|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
240-501 |
6.29e-124 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 370.47 E-value: 6.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 240 LDKIYAHRKNAVDEQKKIPALrpEALQAAYDlniAPPQLSFPDRLRQSDYPLSLMAEIKRASPSKGIISANVCAPAQARE 319
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPL--ADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 320 YAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEGLpnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTRLY 399
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 400 HYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKKEG 479
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 211584265 480 VKAILVGEALMRAPDTSAFVAQ 501
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
238-503 |
1.99e-106 |
|
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439904 Cd Length: 257 Bit Score: 325.44 E-value: 1.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 238 SILDKIYAHRKNAVDEQKkipALRPEA-LQAAydLNIAPPQLSFPDRLRQSDyPLSLMAEIKRASPSKGIISANVCAPAQ 316
Cdd:COG0134 2 TILDKIVAHKREEVAARK---ARVPLAeLEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 317 AREYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLeGLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLT 396
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAAV-DLP----VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 397 RLYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYK 476
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*..
gi 211584265 477 KEGVKAILVGEALMRAPDTSAFVAQLL 503
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALRELL 257
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
280-502 |
2.65e-105 |
|
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.
Pssm-ID: 238203 Cd Length: 217 Bit Score: 320.95 E-value: 2.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 280 FPDRLRQSDYpLSLMAEIKRASPSKGIISANVCAPAQAREYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLeglpnRPA 359
Cdd:cd00331 1 FKAALKRPGG-LGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 360 VLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTS 439
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211584265 440 FEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKKEGVKAILVGEALMRAPDTSAFVAQL 502
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
238-505 |
2.89e-105 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 322.49 E-value: 2.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 238 SILDKIYAHRKNAVDEQKKIPALrpEALQAAydLNIAPPQLSFPDRLRQSdyPLSLMAEIKRASPSKGIISANVCAPAQA 317
Cdd:PRK00278 3 DILDKIVAYKREEVAARKAQVPL--AELKAR--AAAAPPPRDFAAALRAG--KPAVIAEVKKASPSKGVIREDFDPVEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 318 REYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEgLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTR 397
Cdd:PRK00278 77 KAYEAGGAACLSVLTDERFFQGSLEYLRAARAAVS-LP----VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQLKE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 398 LYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKK 477
Cdd:PRK00278 152 LLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRLAK 231
|
250 260
....*....|....*....|....*...
gi 211584265 478 EGVKAILVGEALMRAPDTSAFVAQLLGG 505
Cdd:PRK00278 232 AGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
24-219 |
1.46e-104 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 317.75 E-value: 1.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPE-EAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdasgKNIIMG 183
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTE------DGEIMG 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFLELTAG 219
Cdd:COG0512 154 IRHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
23-218 |
2.27e-100 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 307.06 E-value: 2.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 23 NVILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVC 102
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPA-EAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 103 MGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdasgKNIIM 182
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTD------DGEIM 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 211584265 183 GVRHKEFAVEGVQFHPESILTQYGRKMFRNFLELTA 218
Cdd:PRK05670 154 GVRHKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
24-214 |
1.29e-92 |
|
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: 286.74 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPE-DAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdasgKNIIMG 183
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTE------DGVIMA 153
|
170 180 190
....*....|....*....|....*....|.
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFL 214
Cdd:cd01743 154 LRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
554-745 |
5.54e-71 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 230.31 E-value: 5.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 554 VPDDVALGISRVVKSTPRPADTLQQPSSATS-LEWFDHSTNILRHPSRALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGS 632
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKAGADYLGLIFSESSkRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQLHGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 633 EPLEWSSLIP--VPVIRKFAPGD----IGIARRAYHT-LPLLDSGAGGSGELLEESGVKKVLDSdeGLRVILAGGLNPDN 705
Cdd:pfam00697 81 EDQEYENLLPtgVPVIKAIWVPDsvdtVDIARRADHVdLPLLDSGAGGTGELFDWSLVSKWLKS--GLKVILAGGLNPDN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 211584265 706 VAGTVKKLGqsgqkVVGLDVSSGVETNGAQDLEKIRAFVK 745
Cdd:pfam00697 159 VVEAIKTPG-----VIGVDVSSGVETNGIKDLNKIRKFVQ 193
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
24-216 |
8.72e-70 |
|
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: 226.98 E-value: 8.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPN-EAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDasgknIIMG 183
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI-----EIMA 155
|
170 180 190
....*....|....*....|....*....|...
