 16-173 1.55e-23

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: 92.17  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  16 NLVHYFGELGAQVTVHRNDKiSVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDK-IPIFGVCLGHQAIGEAFGGE 94
Cdd:cd01744    11 NILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGAK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  95 VVRaplpihgkmatiLHSGEtifRGIDGP---------FQATRYHSLVVKAETLPASLHVTATTP-DGLIMALSHVSLPV 164
Cdd:cd01744    90 TYK------------MKFGH---RGSNHPvkdlitgrvYITSQNHGYAVDPDSLPGGLEVTHVNLnDGTVEGIRHKDLPV 154


                  ....*....
gi 1189717604 165 HGVQFHPES 173
Cdd:cd01744   155 FSVQFHPEA 163
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 25-172 2.30e-21

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 89.95  E-value: 2.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  25 GAQVTVHRNDKiSVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQAIGEAFGGEVVRaplpihg 104
Cdd:PRK12838  189 GCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEK------- 260

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189717604 105 kmatiLHSGetiFRGIDGP---------FQATRYHSLVVKAETLPAS-LHVTATT-PDGLIMALSHVSLPVHGVQFHPE 172
Cdd:PRK12838  261 -----LPFG---HRGANHPvidlttgrvWMTSQNHGYVVDEDSLDGTpLSVRFFNvNDGSIEGLRHKKKPVLSVQFHPE 331
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
23-173 4.57e-19

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 83.59  E-value: 4.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  23 ELGAQVTV--HrndKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACD-KIPIFGVCLGHQAIGEAFGGEVVrap 99
Cdd:PRK12564  197 ERGCRVTVvpA---TTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEkKIPIFGICLGHQLLALALGAKTY--- 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604 100 lpihgKMatilHSGEtifRGIDGPFQATRY---------HSLVVKAETLPASLHVTATTP-DGLIMALSHVSLPVHGVQF 169
Cdd:PRK12564  271 -----KM----KFGH---RGANHPVKDLETgkveitsqnHGFAVDEDSLPANLEVTHVNLnDGTVEGLRHKDLPAFSVQY 338


                  ....
gi 1189717604 170 HPES 173
Cdd:PRK12564  339 HPEA 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 16-173 2.03e-18

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: 81.61  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  16 NLVHYFGELGAQVTVHRNDkISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDK-IPIFGVCLGHQAIGEAFGGE 94
Cdd:COG0505   189 NILRELAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAK 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  95 VVraplpihgKMatilHSGetiFRGIDGPFQ--ATR--Y-----HSLVVKAETLPAS-LHVTATTP-DGLIMALSHVSLP 163
Cdd:COG0505   268 TY--------KL----KFG---HRGANHPVKdlETGrvEitsqnHGFAVDEDSLPATdLEVTHVNLnDGTVEGLRHKDLP 332

                         170
                  ....*....|
gi 1189717604 164 VHGVQFHPES 173
Cdd:COG0505   333 AFSVQYHPEA 342
PLN02347 PLN02347
GMP synthetase
 37-187 1.17e-16

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 77.42  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  37 SVEEVMAGSPDAIVLSPGPCTPHEAGV------CLDLIARAcdKIPIFGVCLGHQAIGEAFGGEVVRAPLPIHGKMATIL 110
Cdd:PLN02347   45 SLDRIASLNPRVVILSGGPHSVHVEGAptvpegFFDYCRER--GVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRV 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189717604 111 HSGETIFRGIDGPFQATRYHSLVVKAETLPASLHVTATTPDGLIMALSHVSLPVHGVQFHPESITSQHGHKILKNFL 187
Cdd:PLN02347  123 VCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 15-190 3.08e-15

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 72.91  E-value: 3.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  15 FNLVHYFGELGAQVTVhRNDKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACD-KIPIFGVCLGHQAIGEAFGG 93
Cdd:CHL00197  204 YNILRRLKSFGCSITV-VPATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  94 EVVRaplpihgkmatiLHSGEtifRGIDGPFQ-------ATRYHSLVVKAETLpASLHVTAT---TPDGLIMALSHVSLP 163
Cdd:CHL00197  283 KTFK------------LKFGH---RGLNHPSGlnqqveiTSQNHGFAVNLESL-AKNKFYIThfnLNDGTVAGISHSPKP 346

                         170       180
                  ....*....|....*....|....*...
gi 1189717604 164 VHGVQFHPESITSQHGHKIL-KNFLELA 190
Cdd:CHL00197  347 YFSVQYHPEASPGPHDADYLfEYFIEII 374
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 16-178 1.38e-13

