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Conserved domains on  [gi|489951869|ref|WP_003855176|]
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anthranilate synthase component II [Corynebacterium glutamicum]

Protein Classification

anthranilate synthase component II( domain architecture ID 10792589)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 1-208 6.66e-149

anthranilate synthase component II; Provisional


:

Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 411.93  E-value: 6.66e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGIC 80
Cdd:PRK05637   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  81 LGYQALIEYHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIGRYHSLGCVVAPDGIESLGT 160
Cdd:PRK05637  81 LGFQALLEHHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIARYHSLGCVVAPDGMESLGT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489951869 161 CSSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCVEQLLAN 208
Cdd:PRK05637 161 CSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQLLAN 208
 
Name Accession Description Interval E-value
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 1-208 6.66e-149

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 411.93  E-value: 6.66e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGIC 80
Cdd:PRK05637   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  81 LGYQALIEYHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIGRYHSLGCVVAPDGIESLGT 160
Cdd:PRK05637  81 LGFQALLEHHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIARYHSLGCVVAPDGMESLGT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489951869 161 CSSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCVEQLLAN 208
Cdd:PRK05637 161 CSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQLLAN 208
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 4-198 6.95e-67

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: 203.35  E-value: 6.95e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRNT-VPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCG-PVHGTTDNMILTDagvqSPVFAGLATDVEpdhpeipgrkvpIGRYHSLgcVVA----PDGIES 157
Cdd:COG0512   81 HQAIGEAFGGKVVRAPePMHGKTSPITHDG----SGLFAGLPNPFT------------ATRYHSL--VVDretlPDELEV 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489951869 158 LGTCSSeigDVIMAARTTDGKAIGLQFHPESVLSPTGPVIL 198
Cdd:COG0512  143 TAWTED---GEIMGIRHRELPIEGVQFHPESILTEHGHQLL 180
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 4-202 1.63e-65

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: 199.68  E-value: 1.63e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVP-VETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEItLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCG-PVHGTTDNMILTDAGvqspVFAGLatdvepdhpeipGRKVPIGRYHSLgCVVAPDGIESLGTC 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPePMHGKTSEIHHDGSG----LFKGL------------PQPFTVGRYHSL-VVDPDPLPDLLEVT 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489951869 162 SSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCV 202
Cdd:cd01743  144 ASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
GATase pfam00117
Glutamine amidotransferase class-I;
5-205 1.26e-49

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 159.71  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869    5 VLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLG-QIPLLGICLGY 83
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   84 QALIEYHGGKV--EPCGPVHGTTDNMILTDAGvqspVFAGLatdvepdhpeipGRKVPIGRYHSLGCVVA--PDGIESLG 159
Cdd:pfam00117  81 QLLALAFGGKVvkAKKFGHHGKNSPVGDDGCG----LFYGL------------PNVFIVRRYHSYAVDPDtlPDGLEVTA 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 489951869  160 TCSSeiGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCVEQL 205
Cdd:pfam00117 145 TSEN--DGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-199 8.82e-46

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: 149.94  E-value: 8.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869    3 HVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICL 81
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNdSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   82 GYQALIEYHGGKV-EPCGPVHGTTDNMILTDAGvqspVFAGLATdvepdhpeipgrKVPIGRYHSLgcVVAPDGIESLGT 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVvRANTVMHGKTSEIEHNGAG----IFRGLFN------------PLTATRYHSL--VVEPETLPTCFP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 489951869  161 CS--SEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILS 199
Cdd:TIGR00566 143 VTawEEENIEIMAIRHRDLPLEGVQFHPESILSEQGHQLLA 183
 
Name Accession Description Interval E-value
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 1-208 6.66e-149

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 411.93  E-value: 6.66e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGIC 80
Cdd:PRK05637   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  81 LGYQALIEYHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIGRYHSLGCVVAPDGIESLGT 160
Cdd:PRK05637  81 LGFQALLEHHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIARYHSLGCVVAPDGMESLGT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489951869 161 CSSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCVEQLLAN 208
Cdd:PRK05637 161 CSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQLLAN 208
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 4-198 6.95e-67

