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Conserved domains on  [gi|612157112|gb|AHW86601|]
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para-aminobenzoate synthase component II [Klebsiella michiganensis HKOPL1]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 1-187 2.20e-135

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.


The actual alignment was detected with superfamily member PRK08007:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 187  Bit Score: 375.79  E-value: 2.20e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVF 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 612157112 161 DLEGVQFHPESILSEQGHQLLANFLNR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 2.20e-135

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 375.79  E-value: 2.20e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVF 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 612157112 161 DLEGVQFHPESILSEQGHQLLANFLNR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-186 1.09e-134

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: 373.99  E-value: 1.09e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  82 HQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVFD 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*
gi 612157112 162 LEGVQFHPESILSEQGHQLLANFLN 186
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLE 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 4.06e-110

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: 311.78  E-value: 4.06e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  82 HQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVFD 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 612157112 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 3.75e-109

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: 309.80  E-value: 3.75e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112    1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEG-EIMGIRHRV 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 612157112  160 FDLEGVQFHPESILSEQGHQLLANFLNR 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 5.64e-73

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 218.26  E-value: 5.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112    3 LLIDNYDSFTWNLYQYFCELGAEVLVRRNDElTLADIISLAPAKIVISPGPCTPDESGISLAAIRH-FSGQTPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   82 HQAIAQVFGAAIVRA-AKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGE-IMGIRHRV 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 612157112  160 FDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-185 2.18e-66

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 201.41  E-value: 2.18e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   5 IDNYDSFTWNLYQYFCE--LGAEVLVRRNDElTLADIISLAPAKIVISPGPCTPD---ESGISLAAIRHFSGQTPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  80 LGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLidPLTLPECFEVTARSE-EGE--IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDhDGEelVMGIR 158

                        170       180
                 ....*....|....*....|....*....
gi 612157112 157 HRVFDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFL 187
 
Name Accession Description Interval E-value
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
1-187 2.20e-135

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 375.79  E-value: 2.20e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK08007   1 MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVF 160
Cdd:PRK08007  81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETREIMGIRHRQW 160

                        170       180
                 ....*....|....*....|....*..
gi 612157112 161 DLEGVQFHPESILSEQGHQLLANFLNR 187
Cdd:PRK08007 161 DLEGVQFHPESILSEQGHQLLANFLHR 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-186 1.09e-134

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: 373.99  E-value: 1.09e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLG 81
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  82 HQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVFD 161
Cdd:COG0512   81 HQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTEDGEIMGIRHRELP 160

                        170       180
                 ....*....|....*....|....*
gi 612157112 162 LEGVQFHPESILSEQGHQLLANFLN 186
Cdd:COG0512  161 IEGVQFHPESILTEHGHQLLANFLE 185
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-186 1.13e-130

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 364.07  E-value: 1.13e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVF 160
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTDDGEIMGVRHKEL 160

                        170       180
                 ....*....|....*....|....*.
gi 612157112 161 DLEGVQFHPESILSEQGHQLLANFLN 186
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLLENFLE 186
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
1-185 7.23e-116

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 326.82  E-value: 7.23e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK06774   1 MLLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEG----EIMGIR 156
Cdd:PRK06774  81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGgemdEIMGIR 160

                        170       180
                 ....*....|....*....|....*....
gi 612157112 157 HRVFDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK06774 161 HRTLPLEGVQFHPESILSEQGHQLLDNFL 189
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
1-187 1.42e-111

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 316.05  E-value: 1.42e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK08857   1 MLLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSE--EG---EIMGI 155
Cdd:PRK08857  81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTEleDGsmdEIMGF 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 612157112 156 RHRVFDLEGVQFHPESILSEQGHQLLANFLNR 187
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFLAR 192
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-185 4.06e-110

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: 311.78  E-value: 4.06e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLG 81
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  82 HQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVFD 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLP 160

                        170       180
                 ....*....|....*....|....
gi 612157112 162 LEGVQFHPESILSEQGHQLLANFL 185
Cdd:cd01743  161 IYGVQFHPESILTEYGLRLLENFL 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 1-187 3.75e-109

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: 309.80  E-value: 3.75e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112    1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEG-EIMGIRHRV 159
Cdd:TIGR00566  81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENiEIMAIRHRD 160