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 68.47  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  16 NLVHYFGELGAQVTVHRNdKISVEEVMAGSPDAIVLSPGPCTPHEAGVCLDLIARACDKIPIFGVCLGHQAIGEAFGGEV 95
Cdd:PLN02771  253 NILRRLASYGCKITVVPS-TWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKT 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  96 VRAPLPIHG---KMATILHSGETIfrgidgpfqATRYHSLVVKAETLPASLHVT-ATTPDGLIMALSHVSLPVHGVQFHP 171
Cdd:PLN02771  332 FKMKFGHHGgnhPVRNNRTGRVEI---------SAQNHNYAVDPASLPEGVEVThVNLNDGSCAGLAFPALNVMSLQYHP 402


                  ....*..
gi 1189717604 172 ESITSQH 178
Cdd:PLN02771  403 EASPGPH 409
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 65-187 3.45e-12

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: 62.26  E-value: 3.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  65 LDLIARACD-KIPIFGVCLGHQAIGEAFGGEVVRAPLPIHGKMATI-LHSGET---IFRGIDGPFQATRYHSLVVkaETL 139
Cdd:cd01741    71 KELIRQALAaGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVtLTEAGKadpLFAGLPDEFPVFHWHGDTV--VEL 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1189717604 140 PASLHVTATTPDGLIMALShVSLPVHGVQFHPEsitsqhgHKILKNFL 187
Cdd:cd01741   149 PPGAVLLASSEACPNQAFR-YGDRALGLQFHPE-------ERLLRNFL 188
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 67-172 2.10e-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: 60.28  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  67 LIARACD-KIPIFGVCLGHQAIGEAFGGevvraplpihgkmatilhsgeTIFRGIdgpfQATRYHSLVVKAetLPASLHV 145
Cdd:cd01745    92 LLRAALErGKPILGICRGMQLLNVALGG---------------------TLYQDI----RVNSLHHQAIKR--LADGLRV 144

                          90       100
                  ....*....|....*....|....*...
gi 1189717604 146 TATTPDGLIMALSHVSLP-VHGVQFHPE 172
Cdd:cd01745   145 EARAPDGVIEAIESPDRPfVLGVQWHPE 172
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 65-193 3.17e-11

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: 60.18  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  65 LDLIARACD-KIPIFGVCLGHQAIGEAFGG-----------------EVVRAPLPIH-------GKMATILhsGETifrg 119
Cdd:COG2071    86 LALIRAALErGKPVLGICRGMQLLNVALGGtlyqdlpdqvpgaldhrQPAPRYAPRHtveiepgSRLARIL--GEE---- 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189717604 120 idgPFQATRYHSLVVKaeTLPASLHVTATTPDGLIMALSHVSLP-VHGVQFHPESITSQHGH--KILKNFLELAQVW 193
Cdd:COG2071   160 ---EIRVNSLHHQAVK--RLGPGLRVSARAPDGVIEAIESPGAPfVLGVQWHPEWLAASDPLsrRLFEAFVEAARAR 231
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-87 1.08e-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: 56.84  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFT---FNLVHYFGELGAQVTVHRNDKISVE-EVMAGSPDAIVLSPGPCTPHEAGVC---LDLIARACD-KI 75
Cdd:cd01653     1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLARDealLALLREAAAaGK 80

                          90
                  ....*....|..
gi 1189717604  76 PIFGVCLGHQAI 87
Cdd:cd01653    81 PILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-87 1.48e-10

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 55.67  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   4 VTLIDNYDSFT---FNLVHYFGELGAQVTVHRNDKISVE-EVMAGSPDAIVLSPGPCTPHEAGVC---LDLIARACD-KI 75
Cdd:cd03128     1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDLAWDealLALLREAAAaGK 80

                          90
                  ....*....|..
gi 1189717604  76 PIFGVCLGHQAI 87
Cdd:cd03128    81 PVLGICLGAQLL 92
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 67-172 2.75e-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: 57.65  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  67 LIARACD-KIPIFGVCLGHQAIGEAFGGEVVRAplpIHGKMATILHSgETIFRGIDGPFQA------TRYHSLVVKAETL 139
Cdd:pfam07722  97 LIRAALArGKPILGICRGFQLLNVALGGTLYQD---IQEQPGFTDHR-EHCQVAPYAPSHAvnvepgSLLASLLGSEEFR 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1189717604 140 PASLH------------VTATTPDGLIMALSHVSLP--VHGVQFHPE 172
Cdd:pfam07722 173 VNSLHhqaidrlapglrVEAVAPDGTIEAIESPNAKgfALGVQWHPE 219
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 35-189 4.75e-10