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: 203.35  E-value: 6.95e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRNT-VPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:COG0512    1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCG-PVHGTTDNMILTDagvqSPVFAGLATDVEpdhpeipgrkvpIGRYHSLgcVVA----PDGIES 157
Cdd:COG0512   81 HQAIGEAFGGKVVRAPePMHGKTSPITHDG----SGLFAGLPNPFT------------ATRYHSL--VVDretlPDELEV 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489951869 158 LGTCSSeigDVIMAARTTDGKAIGLQFHPESVLSPTGPVIL 198
Cdd:COG0512  143 TAWTED---GEIMGIRHRELPIEGVQFHPESILTEHGHQLL 180
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 4-202 1.63e-65

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: 199.68  E-value: 1.63e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVP-VETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:cd01743    1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEItLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCG-PVHGTTDNMILTDAGvqspVFAGLatdvepdhpeipGRKVPIGRYHSLgCVVAPDGIESLGTC 161
Cdd:cd01743   81 HQAIAEAFGGKVVRAPePMHGKTSEIHHDGSG----LFKGL------------PQPFTVGRYHSL-VVDPDPLPDLLEVT 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489951869 162 SSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCV 202
Cdd:cd01743  144 ASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 3-208 8.76e-62

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 190.34  E-value: 8.76e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   3 HVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICL 81
Cdd:PRK05670   1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNdEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  82 GYQALIEYHGGKVEPCG-PVHGTTDNMILTDagvqSPVFAGLatdvepdhPEipgrKVPIGRYHSLgcVVA----PDGIE 156
Cdd:PRK05670  81 GHQAIGEAFGGKVVRAKeIMHGKTSPIEHDG----SGIFAGL--------PN----PFTVTRYHSL--VVDreslPDCLE 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489951869 157 SlgTCSSEIGdVIMAARTTDGKAIGLQFHPESVLSPTGpvilsrcvEQLLAN 208
Cdd:PRK05670 143 V--TAWTDDG-EIMGVRHKELPIYGVQFHPESILTEHG--------HKLLEN 183
GATase pfam00117
Glutamine amidotransferase class-I;
5-205 1.26e-49

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 159.71  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869    5 VLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLG-QIPLLGICLGY 83
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   84 QALIEYHGGKV--EPCGPVHGTTDNMILTDAGvqspVFAGLatdvepdhpeipGRKVPIGRYHSLGCVVA--PDGIESLG 159
Cdd:pfam00117  81 QLLALAFGGKVvkAKKFGHHGKNSPVGDDGCG----LFYGL------------PNVFIVRRYHSYAVDPDtlPDGLEVTA 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 489951869  160 TCSSeiGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCVEQL 205
Cdd:pfam00117 145 TSEN--DGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 3-199 8.82e-46

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: 149.94  E-value: 8.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869    3 HVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICL 81
Cdd:TIGR00566   1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNdSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   82 GYQALIEYHGGKV-EPCGPVHGTTDNMILTDAGvqspVFAGLATdvepdhpeipgrKVPIGRYHSLgcVVAPDGIESLGT 160
Cdd:TIGR00566  81 GHQAMGQAFGGDVvRANTVMHGKTSEIEHNGAG----IFRGLFN------------PLTATRYHSL--VVEPETLPTCFP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 489951869  161 CS--SEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILS 199
Cdd:TIGR00566 143 VTawEEENIEIMAIRHRDLPLEGVQFHPESILSEQGHQLLA 183
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 1-207 9.20e-42

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 147.87  E-value: 9.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETIL-----AANPDLIcLSPGPGYPADAGNMMALIERTLGQIP 75
Cdd:PRK09522   1 MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIerlatMSNPVLM-LSPGPGVPSEAGCMPELLTRLRGKLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  76 LLGICLGYQALIEYHGGKVEPCGPV-HGTTDNmILTDAgvqSPVFAGLatdVEPdhpeipgrkVPIGRYHSLGCVVAPDG 154
Cdd:PRK09522  80 IIGICLGHQAIVEAYGGYVGQAGEIlHGKASS-IEHDG---QAMFAGL---TNP---------LPVARYHSLVGSNIPAG 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489951869 155 IeslgTCSSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGpvilSRCVEQLLA 207
Cdd:PRK09522 144 L----TINAHFNGMVMAVRHDADRVCGFQFHPESILTTQG----ARLLEQTLA 188
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
4-199 3.51e-38