                         170       180
                  ....*....|....*....|....*...
gi 612157112  160 FDLEGVQFHPESILSEQGHQLLANFLNR 187
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFLHR 188
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
1-186 2.01e-105

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 312.42  E-value: 2.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAE-VLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVC 79
Cdd:PRK14607   1 MIILIDNYDSFTYNIYQYIGELGPEeIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  80 LGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRV 159
Cdd:PRK14607  81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKE 160

                        170       180
                 ....*....|....*....|....*..
gi 612157112 160 FDLEGVQFHPESILSEQGHQLLANFLN 186
Cdd:PRK14607 161 HPIFGVQFHPESILTEEGKRILKNFLN 187
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
1-186 1.82e-104

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 298.26  E-value: 1.82e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK07649   1 MILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVF 160
Cdd:PRK07649  81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTL 160

                        170       180
                 ....*....|....*....|....*.
gi 612157112 161 DLEGVQFHPESILSEQGHQLLANFLN 186
Cdd:PRK07649 161 PIEGVQFHPESIMTSHGKELLQNFIR 186
trpG CHL00101
anthranilate synthase component 2
 1-186 3.39e-89

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 259.28  E-value: 3.39e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:CHL00101   1 MILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVF 160
Cdd:CHL00101  81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHKKY 160

                        170       180
                 ....*....|....*....|....*..
gi 612157112 161 D-LEGVQFHPESILSEQGHQLLANFLN 186
Cdd:CHL00101 161 KmLRGIQFHPESLLTTHGQQILRNFLS 187
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-185 1.42e-87

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 256.13  E-value: 1.42e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAP--AKIVISPGPCTPDESGISLAAIRHFSG-QTPILGV 78
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAqfDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  79 CLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHR 158
Cdd:PRK07765  83 CLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSGVIMAVRHR 162

                        170       180
                 ....*....|....*....|....*..
gi 612157112 159 VFDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK07765 163 ELPIHGVQFHPESVLTEGGHRMLANWL 189
PLN02335 PLN02335
anthranilate synthase
 2-186 5.85e-76

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 226.99  E-value: 5.85e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLG 81
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  82 HQAIAQVFGAAIVRAA-KVMHGKTSPVSHT---GQGVFLGLNNPLTVTRYHSLLIDPLTLPE-CFEVTARSEEGEIMGIR 156
Cdd:PLN02335 101 LQCIGEAFGGKIVRSPfGVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAWTEDGLIMAAR 180

                        170       180       190
                 ....*....|....*....|....*....|.
gi 612157112 157 HRVFD-LEGVQFHPESILSEQGHQLLANFLN 186
Cdd:PLN02335 181 HRKYKhIQGVQFHPESIITTEGKTIVRNFIK 211
GATase pfam00117
Glutamine amidotransferase class-I;
3-185 5.64e-73

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 218.26  E-value: 5.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112    3 LLIDNYDSFTWNLYQYFCELGAEVLVRRNDElTLADIISLAPAKIVISPGPCTPDESGISLAAIRH-FSGQTPILGVCLG 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAAGGAIEAIREaRELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   82 HQAIAQVFGAAIVRA-AKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGE-IMGIRHRV 159
Cdd:pfam00117  80 HQLLALAFGGKVVKAkKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGtIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*.
gi 612157112  160 FDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFF 185
Anth_synII_Halo NF041322
anthranilate synthase component II;
5-185 2.18e-66

anthranilate synthase component II;


Pssm-ID: 469219 [Multi-domain]  Cd Length: 190  Bit Score: 201.41  E-value: 2.18e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   5 IDNYDSFTWNLYQYFCE--LGAEVLVRRNDElTLADIISLAPAKIVISPGPCTPD---ESGISLAAIRHFSGQTPILGVC 79
Cdd:NF041322   2 VDNFDSFTYNLVEYVSEqrEHAETTVLKNTA-SLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLGVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  80 LGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLidPLTLPECFEVTARSE-EGE--IMGIR 156
Cdd:NF041322  81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLV--ATEVPDCFEVTATTDhDGEelVMGIR 158