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 56.80  E-value: 4.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  35 KISVEEVMAGSPDAIVLsPGPCTPHEAGVCL----DLIARACDK-IPIFGVCLGHQAIGEA------------FGGEVVR 97
Cdd:PRK13143   28 VITSDPEEILDADGIVL-PGVGAFGAAMENLsplrDVILEAARSgKPFLGICLGMQLLFESseegggvrglglFPGRVVR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  98 aplpIHGKMaTILHSG---------ETIFRGIDGPFQatrY--HSLVVKaetlPASLHVTATTPD-GLIMALSHVSLPVH 165
Cdd:PRK13143  107 ----FPAGV-KVPHMGwntvkvvkdCPLFEGIDGEYV---YfvHSYYAY----PDDEDYVVATTDyGIEFPAAVCNDNVF 174

                         170       180
                  ....*....|....*....|....
gi 1189717604 166 GVQFHPESiTSQHGHKILKNFLEL 189
Cdd:PRK13143  175 GTQFHPEK-SGETGLKILENFVEL 197
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 24-189 1.21e-08

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: 52.71  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  24 LGAQVTVHRNDKIsveevmAGSPDAIVLsPGPCTPHEA-------GVCLDLIARACDKIPIFGVCLGHQAIGEA------ 90
Cdd:TIGR01855  21 VGAEPVVVKDSKE------AELADKLIL-PGVGAFGAAmarlrenGLDLFVELVVRLGKPVLGICLGMQLLFERseeggg 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  91 ------FGGEVVR---APLPIHGKMATILHSGETIFRGIDGPFQATRYHSLVVKaetlPASLHVTATTPDGlIMALSHVS 161
Cdd:TIGR01855  94 vpglglIKGNVVKleaRKVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAV----CEEEAVLAYADYG-EKFPAAVQ 168

                         170       180       190
                  ....*....|....*....|....*....|
gi 1189717604 162 LP-VHGVQFHPESitSQH-GHKILKNFLEL 189
Cdd:TIGR01855 169 KGnIFGTQFHPEK--SGKtGLKLLENFLEL 196
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 73-189 5.79e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 47.94  E-value: 5.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  73 DKIPIFGVCLGHQAIGEA-----------FGGEVVR---APLPI-HGKMATILHSGE-TIFRGI-DGPFqatRY--HSLV 133
Cdd:PRK13181   71 KKQPVLGICLGMQLLFESseegnvkglglIPGDVKRfrsEPLKVpQMGWNSVKPLKEsPLFKGIeEGSY---FYfvHSYY 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189717604 134 VKAEtlpASLHVTATTPDGLIMALSHVSLPVHGVQFHPESiTSQHGHKILKNFLEL 189
Cdd:PRK13181  148 VPCE---DPEDVLATTEYGVPFCSAVAKDNIYAVQFHPEK-SGKAGLKLLKNFAEL 199
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-189 1.40e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 46.77  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604   3 KVTLID----NYDSFTFNlvhyFGELGAQVTVHRN-DKISveevmagSPDAIVLsPGPCTPHEAGVCL---DLIA--RAC 72
Cdd:PRK13170    2 NVVIIDtgcaNLSSVKFA----IERLGYEPVVSRDpDVIL-------AADKLFL-PGVGTAQAAMDQLrerELIDliKAC 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  73 DKiPIFGVCLGHQAIGEA------------FGGEVVRA-----PLPiHGKMATILHS-GETIFRGIDgpfqATRY----H 130
Cdd:PRK13170   70 TQ-PVLGICLGMQLLGERseesggvdclgiIDGPVKKMtdfglPLP-HMGWNQVTPQaGHPLFQGIE----DGSYfyfvH 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189717604 131 SLVVkaetlPASLHVTATTPDGliMALSHVslpVH-----GVQFHPESiTSQHGHKILKNFLEL 189
Cdd:PRK13170  144 SYAM-----PVNEYTIAQCNYG--EPFSAA---IQkdnffGVQFHPER-SGAAGAQLLKNFLEM 196
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 24-193 1.70e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 46.66  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  24 LGAQVTVHRNdkisVEEVMAGspDAIVLsPG-----PCTPH--EAGVCLDLIARACDKIPIFGVCLGHQAI---GEAFG- 92
Cdd:PRK13141   22 LGAEAVITSD----PEEILAA--DGVIL-PGvgafpDAMANlrERGLDEVIKEAVASGKPLLGICLGMQLLfesSEEFGe 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  93 --------GEVVRapLPIHGKMaTILHSG---------ETIFRGI-DGPFQatrY--HSLVVKAEtlPASlHVTATTPDG 152
Cdd:PRK13141   95 teglgllpGRVRR--FPPEEGL-KVPHMGwnqlelkkeSPLLKGIpDGAYV---YfvHSYYADPC--DEE-YVAATTDYG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1189717604 153 limalshVSLP-------VHGVQFHPESitSQH-GHKILKNFLELAQVW 193
Cdd:PRK13141  166 -------VEFPaavgkdnVFGAQFHPEK--SGDvGLKILKNFVEMVEEC 205
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 24-187 2.03e-06