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 137.93  E-value: 3.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKC-TVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICL 81
Cdd:PRK14607   2 IILIDNYDSFTYNIYQYIGELGPEEiEVVRNdEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  82 GYQALIEYHGGK-VEPCGPVHGTTDNMILTDAGvqspVFAGLatdvepdhpeipGRKVPIGRYHSLgcVVA----PDGIE 156
Cdd:PRK14607  82 GHQAIGYAFGGKiVHAKRILHGKTSPIDHNGKG----LFRGI------------PNPTVATRYHSL--VVEeaslPECLE 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489951869 157 SlgTCSSEIGDvIMAARTTDGKAIGLQFHPESVLSPTGPVILS 199
Cdd:PRK14607 144 V--TAKSDDGE-IMGIRHKEHPIFGVQFHPESILTEEGKRILK 183
PRK13566 PRK13566
anthranilate synthase component I;
3-196 1.95e-34

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 128.88  E-value: 1.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   3 HVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGnMMALIERTLG-QIPLLGICL 81
Cdd:PRK13566 528 RVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSDFD-CKATIDAALArNLPIFGVCL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  82 GYQALIEYHGGKVEPCG-PVHGTTDNMILTDAGvqsPVFAGLatdvepdhpeipGRKVPIGRYHSLgcVVAPDGI--ESL 158
Cdd:PRK13566 607 GLQAIVEAFGGELGQLAyPMHGKPSRIRVRGPG---RLFSGL------------PEEFTVGRYHSL--FADPETLpdELL 669

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489951869 159 GTCSSEIGdVIMAARTTDGKAIGLQFHPESVLSPTGPV 196
Cdd:PRK13566 670 VTAETEDG-VIMAIEHKTLPVAAVQFHPESIMTLGGDV 706
PLN02335 PLN02335
anthranilate synthase
 4-199 1.47e-31

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 114.51  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:PLN02335  21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNdELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKV--EPCGPVHGTTdNMILTDAGVQSPVFAGLATDVEpdhpeipgrkvpIGRYHSLgcVVAPDGI--ESL 158
Cdd:PLN02335 101 LQCIGEAFGGKIvrSPFGVMHGKS-SPVHYDEKGEEGLFSGLPNPFT------------AGRYHSL--VIEKDTFpsDEL 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489951869 159 G-TCSSEIGdVIMAARTTDGKAI-GLQFHPESVLSPTGPVILS 199
Cdd:PLN02335 166 EvTAWTEDG-LIMAARHRKYKHIqGVQFHPESIITTEGKTIVR 207
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
4-200 5.26e-31

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 112.84  E-value: 5.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN---TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLG-QIPLLGI 79
Cdd:PRK07765   3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNddpRLADEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  80 CLGYQALIEYHGGKVEPcGP--VHGTTDNMILTDAGvqspVFAGL-----ATdvepdhpeipgrkvpigRYHSLGCV--V 150
Cdd:PRK07765  83 CLGHQAIGVAFGATVDR-APelLHGKTSSVHHTGVG----VLAGLpdpftAT-----------------RYHSLTILpeT 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489951869 151 APDGIESLGTCSSeigDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSR 200
Cdd:PRK07765 141 LPAELEVTARTDS---GVIMAVRHRELPIHGVQFHPESVLTEGGHRMLAN 187
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
4-208 2.63e-30

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 110.01  E-value: 2.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:PRK08007   2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNdALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLATdvepdhpeipgrKVPIGRYHSLgcVVAPDGIESLG-- 159
Cdd:PRK08007  82 HQAMAQAFGGKVVRAAKVmHGKTSPITHNGEG----VFRGLAN------------PLTVTRYHSL--VVEPDSLPACFev 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489951869 160 TCSSEIGDvIMAARTTDGKAIGLQFHPESVLSPTGpvilsrcvEQLLAN 208
Cdd:PRK08007 144 TAWSETRE-IMGIRHRQWDLEGVQFHPESILSEQG--------HQLLAN 183
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
4-203 1.25e-28

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 106.04  E-value: 1.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:PRK07649   2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNdEVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKV-EPCGPVHGTTDNMILTD----AGVQSPVFAglatdvepdhpeipgrkvpiGRYHSLgcVVAPDGIES 157
Cdd:PRK07649  82 HQSIAQVFGGEVvRAERLMHGKTSLMHHDGktifSDIPNPFTA--------------------TRYHSL--IVKKETLPD 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489951869 158 LGTCSSEIG-DVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCVE 203
Cdd:PRK07649 140 CLEVTSWTEeGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFIR 186
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
4-208 7.47e-27