                        170       180
                 ....*....|....*....|....*....
gi 612157112 157 HRVFDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFL 187
PRK13566 PRK13566
anthranilate synthase component I;
2-183 1.16e-49

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 170.48  E-value: 1.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDE-LTLADiiSLAPAKIVISPGPCTPDESGIS--LAAIRhfSGQTPILGV 78
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFaEEMLD--RVNPDLVVLSPGPGRPSDFDCKatIDAAL--ARNLPIFGV 604

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  79 CLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTG-QGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRH 157
Cdd:PRK13566 605 CLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGpGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTAETEDGVIMAIEH 684

                        170       180
                 ....*....|....*....|....*....
gi 612157112 158 RVFDLEGVQFHPESILS---EQGHQLLAN 183
Cdd:PRK13566 685 KTLPVAAVQFHPESIMTlggDVGLRIIEN 713
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 2-186 4.40e-47

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 160.96  E-value: 4.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRND---ELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGV 78
Cdd:PRK09522   4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  79 CLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDplTLPECFEVTArSEEGEIMGIRHR 158
Cdd:PRK09522  84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGS--NIPAGLTINA-HFNGMVMAVRHD 160

                        170       180
                 ....*....|....*....|....*...
gi 612157112 159 VFDLEGVQFHPESILSEQGHQLLANFLN 186
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTLA 188
PRK06895 PRK06895
anthranilate synthase component II;
1-186 1.06e-37

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 128.32  E-value: 1.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLApaKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCL 80
Cdd:PRK06895   3 KLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDEVENFS--HILISPGPDVPRAYPQLFAMLERYHQHKSILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQG-VFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRV 159
Cdd:PRK06895  81 GHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKT 160

                        170       180
                 ....*....|....*....|....*..
gi 612157112 160 FDLEGVQFHPESILSEQGHQLLANFLN 186
Cdd:PRK06895 161 LPIYGVQFHPESYISEFGEQILRNWLA 187
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 3-184 1.00e-36

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 134.59  E-value: 1.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   3 LLIDNYDSFTWNLYQyfcEL----GAEVLVRRNDELTLADII-----SLAPAKIVISPGPCTP---DESGISLAAIRHfS 70
Cdd:PLN02889  85 LLIDNYDSYTYNIYQ---ELsivnGVPPVVVRNDEWTWEEVYhylyeEKAFDNIVISPGPGSPtcpADIGICLRLLLE-C 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  71 GQTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVF----LGLNNPLTVTRYHSLLIDPLTLPE------- 139
Cdd:PLN02889 161 RDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKelvpiaw 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112 140 ---------------------------------------------CFEVTARSEEGEI-MGIRHRVFDLEGVQFHPESIL 173
Cdd:PLN02889 241 tsssdtlsflesqksglvpdayesqigqsgssdpfssklkngtswPSSHSERMQNGKIlMGIMHSTRPHYGLQFHPESIA 320

                        250
                 ....*....|.
gi 612157112 174 SEQGHQLLANF 184
Cdd:PLN02889 321 TCYGRQIFKNF 331
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 2-185 7.70e-30

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: 108.17  E-value: 7.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112    2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNDElTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLG 81
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTT-PLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   82 HQAIAQVFGAAIVRAAKVMHGKTSpVSHTGQGV-FLGLNNPLTVTRYHSlliDPLT-LPECFEVTARSEEGEIMGIRHRV 159
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGKAE-LEILDEDDlFRGLPDESTVWMSHG---DKVKeLPEGFKVLATSDNCPVAAMAHEE 155

                         170       180
                  ....*....|....*....|....*.
gi 612157112  160 FDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:TIGR00888 156 KPIYGVQFHPEVTHTEYGNELLENFV 181
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 21-185 6.11e-29

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: 105.70  E-value: 6.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  21 ELGAEVLVRRNDElTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLGHQAIAQVFGAAIVRAAKVM 100
Cdd:cd01742   20 ELGVYSEILPNTT-PLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKRE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112 101 HGKTSPVSHTGQGVFLGLNNPLTVTRYHSlliDPLT-LPECFEVTARSEEGEIMGIRHRVFDLEGVQFHPESILSEQGHQ 179
Cdd:cd01742   99 YGKAEIEIDDSSPLFEGLPDEQTVWMSHG---DEVVkLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKE 175