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFLEL 216
Cdd:TIGR00566 156 IRHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
25-214 |
1.88e-60 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 201.70 E-value: 1.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 25 ILIDNYDSFTWNIYQYLVLEGATVTVYRNDEvTVEDLVAKKPTQLVISPGPGHPdTDAGISNAVIKH-FSGKVPIFGVCM 103
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSP-GAAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTG-EILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDAsgkniIM 182
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGT-----IM 153
|
170 180 190
....*....|....*....|....*....|..
gi 211584265 183 GVRHKEFAVEGVQFHPESILTQYGRKMFRNFL 214
Cdd:pfam00117 154 GIRHKKLPIFGVQFHPESILTPHGPEILFNFF 185
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
27-215 |
3.18e-60 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 201.41 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 27 IDNYDSFTWNIYQYL--VLEGATVTVYRNdEVTVEDLVAKKPTQLVISPGPGHP--DTDAGISNAVIKHFSGKVPIFGVC 102
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPknDRDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 103 MGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGThsTIPDCLEVTSRVelgDASGKNIIM 182
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATT---DHDGEELVM 155
|
170 180 190
....*....|....*....|....*....|...
gi 211584265 183 GVRHKEFAVEGVQFHPESILTQYGRKMFRNFLE 215
Cdd:NF041322 156 GIRHREHPIECVQFHPESVLTGVGHDVIENFLA 188
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
520-747 |
2.04e-46 |
|
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.
Pssm-ID: 238237 Cd Length: 203 Bit Score: 163.90 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 520 VKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVkstprpadtlqqpssatslewfdhstnilrhPS 599
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAAL-------------------------------PP 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 600 RALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLEW----SSLIPVPVIRKF---APGDIGIARRAYHT--LPLLDS- 669
Cdd:cd00405 50 FVKRVGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYcaqlRARLGLPVIKAIrvkDEEDLEKAAAYAGEvdAILLDSk 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 670 ---GAGGSGELLEESGVKKVldsDEGLRVILAGGLNPDNVAGTVKKLgqsgqKVVGLDVSSGVETN-GAQDLEKIRAFVK 745
Cdd:cd00405 130 sggGGGGTGKTFDWSLLRGL---ASRKPVILAGGLTPDNVAEAIRLV-----RPYGVDVSSGVETSpGIKDPEKIRAFIE 201
|
..
gi 211584265 746 SA 747
Cdd:cd00405 202 AA 203
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
518-749 |
3.14e-40 |
|
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; Phosphoribosylanthranilate isomerase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439905 Cd Length: 208 Bit Score: 146.82 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 518 PLVKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVkstprpadtlqqpssatslewfdhstnilrh 597
Cdd:COG0135 2 TRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAAL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 598 PSRALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLEW----SSLIPVPVIRKFAPGDIGIARRAYHTLP-----LLD 668
Cdd:COG0135 51 PPFVKKVGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYcaalRERLGLPVIKAIRVGDGADLEEAAAYAPvadalLLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 669 SGA----GGSGELLEESGVKKVldsDEGLRVILAGGLNPDNVAGTVKKLGqsgqkVVGLDVSSGVET-NGAQDLEKIRAF 743
Cdd:COG0135 131 AKVpglyGGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVR-----PYGVDVSSGVESaPGVKDPDKIRAF 202
|
....*.
gi 211584265 744 VKSAKS 749
Cdd:COG0135 203 VEAVRA 208
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
520-749 |
1.70e-32 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 124.92 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 520 VKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVkstprpadtlqqpssatslewfdhstnilrhPS 599
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAAL-------------------------------PP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 600 RALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLE----WSSLIPVPVIRKF---APGDIGIARRAYHT--LPLLDSG 670
Cdd:PRK01222 54 FVKVVGVFVNASDEEIDEIVETVPLDLLQLHGDETPEfcrqLKRRYGLPVIKALrvrSAGDLEAAAAYYGDadGLLLDAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 671 A---GGSGELLEESgvkkVLDSDEGLRVILAGGLNPDNVAGTVKKLGQSgqkvvGLDVSSGVET-NGAQDLEKIRAFVKS 746
Cdd:PRK01222 134 VglpGGTGKTFDWS----LLPAGLAKPWILAGGLNPDNVAEAIRQVRPY-----GVDVSSGVESaPGIKDPEKIRAFIEA 204
|
...