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 101.49  E-value: 7.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:PRK08857   2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNdEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLatdvepDHPeipgrkVPIGRYHSLgcVVA----PDGIES 157
Cdd:PRK08857  82 HQAIAQVFGGQVVRARQVmHGKTSPIRHTGRS----VFKGL------NNP------LTVTRYHSL--VVKndtlPECFEL 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489951869 158 LGTCSSEIG--DVIMAARTTDGKAIGLQFHPESVLSPTGpvilsrcvEQLLAN 208
Cdd:PRK08857 144 TAWTELEDGsmDEIMGFQHKTLPIEAVQFHPESIKTEQG--------HQLLAN 188
trpG CHL00101
anthranilate synthase component 2
 4-198 2.62e-26

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 99.81  E-value: 2.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:CHL00101   2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNdEIDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCGPV-HGTTdNMILTDagvQSPVFAGLatdvepdhpeipgrKVPI--GRYHSLgcVVAPDGIES-- 157
Cdd:CHL00101  82 HQSIGYLFGGKIIKAPKPmHGKT-SKIYHN---HDDLFQGL--------------PNPFtaTRYHSL--IIDPLNLPSpl 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489951869 158 LGTCSSEIGdVIMAARTTDGKAI-GLQFHPESVLSPTGPVIL 198
Cdd:CHL00101 142 EITAWTEDG-LIMACRHKKYKMLrGIQFHPESLLTTHGQQIL 182
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
4-199 1.00e-25

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 98.40  E-value: 1.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLG 82
Cdd:PRK06774   2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNdELQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLAtdvepdhpeipgRKVPIGRYHSLgcVVA----PDGIES 157
Cdd:PRK06774  82 HQALGQAFGARVVRARQVmHGKTSAICHSGQG----VFRGLN------------QPLTVTRYHSL--VIAadslPGCFEL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489951869 158 lgTCSSEIG---DVIMAARTTDGKAIGLQFHPESVLSPTGPVILS 199
Cdd:PRK06774 144 --TAWSERGgemDEIMGIRHRTLPLEGVQFHPESILSEQGHQLLD 186
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 3-200 1.95e-25

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: 103.06  E-value: 1.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869    3 HVVLIDNHDSFVYNLVDAFavagYKCTvfRNTVPVETILAANP-----------DLICLSPGPGYPADAGNMMALIE--- 68
Cdd:TIGR01823   7 HVLFIDSYDSFTYNVVRLL----EQQT--DISVHVTTVHSDTFqdqllellplfDAIVVGPGPGNPNNAQDMGIISElwe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   69 -RTLGQIPLLGICLGYQALIEYHGGKVEPCG-PVHGTTDNMILTDAGVQSPVFAglatdvepdhpeipgrkVPIGRYHSL 146
Cdd:TIGR01823  81 lANLDEVPVLGICLGFQSLCLAQGADISRLPtPKHGQVYEMHTNDAAIFCGLFS-----------------VKSTRYHSL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489951869  147 gcVVAPDGIESLG---TCSSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSR 200
Cdd:TIGR01823 144 --YANPEGIDTLLplcLTEDEEGIILMSAQTKKKPWFGVQYHPESCCSELGSGKLVS 198
PRK06895 PRK06895
anthranilate synthase component II;
1-208 2.41e-23

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 92.11  E-value: 2.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   1 MTHVVLIDNHDSFVYNLVDafavagykcTVFRNTVPVETILAANPDL--------ICLSPGPGYPADAGNMMALIERTLG 72
Cdd:PRK06895   1 ATKLLIINNHDSFTFNLVD---------LIRKLGVPMQVVNVEDLDLdevenfshILISPGPDVPRAYPQLFAMLERYHQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  73 QIPLLGICLGYQALIEYHGGKVEPCGPV-HGTTDNMILTDAgvqSPVFAGLATDVEpdhpeipgrkvpIGRYHS--LGCV 149
Cdd:PRK06895  72 HKSILGVCLGHQTLCEFFGGELYNLNNVrHGQQRPLKVRSN---SPLFDGLPEEFN------------IGLYHSwaVSEE 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489951869 150 VAPDGIESLGTCSSEigdVIMAARTTDGKAIGLQFHPESVLSPTGpvilsrcvEQLLAN 208
Cdd:PRK06895 137 NFPTPLEITAVCDEN---VVMAMQHKTLPIYGVQFHPESYISEFG--------EQILRN 184
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 25-200 8.36e-15