                 ....*.
gi 612157112 180 LLANFL 185
Cdd:cd01742  176 ILKNFL 181
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 2-177 8.65e-29

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 106.08  E-value: 8.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTWNLYQYFCELGAEVLVRRNdELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLG 81
Cdd:PRK05637   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  82 HQAIAQVFGAAiVRAAKVMHGKTSPVSHTGQG----VFLGL------NNP------LTVTRYHSLliDPLTLPECFEV-- 143
Cdd:PRK05637  83 FQALLEHHGGK-VEPCGPVHGTTDNMILTDAGvqspVFAGLatdvepDHPeipgrkVPIARYHSL--GCVVAPDGMESlg 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 612157112 144 TARSEEGE-IMGIRHRVFDLEGVQFHPESILSEQG 177
Cdd:PRK05637 160 TCSSEIGPvIMAAETTDGKAIGLQFHPESVLSPTG 194
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 2-186 8.02e-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: 106.14  E-value: 8.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112    2 ILLIDNYDSFTWNLYQYF---CELGAEVLVRRNDELT--LADIISLAPAkIVISPGPCTPD---ESGIsLAAIRHFSG-- 71
Cdd:TIGR01823   8 VLFIDSYDSFTYNVVRLLeqqTDISVHVTTVHSDTFQdqLLELLPLFDA-IVVGPGPGNPNnaqDMGI-ISELWELANld 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   72 QTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNpLTVTRYHSLLIDPLT----LPECfevTARS 147
Cdd:TIGR01823  86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGidtlLPLC---LTED 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 612157112  148 EEGEI-MGIRHRVFDLEGVQFHPESILSEQGH-QLLANFLN 186
Cdd:TIGR01823 162 EEGIIlMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLK 202
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-185 1.03e-25

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 97.23  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   1 MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDeLTLADIISLAPAkIVISPGPcTPDESGISLAAIRHFSgqTPILGVCL 80
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNT-TPVEEIKAFEDG-LILSGGP-DIERAGNCPEYLKELD--VPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVRAAKVMHGKT--SPVSHTGqgVFLGLNNPLTVTRYHSlliDPLT-LPECFEVTARSEEGEIMGIRH 157
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYALVevEILDEDD--ILKGLPPEIRVWASHA---DEVKeLPDGFEILARSDICEVEAMKH 150

                        170       180
                 ....*....|....*....|....*...
gi 612157112 158 RVFDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK00758 151 KEKPIYGVQFHPEVAHTEYGEEIFKNFL 178
guaA PRK00074
GMP synthase; Reviewed
 35-185 2.83e-22

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 92.80  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  35 TLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGV 114
Cdd:PRK00074  38 SAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPL 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612157112 115 FLGLNNPLTVTRYHSlliDPLT-LPECFEVTARSEEGEIMGIRHRVFDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PRK00074 118 FKGLPEEQDVWMSHG---DKVTeLPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFV 186
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 13-171 6.18e-22

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: 87.55  E-value: 6.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  13 WNLYQYFCELGAEVLVRRNDeLTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQT-PILGVCLGHQAIAQVFGA 91
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYN-TDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKiPIFGICLGHQLLALALGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  92 AIVRaakvM----HGKTSPVSH--TGQgVFLGLNNpltvtryHSLLIDPLTLPECFEVTARS-EEGEIMGIRHRVFDLEG 164
Cdd:cd01744   89 KTYK----MkfghRGSNHPVKDliTGR-VYITSQN-------HGYAVDPDSLPGGLEVTHVNlNDGTVEGIRHKDLPVFS 156


                 ....*..
gi 612157112 165 VQFHPES 171
Cdd:cd01744  157 VQFHPEA 163
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-170 2.84e-20

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: 84.23  E-value: 2.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLID---NYDSFTWNLYQYFCELGAEVLVRR--NDELTLADIISLAPAKIVISPGPCTPDESGISL----AAIRH-FSG 71
Cdd:COG0518    2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLedepALIREaFEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  72 QTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTsPVSHTGQ-GVFLGLNNPLTVTRYHSLLIDplTLPECFEVTARSEEG 150
Cdd:COG0518   82 GKPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVELTEAdPLFAGLPDEFTVWMSHGDTVT--ELPEGAEVLASSDNC 158