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


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 46.34  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  24 LGAQVTVHRNDkisvEEVMagSPDAIVLsPG-----PCTPH--EAGVCLDLIARACDKIPIFGVCLGHQAIGEA------ 90
Cdd:cd01748    21 LGAEVIITSDP----EEIL--SADKLIL-PGvgafgDAMANlrERGLIEALKEAIASGKPFLGICLGMQLLFESseeggg 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  91 ------FGGEVVRAPLPIHGKM-------ATILHSGETIFRGIDGPFQatrY--HSLVVkaeTLPASLHVTATTPDGLIM 155
Cdd:cd01748    94 tkglglIPGKVVRFPASEGLKVphmgwnqLEITKESPLFKGIPDGSYF---YfvHSYYA---PPDDPDYILATTDYGGKF 167

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1189717604 156 ALSHVSLPVHGVQFHPE-SitSQHGHKILKNFL 187
Cdd:cd01748   168 PAAVEKDNIFGTQFHPEkS--GKAGLKLLKNFL 198
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 47-178 3.33e-06

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 46.43  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  47 DAIVL--SPGPCTPHEAG--------------VCLDLIARACDK-IPIFGVCLGHQAIGEAFGGEVVR------------ 97
Cdd:PRK11366   63 DGIYLpgSPSNVQPHLYGengdepdadpgrdlLSMALINAALERrIPIFAICRGLQELVVATGGSLHRklceqpellehr 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  98 --APLPIHGKMA----TILHSGETIFRGIDG--PFQATRYHSLvvKAETLPASLHVTATTPDGLIMALSHVSLP-VHGVQ 168
Cdd:PRK11366  143 edPELPVEQQYApsheVQVEEGGLLSALLPEcsNFWVNSLHGQ--GAKVVSPRLRVEARSPDGLVEAVSVINHPfALGVQ 220

                         170
                  ....*....|
gi 1189717604 169 FHPESITSQH 178
Cdd:PRK11366  221 WHPEWNSSEY 230
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 73-172 2.61e-05

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 43.41  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  73 DKIPIFGVCLGHQAIGEAFGGEVVRAPLPIH-GKMATILH---SGETIFRGIDGPFQATRYHSLVVKaeTLPASLHVTAT 148
Cdd:PRK09065   87 AGMPLLGICYGHQLLAHALGGEVGYNPAGREsGTVTVELHpaaADDPLFAGLPAQFPAHLTHLQSVL--RLPPGAVVLAR 164

                          90       100
                  ....*....|....*....|....*.
gi 1189717604 149 TP-DGL-IMALSHVSLpvhGVQFHPE 172
Cdd:PRK09065  165 SAqDPHqAFRYGPHAW---GVQFHPE 187
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 74-189 5.30e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 42.52  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189717604  74 KIPIFGVCLGHQAI---GEAFG---------GEVVRAPLPIHGKmatILHSG---------ETIFRGIDGPFQATRYHSL 132
Cdd:PRK13152   73 KKPILGICLGMQLFlerGYEGGvceglgfieGEVVKFEEDLNLK---IPHMGwneleilkqSPLYQGIPEKSDFYFVHSF 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189717604 133 VVKAEtlpaSLHVTATTPDGLIMALSHVSLPVHGVQFHPESitSQH-GHKILKNFLEL 189
Cdd:PRK13152  150 YVKCK----DEFVSAKAQYGHKFVASLQKDNIFATQFHPEK--SQNlGLKLLENFARL 201
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 67-99 2.38e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 37.64  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1189717604  67 LIARA--CDKIpIFGVCLGHQAIGEAFGGEVVRAP 99
Cdd:PRK08250   76 LINQAikAGKA-VIGVCLGAQLIGEALGAKYEHSP 109
 
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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