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: 69.10  E-value: 8.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  25 GYKCTVFRNTVPVETILAANPDLICLSPGPG--YPADAGNM-MALIErtLGqIPLLGICLGYQALIEYHGGKVEPC-GPV 100
Cdd:cd01742   22 GVYSEILPNTTPLEEIKLKNPKGIILSGGPSsvYEEDAPRVdPEIFE--LG-VPVLGICYGMQLIAKALGGKVERGdKRE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869 101 HGTTDNMILTDagvqSPVFAGLA--TDVEPDHpeipGRKVpigryhslgcVVAPDGIESLGtcSSEIGDVImAARTTDGK 178
Cdd:cd01742   99 YGKAEIEIDDS----SPLFEGLPdeQTVWMSH----GDEV----------VKLPEGFKVIA--SSDNCPVA-AIANEEKK 157

                        170       180
                 ....*....|....*....|..
gi 489951869 179 AIGLQFHPESVLSPTGPVILSR 200
Cdd:cd01742  158 IYGVQFHPEVTHTEKGKEILKN 179
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 3-93 3.87e-14

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 69.66  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   3 HVVLIDnhdsF-V-YNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQ-IPLLGI 79
Cdd:COG0505  178 HVVALD----FgVkRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRELLGKgIPIFGI 253

                         90
                 ....*....|....
gi 489951869  80 CLGYQALIEYHGGK 93
Cdd:COG0505  254 CLGHQLLALALGAK 267
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
3-86 1.92e-13

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 67.79  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   3 HVVLIDnhdsF-V-YNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQ-IPLLGI 79
Cdd:PRK12564 179 KVVAID----FgVkRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIRELLEKkIPIFGI 254


                 ....*..
gi 489951869  80 CLGYQAL 86
Cdd:PRK12564 255 CLGHQLL 261
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 15-93 4.54e-13

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: 64.44  E-value: 4.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  15 YNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQ-IPLLGICLGYQALIEYHGGK 93
Cdd:cd01744   10 HNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALGAK 89
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 30-187 6.67e-12

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: 62.27  E-value: 6.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  30 VFRNTVPVETILAANPDLICLSPGPG--YPADAG--NMMALIERTL-GQIPLLGICLGYQALIEYHGGKVEPC-GPVHGT 103
Cdd:COG0518   34 VYAGEILPYDPDLEDPDGLILSGGPMsvYDEDPWleDEPALIREAFeLGKPVLGICYGAQLLAHALGGKVEPGpGREIGW 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869 104 TDNMILTDagvqSPVFAGLatdvePDHPEIpgrkvpigrYHSLGCVVA--PDGIESLgtCSSEIGDViMAARTTDgKAIG 181
Cdd:COG0518  114 APVELTEA----DPLFAGL-----PDEFTV---------WMSHGDTVTelPEGAEVL--ASSDNCPN-QAFRYGR-RVYG 171


                 ....*.
gi 489951869 182 LQFHPE 187
Cdd:COG0518  172 VQFHPE 177
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 5-189 1.20e-11

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 62.94  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   5 VLIDNHDSFVYNLVDAFAVAgykctvfrNTVPveTILAANPDL-----------------ICLSPGPGYP---ADAGNMM 64
Cdd:PLN02889  85 LLIDNYDSYTYNIYQELSIV--------NGVP--PVVVRNDEWtweevyhylyeekafdnIVISPGPGSPtcpADIGICL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  65 ALIeRTLGQIPLLGICLGYQALIEYHGGK-VEPCGPVHGTT-----DNMILTD-------AGVQSPVFAGLATDVEpdhp 131
Cdd:PLN02889 155 RLL-LECRDIPILGVCLGHQALGYVHGARiVHAPEPVHGRLseiehNGCRLFDdipsgrnSGFKVVRYHSLVIDAE---- 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869 132 EIPGRKVPIGRYHSLG---------CVVAPDGIES--LGTCSSEI---------------------GDVIMAARTTDGKA 179
Cdd:PLN02889 230 SLPKELVPIAWTSSSDtlsflesqkSGLVPDAYESqiGQSGSSDPfssklkngtswpsshsermqnGKILMGIMHSTRPH 309