                        170       180
                 ....*....|....*....|..
gi 612157112 151 EIMGIRH--RVFdleGVQFHPE 170
Cdd:COG0518  159 PNQAFRYgrRVY---GVQFHPE 177
PLN02347 PLN02347
GMP synthetase
 36-185 1.38e-18

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 82.42  E-value: 1.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  36 LADIISLAPAKIVISPGPCTPDESGISLAAIRHF----SGQTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTG 111
Cdd:PLN02347  46 LDRIASLNPRVVILSGGPHSVHVEGAPTVPEGFFdycrERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612157112 112 QGVFLGLNNPLTVTRYHSLLIDPLTLPECFEVTARSEEGEIMGIRHRVFDLEGVQFHPESILSEQGHQLLANFL 185
Cdd:PLN02347 126 SQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 35-170 1.83e-16

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 75.70  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  35 TLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPV--SHTGQ 112
Cdd:PRK12838 200 SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVidLTTGR 279

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112 113 gVFLGLNNpltvtryHSLLIDPLTLPEC-FEVTARS-EEGEIMGIRHRVFDLEGVQFHPE 170
Cdd:PRK12838 280 -VWMTSQN-------HGYVVDEDSLDGTpLSVRFFNvNDGSIEGLRHKKKPVLSVQFHPE 331
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-185 1.31e-13

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: 65.73  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  63 LAAIRH-FSGQTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQG----VFLGLNNPLTVTRYHSlliD-PLT 136
Cdd:cd01741   71 KELIRQaLAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGkadpLFAGLPDEFPVFHWHG---DtVVE 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612157112 137 LPECFEVTARSEEGEIMGIR--HRVFdleGVQFHPEsilseqgHQLLANFL 185
Cdd:cd01741  148 LPPGAVLLASSEACPNQAFRygDRAL---GLQFHPE-------ERLLRNFL 188
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 37-171 3.49e-13

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 66.54  E-value: 3.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  37 ADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQG-VF 115
Cdd:PLN02771 275 SEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGrVE 354

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 612157112 116 LGLNNpltvtryHSLLIDPLTLPECFEVT-ARSEEGEIMGIRHRVFDLEGVQFHPES 171
Cdd:PLN02771 355 ISAQN-------HNYAVDPASLPEGVEVThVNLNDGSCAGLAFPALNVMSLQYHPEA 404
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
35-171 3.24e-12

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 63.56  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  35 TLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQT-PILGVCLGHQAIAQVFGAAIVRaakvM----HGKTSPVSH 109
Cdd:PRK12564 210 TAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKKiPIFGICLGHQLLALALGAKTYK----MkfghRGANHPVKD 285

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612157112 110 --TGQGVFLGLNnpltvtryHSLLIDPLTLPECFEVTARS-EEGEIMGIRHRVFDLEGVQFHPES 171
Cdd:PRK12564 286 leTGKVEITSQN--------HGFAVDEDSLPANLEVTHVNlNDGTVEGLRHKDLPAFSVQYHPEA 342
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 35-171 4.92e-12

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: 63.12  E-value: 4.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  35 TLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQ-TPILGVCLGHQAIAQVFGAAIVRaakvM----HG------- 102
Cdd:COG0505  209 SAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYK----LkfghRGanhpvkd 284

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612157112 103 -KTSPVSHTGQgvflglNnpltvtryHSLLIDPLTLPE-CFEVTARS-EEGEIMGIRHRVFDLEGVQFHPES 171
Cdd:COG0505  285 lETGRVEITSQ------N--------HGFAVDEDSLPAtDLEVTHVNlNDGTVEGLRHKDLPAFSVQYHPEA 342
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-92 7.06e-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: 54.14  E-value: 7.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTW---NLYQYFCELGAEVLVRRNDELTLADIISLAPAK-IVISPGPCTPDESGIS---LAAIRHFSGQ-T 73
Cdd:cd01653    1 VAVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVESDVDLDDYDgLILPGGPGTPDDLARDealLALLREAAAAgK 80