gi 211584265 747 AKS 749
Cdd:PRK01222 205 VKS 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
240-501 |
6.29e-124 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 370.47 E-value: 6.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 240 LDKIYAHRKNAVDEQKKIPALrpEALQAAYDlniAPPQLSFPDRLRQSDYPLSLMAEIKRASPSKGIISANVCAPAQARE 319
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPL--ADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 320 YAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEGLpnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTRLY 399
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 400 HYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKKEG 479
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 211584265 480 VKAILVGEALMRAPDTSAFVAQ 501
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
238-503 |
1.99e-106 |
|
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439904 Cd Length: 257 Bit Score: 325.44 E-value: 1.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 238 SILDKIYAHRKNAVDEQKkipALRPEA-LQAAydLNIAPPQLSFPDRLRQSDyPLSLMAEIKRASPSKGIISANVCAPAQ 316
Cdd:COG0134 2 TILDKIVAHKREEVAARK---ARVPLAeLEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 317 AREYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLeGLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLT 396
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAAV-DLP----VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 397 RLYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYK 476
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*..
gi 211584265 477 KEGVKAILVGEALMRAPDTSAFVAQLL 503
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALRELL 257
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
280-502 |
2.65e-105 |
|
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.
Pssm-ID: 238203 Cd Length: 217 Bit Score: 320.95 E-value: 2.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 280 FPDRLRQSDYpLSLMAEIKRASPSKGIISANVCAPAQAREYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLeglpnRPA 359
Cdd:cd00331 1 FKAALKRPGG-LGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 360 VLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTS 439
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211584265 440 FEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKKEGVKAILVGEALMRAPDTSAFVAQL 502
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
238-505 |
2.89e-105 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 322.49 E-value: 2.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 238 SILDKIYAHRKNAVDEQKKIPALrpEALQAAydLNIAPPQLSFPDRLRQSdyPLSLMAEIKRASPSKGIISANVCAPAQA 317
Cdd:PRK00278 3 DILDKIVAYKREEVAARKAQVPL--AELKAR--AAAAPPPRDFAAALRAG--KPAVIAEVKKASPSKGVIREDFDPVEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 318 REYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEgLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTR 397
Cdd:PRK00278 77 KAYEAGGAACLSVLTDERFFQGSLEYLRAARAAVS-LP----VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQLKE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 398 LYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKK 477
Cdd:PRK00278 152 LLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRLAK 231
|
250 260
....*....|....*....|....*...
gi 211584265 478 EGVKAILVGEALMRAPDTSAFVAQLLGG 505
Cdd:PRK00278 232 AGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
24-219 |
1.46e-104 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 317.75 E-value: 1.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPE-EAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdasgKNIIMG 183
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAWTE------DGEIMG 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFLELTAG 219
Cdd:COG0512 154 IRHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
23-218 |
2.27e-100 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 307.06 E-value: 2.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 23 NVILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVC 102
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPA-EAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 103 MGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdasgKNIIM 182
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAWTD------DGEIM 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 211584265 183 GVRHKEFAVEGVQFHPESILTQYGRKMFRNFLELTA 218
Cdd:PRK05670 154 GVRHKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
24-214 |
1.29e-92 |
|
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: 286.74 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPE-DAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdasgKNIIMG 183
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTE------DGVIMA 153
|
170 180 190
....*....|....*....|....*....|.
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFL 214
Cdd:cd01743 154 LRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PRK09427 |
PRK09427 |
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
235-752 |
2.06e-92 |
|
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;
Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 295.96 E-value: 2.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 235 KKLSILDKIYAHRKNAVDEQKKIPALrpEALQAaydlNIAPPQLSFPDRLRQSDYplSLMAEIKRASPSKGIISANVCAP 314
Cdd:PRK09427 2 MMPTVLAKIVADKAIWVAARKQQQPL--ASFQN----EIQPSDRSFYDALKGPKT--AFILECKKASPSKGLIRDDFDPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 315 AQAREYaKAGASVISVLTEPEWFKGTIDDLRAVRQSLEgLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIEL 394