                        250
                 ....*....|
gi 489951869 180 IGLQFHPESV 189
Cdd:PLN02889 310 YGLQFHPESI 319
guaA PRK00074
GMP synthase; Reviewed
 24-200 1.79e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 62.37  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  24 AGYKCTVFRNTVPVETILAANPDLICLSPGP------GYP-ADAgnmmALIErtLGqIPLLGICLGYQALIEYHGGKVEP 96
Cdd:PRK00074  26 LGVYSEIVPYDISAEEIRAFNPKGIILSGGPasvyeeGAPrADP----EIFE--LG-VPVLGICYGMQLMAHQLGGKVER 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  97 CGpvH---GTTDNMILTDagvqSPVFAGL--ATDVEPDHpeipGRKVpigryhslgcVVAPDGIESLGtcSSEigDVIMA 171
Cdd:PRK00074  99 AG--KreyGRAELEVDND----SPLFKGLpeEQDVWMSH----GDKV----------TELPEGFKVIA--STE--NCPIA 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 489951869 172 ARTTDGKAI-GLQFHPESVLSPTGPVILSR 200
Cdd:PRK00074 155 AIANEERKFyGVQFHPEVTHTPQGKKLLEN 184
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 2-92 3.05e-11

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 61.45  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   2 THVVLIDnhdsFVY--NLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGI 79
Cdd:PRK12838 168 KHVALID----FGYkkSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPILGI 243

                         90
                 ....*....|...
gi 489951869  80 CLGYQALIEYHGG 92
Cdd:PRK12838 244 CLGHQLIALALGA 256
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 2-86 7.83e-11

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 60.33  E-value: 7.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869    2 THVVLIDNhdSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICL 81
Cdd:TIGR01368 173 KRVVVIDF--GVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICL 250


                  ....*
gi 489951869   82 GYQAL 86
Cdd:TIGR01368 251 GHQLL 255
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-92 1.49e-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: 56.45  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSF---VYNLVDAFAVAGYKCTVFRNTVPVET--ILAANPDLICLSPGPGYPADAGN---MMALIERTLGQ-I 74
Cdd:cd01653    1 VAVLLFPGFEeleLASPLDALREAGAEVDVVSPDGGPVEsdVDLDDYDGLILPGGPGTPDDLARdeaLLALLREAAAAgK 80

                         90
                 ....*....|....*...
gi 489951869  75 PLLGICLGYQALIEYHGG 92
Cdd:cd01653   81 PILGICLGAQLLVLGVQF 98
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 64-187 2.93e-10

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: 57.26  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  64 MALIERTL-GQIPLLGICLGYQALIEYHGGKVE--PCGPVHGTTDnMILTDAGVQSPVFAGLatdvePDHPEIpgrkvpi 140
Cdd:cd01741   71 KELIRQALaAGKPVLGICLGHQLLARALGGKVGrnPKGWEIGWFP-VTLTEAGKADPLFAGL-----PDEFPV------- 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489951869 141 grYHSLGCVVA--PDGIESLGtcSSEIGDViMAARtTDGKAIGLQFHPE 187
Cdd:cd01741  138 --FHWHGDTVVelPPGAVLLA--SSEACPN-QAFR-YGDRALGLQFHPE 180
PLN02347 PLN02347
GMP synthetase
 28-200 2.15e-09

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 56.23  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  28 CTVFRNTVPVETILAANPDLICLSPGP------GYPADAGNMMALIERtlGQIPLLGICLGYQALIEYHGGKVEPCGpvH 101
Cdd:PLN02347  37 SLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVPVLGICYGMQLIVQKLGGEVKPGE--K 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869 102 GTTDNMILtDAGVQSPVFAGLATdvepdhpeipGRKVPIGRYHSLGCVVAPDGIESLGTcsSEIGDVImAARTTDGKAIG 181
Cdd:PLN02347 113 QEYGRMEI-RVVCGSQLFGDLPS----------GETQTVWMSHGDEAVKLPEGFEVVAK--SVQGAVV-AIENRERRIYG 178

                        170
                 ....*....|....*....
gi 489951869 182 LQFHPESVLSPTGPVILSR 200
Cdd:PLN02347 179 LQYHPEVTHSPKGMETLRH 197
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 15-93 2.26e-09

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 56.14  E-value: 2.26e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489951869  15 YNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLGYQALIEYHGGK 93
Cdd:PLN02771 252 HNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGK 330
PRK00758 PRK00758
GMP synthase subunit A; Validated
 3-187 6.55e-09