                         90
                 ....*....|....*....
gi 612157112  74 PILGVCLGHQAIaqVFGAA 92
Cdd:cd01653   81 PILGICLGAQLL--VLGVQ 97
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 1.08e-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: 52.97  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNYDSFTW---NLYQYFCELGAEVLVRRNDELTLADIISLAPAK-IVISPGPCTPDESGIS---LAAIRHFSGQ-T 73
Cdd:cd03128    1 VAVLLFGGSEELelaSPLDALREAGAEVDVVSPDGGPVESDVDLDDYDgLILPGGPGTPDDLAWDealLALLREAAAAgK 80

                         90
                 ....*....|..
gi 612157112  74 PILGVCLGHQAI 85
Cdd:cd03128   81 PVLGICLGAQLL 92
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-171 1.05e-08

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 53.65  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   2 ILLIDNydSFTWNLYQYFCELGAEVLVRrNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQT-PILGVCL 80
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYNiPIFGICM 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  81 GHQAIAQVFGAAIVrAAKVMH-GKTSPVshtgqgvflGLNNPLTVT-RYHSLLID-PLTLPECFEVTARS-EEGEIMGIR 156
Cdd:CHL00197 272 GHQILSLALEAKTF-KLKFGHrGLNHPS---------GLNQQVEITsQNHGFAVNlESLAKNKFYITHFNlNDGTVAGIS 341

                        170
                 ....*....|....*
gi 612157112 157 HRVFDLEGVQFHPES 171
Cdd:CHL00197 342 HSPKPYFSVQYHPEA 356
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 74-180 3.63e-08

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: 51.04  E-value: 3.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  74 PILGVCLGHQAIAQVFGAAIVRAakvmhgktspvshtgqgvflglnnpLTVTRYHSLLIDplTLPECFEVTARSEEGEIM 153
Cdd:cd01745  102 PILGICRGMQLLNVALGGTLYQD-------------------------IRVNSLHHQAIK--RLADGLRVEARAPDGVIE 154

                         90       100       110
                 ....*....|....*....|....*....|.
gi 612157112 154 GIRH----RVFdleGVQFHPESILSEQGHQL 180
Cdd:cd01745  155 AIESpdrpFVL---GVQWHPEWLADTDPDSL 182
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 62-170 1.31e-05

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: 43.78  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112   62 SLAAIRHFSGQ-TPILGVCLG------------HQAIAQVFGAAIVRA--AKVMHGKTSPVSHTGQGVF---LGLNNPLt 123
Cdd:pfam07722  94 ELALIRAALARgKPILGICRGfqllnvalggtlYQDIQEQPGFTDHREhcQVAPYAPSHAVNVEPGSLLaslLGSEEFR- 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 612157112  124 VTRYHSLLIDplTLPECFEVTARSEEGEIMGIR---HRVFDLeGVQFHPE 170
Cdd:pfam07722 173 VNSLHHQAID--RLAPGLRVEAVAPDGTIEAIEspnAKGFAL-GVQWHPE 219
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 74-170 9.56e-04

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: 38.61  E-value: 9.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  74 PILGVCLGHQAIAQVFGAAI------VRAAKVMHGKTSPVSHTGQGVF----------LGlNNPLTVTRYHSLLIDplTL 137
Cdd:COG2071   98 PVLGICRGMQLLNVALGGTLyqdlpdQVPGALDHRQPAPRYAPRHTVEiepgsrlariLG-EEEIRVNSLHHQAVK--RL 174

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 612157112 138 PECFEVTARSEEGEIMGIRHR--VFDLeGVQFHPE 170
Cdd:COG2071  175 GPGLRVSARAPDGVIEAIESPgaPFVL-GVQWHPE 208
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 74-170 2.90e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 37.23  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612157112  74 PILGVCLGHQAIAQVFGAAiVRAAKVMHGKTSPVSHT--GQGVFLG-LNNPLTVTRYHSlliDPLTLPECFEVTARSEEG 150
Cdd:PRK07053  85 PTLGICLGAQLIARALGAR-VYPGGQKEIGWAPLTLTdaGRASPLRhLGAGTPVLHWHG---DTFDLPEGATLLASTPAC 160

                         90       100
                 ....*....|....*....|....
gi 612157112 151 eimgiRHRVFDLE----GVQFHPE 170
Cdd:PRK07053 161 -----RHQAFAWGnhvlALQFHPE 179
 
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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