Cdd:PRK09427 74 EIARVY-KHYASAISVLTDEKYFQGSFDFLPIVRAIVT-QP----ILCKDFIIDPYQIYLARYYGADAILLMLSVLDDEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 395 LTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEA 474
Cdd:PRK09427 148 YRQLAAVAHSLNMGVLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPADVIVISESGIYTHAQVRE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 475 YKKeGVKAILVGEALMRAPDTSAFVAQLLGGSNqnfagaspssplvKICG-TRTEEgALAAIQAGADLIGIIMVQGRSRL 553
Cdd:PRK09427 228 LSP-FANGFLIGSSLMAEDDLELAVRKLILGEN-------------KVCGlTRPQD-AKAAYDAGAVYGGLIFVEKSPRY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 554 VPDDVALGIsrvvkstprpadtlqqpSSATSLEwfdhstnilrhpsralLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSE 633
Cdd:PRK09427 293 VSLEQAQEI-----------------IAAAPLR----------------YVGVFRNADIEDIVDIAKQLSLAAVQLHGDE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 634 PLEWsslipVPVIRKFAPGDIGIArRAY---HTLP----------LLDSGAGGSGELLEESgvkkVLDSDEGLRVILAGG 700
Cdd:PRK09427 340 DQAY-----IDALREALPKTCQIW-KAIsvgDTLPardlqhvdryLLDNGQGGTGQTFDWS----LLPGQSLDNVLLAGG 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 211584265 701 LNPDNVAGTVKklgqsgQKVVGLDVSSGVETN-GAQDLEKIRAFvksAKSIRQ 752
Cdd:PRK09427 410 LNPDNCQQAAQ------LGCAGLDFNSGVESApGIKDAQKLASV---FQTLRA 453
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
24-217 |
8.61e-79 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 262.73 E-value: 8.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLV-LEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVC 102
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGeLGPEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPE-EAGISVEVIRHFSGKVPILGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 103 MGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDasgkniIM 182
Cdd:PRK14607 81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAKSDDGE------IM 154
|
170 180 190
....*....|....*....|....*....|....*
gi 211584265 183 GVRHKEFAVEGVQFHPESILTQYGRKMFRNFLELT 217
Cdd:PRK14607 155 GIRHKEHPIFGVQFHPESILTEEGKRILKNFLNYQ 189
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
24-215 |
3.69e-72 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 233.54 E-value: 3.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPN-EAGISMEVIRYFAGKIPIFGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDasgkniIMG 183
Cdd:PRK07649 81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTEEGE------IMA 154
|
170 180 190
....*....|....*....|....*....|..
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFLE 215
Cdd:PRK07649 155 IRHKTLPIEGVQFHPESIMTSHGKELLQNFIR 186
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
24-214 |
6.83e-72 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 232.50 E-value: 6.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPD-EAGISLDVIRHYAGRLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDasgkniIMG 183
Cdd:PRK08007 81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETRE------IMG 154
|
170 180 190
....*....|....*....|....*....|.
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFL 214
Cdd:PRK08007 155 IRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
554-745 |
5.54e-71 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 230.31 E-value: 5.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 554 VPDDVALGISRVVKSTPRPADTLQQPSSATS-LEWFDHSTNILRHPSRALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGS 632
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKAGADYLGLIFSESSkRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQLHGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 633 EPLEWSSLIP--VPVIRKFAPGD----IGIARRAYHT-LPLLDSGAGGSGELLEESGVKKVLDSdeGLRVILAGGLNPDN 705
Cdd:pfam00697 81 EDQEYENLLPtgVPVIKAIWVPDsvdtVDIARRADHVdLPLLDSGAGGTGELFDWSLVSKWLKS--GLKVILAGGLNPDN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 211584265 706 VAGTVKKLGqsgqkVVGLDVSSGVETNGAQDLEKIRAFVK 745
Cdd:pfam00697 159 VVEAIKTPG-----VIGVDVSSGVETNGIKDLNKIRKFVQ 193
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
24-216 |
8.72e-70 |
|
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: 226.98 E-value: 8.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPN-EAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDasgknIIMG 183
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI-----EIMA 155
|
170 180 190
....*....|....*....|....*....|...
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFLEL 216
Cdd:TIGR00566 156 IRHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
24-214 |
5.68e-69 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 224.76 E-value: 5.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPN-EAGISLQAIEHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDASgKNIIMG 183
Cdd:PRK08857 81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGS-MDEIMG 159
|
170 180 190
....*....|....*....|....*....|.
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFL 214
Cdd:PRK08857 160 FQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
24-215 |
1.19e-66 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 218.58 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPN-EAGISLAVIRHFADKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGdaSGKNIIMG 183
Cdd:PRK06774 81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERG--GEMDEIMG 158
|
170 180 190
....*....|....*....|....*....|..