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 53.32  E-value: 6.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   3 HVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETIlAANPDLICLSPGPGYpADAGNMMALIERTlgQIPLLGICLG 82
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEI-KAFEDGLILSGGPDI-ERAGNCPEYLKEL--DVPILGICLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  83 YQALIEYHGGKVEPCG-PVHGTTDNMILTDAGvqspVFAGLA--TDVEPDHP-EIpgrkvpigryhslgcVVAPDGIESL 158
Cdd:PRK00758  77 HQLIAKAFGGEVGRGEyGEYALVEVEILDEDD----ILKGLPpeIRVWASHAdEV---------------KELPDGFEIL 137

                        170       180
                 ....*....|....*....|....*....
gi 489951869 159 GTcsSEIGDViMAARTTDGKAIGLQFHPE 187
Cdd:PRK00758 138 AR--SDICEV-EAMKHKEKPIYGVQFHPE 163
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 15-93 9.26e-09

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 54.42  E-value: 9.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  15 YNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQ-IPLLGICLGYQALIEYHGGK 93
Cdd:CHL00197 204 YNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYnIPIFGICMGHQILSLALEAK 283
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-86 1.28e-08

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: 50.66  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLIDNHDSF---VYNLVDAFAVAGYKCTVFRNTVPVET--ILAANPDLICLSPGPGYPADAGN---MMALIERTLGQ-I 74
Cdd:cd03128    1 VAVLLFGGSEeleLASPLDALREAGAEVDVVSPDGGPVEsdVDLDDYDGLILPGGPGTPDDLAWdeaLLALLREAAAAgK 80

                         90
                 ....*....|..
gi 489951869  75 PLLGICLGYQAL 86
Cdd:cd03128   81 PVLGICLGAQLL 92
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 38-187 6.33e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 44.86  E-value: 6.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  38 ETILAAnpDLICLsPGPGYPADAGNMM-----ALIERTLGQIPLLGICLGYQALIEY--HGGKVEPCGPVHGTTDNMilt 110
Cdd:PRK13143  34 EEILDA--DGIVL-PGVGAFGAAMENLsplrdVILEAARSGKPFLGICLGMQLLFESseEGGGVRGLGLFPGRVVRF--- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869 111 DAGVQSPVFAGLATDVEPDHPEIPGRKvpiGRY----HSLGcvVAPDGIES-LGTCSSEIGdviMAARTTDGKAIGLQFH 185
Cdd:PRK13143 108 PAGVKVPHMGWNTVKVVKDCPLFEGID---GEYvyfvHSYY--AYPDDEDYvVATTDYGIE---FPAAVCNDNVFGTQFH 179


                 ..
gi 489951869 186 PE 187
Cdd:PRK13143 180 PE 181
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 20-89 7.44e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 42.04  E-value: 7.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489951869  20 AFAVAGYKCTVFRNtvpVETILAAnpDLICLsPGPGYPADAgnMMALIERTLGQ---------IPLLGICLGYQALIEY 89
Cdd:PRK13141  18 ALERLGAEAVITSD---PEEILAA--DGVIL-PGVGAFPDA--MANLRERGLDEvikeavasgKPLLGICLGMQLLFES 88
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 63-122 1.45e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 41.47  E-value: 1.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489951869  63 MMALIERTLGQ-IPLLGICLGYQALIEYHGGKV-----EPCGPVHGTtdnmiLTDAGVQSPVFAGL 122
Cdd:PRK07567  82 LSGLLDEVVARdFPFLGACYGVGTLGHHQGGVVdrtygEPVGAVTVS-----LTDAGRADPLLAGL 142
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 75-187 1.59e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 41.10  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  75 PLLGICLGYQALIEYHGGKV--EPCGPVHGTTDnMILTDAGVQSPVFAGLAtdvepdhPEIPGRKVpigryHSLGCVVAP 152
Cdd:PRK09065  90 PLLGICYGHQLLAHALGGEVgyNPAGRESGTVT-VELHPAAADDPLFAGLP-------AQFPAHLT-----HLQSVLRLP 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489951869 153 DGIeslgtcsseigdVIMAARTTDG--------KAIGLQFHPE 187
Cdd:PRK09065 157 PGA------------VVLARSAQDPhqafrygpHAWGVQFHPE 187
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 4-187 2.09e-04

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: 40.56  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   4 VVLID----NhdsfVYNLVDAFAVAGYKCTVFRNTvpvETILAAnpDLICLsPGPGYPADAGNMM-------ALIERTLG 72
Cdd:cd01748    1 IAIIDygmgN----LRSVANALERLGAEVIITSDP---EEILSA--DKLIL-PGVGAFGDAMANLrerglieALKEAIAS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  73 QIPLLGICLGYQALIE--YHGGKVEPCGPVHGTTDNMiltdagvqsPVFAGLAT--------DVEPDHPEIPGrkVPIGR 142
Cdd:cd01748   71 GKPFLGICLGMQLLFEssEEGGGTKGLGLIPGKVVRF---------PASEGLKVphmgwnqlEITKESPLFKG--IPDGS 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489951869 143 Y----HSLGcVVAPDGIESLGTC--SSEIGDVIMaarttDGKAIGLQFHPE 187
Cdd:cd01748  140 YfyfvHSYY-APPDDPDYILATTdyGGKFPAAVE-----KDNIFGTQFHPE 184
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-187 2.25e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 40.54  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   1 MTHVVLIDnhdsfvY---NL---VDAFAVAGYKCTVFRNTVPvETILAAnpDLICLsPGPG-YPA-----DAGNMM-ALI 67
Cdd:PRK13146   1 MMTVAIID------YgsgNLrsaAKALERAGAGADVVVTADP-DAVAAA--DRVVL-PGVGaFADcmrglRAVGLGeAVI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  68 ERTLGQ-IPLLGICLGYQALIEY--HGGKVEPCGPVHGTTDNMILTDAG--------------VQSPVFAGLATDvepdh 130
Cdd:PRK13146  71 EAVLAAgRPFLGICVGMQLLFERglEHGDTPGLGLIPGEVVRFQPDGPAlkvphmgwntvdqtRDHPLFAGIPDG----- 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869 131 peipgrkvpiGRY---HSLGcVVAPDGIESLGTCssEIGDVIMAArTTDGKAIGLQFHPE 187
Cdd:PRK13146 146 ----------ARFyfvHSYY-AQPANPADVVAWT--DYGGPFTAA-VARDNLFATQFHPE 191
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 64-187 2.81e-04

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: 40.32  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869   64 MALIERTLGQ-IPLLGICLGYQALIEYHGGKVEPcgPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHP--EIPGRKVP- 139
Cdd:pfam07722  95 LALIRAALARgKPILGICRGFQLLNVALGGTLYQ--DIQEQPGFTDHREHCQVAPYAPSHAVNVEPGSLlaSLLGSEEFr 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  140 IGRYHSLG----------CVVAPDGieslgtcsseigdVIMAARTTDGK--AIGLQFHPE 187
Cdd:pfam07722 173 VNSLHHQAidrlapglrvEAVAPDG-------------TIEAIESPNAKgfALGVQWHPE 219
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 75-187 1.12e-03

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 39.31  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  75 PLLGICLGYQALIEY--HGGKVEPCGPVHGTTDNMILTDaGVQSPVFAGLATDVEPDHP---EIPGRKVpigrY--HSLG 147
Cdd:PLN02617  81 PFLGICLGLQLLFESseENGPVEGLGVIPGVVGRFDSSN-GLRVPHIGWNALQITKDSElldGVGGRHV----YfvHSYR 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489951869 148 CVVAPDGIE-SLGTCSSEiGDVIMAARTtdGKAIGLQFHPE 187
Cdd:PLN02617 156 ATPSDENKDwVLATCNYG-GEFIASVRK--GNVHAVQFHPE 193
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 17-130 2.60e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 37.62  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489951869  17 LVDAFAVAGYKCTVFRNTVP-VETILAANPDLICLSPGP-------GYPADAgNMMALIERTL-GQIPLLGICLGYQALI 87
Cdd:PRK07053  19 FEQVLGARGYRVRYVDVGVDdLETLDALEPDLLVVLGGPigvyddeLYPFLA-PEIALLRQRLaAGLPTLGICLGAQLIA 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489951869  88 EYHGGKVEPCG-------PVhgttdnmILTDAGVQSPVfAGLATDVEPDH 130
Cdd:PRK07053  98 RALGARVYPGGqkeigwaPL-------TLTDAGRASPL-RHLGAGTPVLH 139
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 28-75 7.32e-03

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 36.26  E-value: 7.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489951869  28 CTVFRNTVPvetILAANPDLICLSPGpGYPADAGNMMALIERTLGQIP 75
Cdd:cd16422  128 CLLLRRGIP---YIATHPDINCPSEE-GPIPDAGSIIALIETSTGRRP 171
 
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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