gi 211584265 184 VRHKEFAVEGVQFHPESILTQYGRKMFRNFLE 215
Cdd:PRK06774 159 IRHRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
24-215 |
1.49e-65 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 216.45 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDL--VAKKPTQLVISPGPGHPDTdAGISNAVIKHFSG-KVPIFG 100
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEaaVAAQFDGVLLSPGPGTPER-AGASIDMVRACAAaGTPLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 101 VCMGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGdasgknI 180
Cdd:PRK07765 82 VCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTDSG------V 155
|
170 180 190
....*....|....*....|....*....|....*
gi 211584265 181 IMGVRHKEFAVEGVQFHPESILTQYGRKMFRNFLE 215
Cdd:PRK07765 156 IMAVRHRELPIHGVQFHPESVLTEGGHRMLANWLT 190
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
24-216 |
3.71e-63 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 209.20 E-value: 3.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPR-DSGISLDVISSYAPYIPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdasgKNIIMG 183
Cdd:CHL00101 81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWTE------DGLIMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 211584265 184 VRHKEF-AVEGVQFHPESILTQYGRKMFRNFLEL 216
Cdd:CHL00101 155 CRHKKYkMLRGIQFHPESLLTTHGQQILRNFLSL 188
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
24-216 |
6.02e-62 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 207.34 E-value: 6.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSGKVPIFGVCM 103
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQ-DSGISLQTVLELGPLVPLFGVCM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGK-VDVTGEILHGKTSELKHDSK---GVYQGLPTSLEVTRYHSLAGTHSTIP-DCLEVTSRVELGdasgk 178
Cdd:PLN02335 100 GLQCIGEAFGGKiVRSPFGVMHGKSSPVHYDEKgeeGLFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTEDG----- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 211584265 179 nIIMGVRHKEFA-VEGVQFHPESILTQYGRKMFRNFLEL 216
Cdd:PLN02335 175 -LIMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKI 212
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
25-214 |
1.88e-60 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 201.70 E-value: 1.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 25 ILIDNYDSFTWNIYQYLVLEGATVTVYRNDEvTVEDLVAKKPTQLVISPGPGHPdTDAGISNAVIKH-FSGKVPIFGVCM 103
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSP-GAAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 104 GQQCMITSFGGKVDVTG-EILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDAsgkniIM 182
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGT-----IM 153
|
170 180 190
....*....|....*....|....*....|..
gi 211584265 183 GVRHKEFAVEGVQFHPESILTQYGRKMFRNFL 214
Cdd:pfam00117 154 GIRHKKLPIFGVQFHPESILTPHGPEILFNFF 185
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
27-215 |
3.18e-60 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 201.41 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 27 IDNYDSFTWNIYQYL--VLEGATVTVYRNdEVTVEDLVAKKPTQLVISPGPGHP--DTDAGISNAVIKHFSGKVPIFGVC 102
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPknDRDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 103 MGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGThsTIPDCLEVTSRVelgDASGKNIIM 182
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTATT---DHDGEELVM 155
|
170 180 190
....*....|....*....|....*....|...
gi 211584265 183 GVRHKEFAVEGVQFHPESILTQYGRKMFRNFLE 215
Cdd:NF041322 156 GIRHREHPIECVQFHPESVLTGVGHDVIENFLA 188
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
237-519 |
1.88e-49 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 185.23 E-value: 1.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 237 LSILDKIYAhrkNAVDEQK------KIPALRPEALQAaydlniaPPQLSFPDRLRQSDyPLSLMAEIKRASPSKGIISAN 310
Cdd:PRK13802 1 MSVLDELVA---GALEDQRtreltvSLEEVKKAAAAA-------PAPIDATRWLKRAD-GIPVIAEIKRASPSKGHLSDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 311 VCAPAQAREYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEgLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKML 390
Cdd:PRK13802 70 PDPAALAREYEQGGASAISVLTEGRRFLGSLDDFDKVRAAVH-IP----VLRKDFIVTDYQIWEARAHGADLVLLIVAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 391 DIELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQ 470
Cdd:PRK13802 145 DDAQLKHLLDLAHELGMTVLVETHTREEIERAIAAGAKVIGINARNLKDLKVDVNKYNELAADLPDDVIKVAESGVFGAV 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 211584265 471 DVEAYKKEGVKAILVGEALMRAPDTSAFVAQLLGGSNQnfAGASPSSPL 519
Cdd:PRK13802 225 EVEDYARAGADAVLVGEGVATADDHELAVERLVKAGAR--VKASETTPL 271
|
|
| PLN02460 |
PLN02460 |
indole-3-glycerol-phosphate synthase |
239-504 |
8.76e-47 |
|
indole-3-glycerol-phosphate synthase
Pssm-ID: 215254 Cd Length: 338 Bit Score: 169.57 E-value: 8.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 239 ILDKIYAHRKNAVDEQKkipALRP-EALQAAydLNIAPPQLSFPDRLRQSD----YPlSLMAEIKRASPSKGIISANVCA 313
Cdd:PLN02460 68 ILEEIVWYKDVEVAQMK---ERKPlYLLKKA--LQNAPPARDFVGALRAAHkrtgQP-GLIAEVKKASPSRGVLRENFDP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 314 PAQAREYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEGLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKML--- 390
Cdd:PLN02460 142 VEIAQAYEKGGAACLSVLTDEKYFQGSFENLEAIRNAGVKCP----LLCKEFIVDAWQIYYARSKGADAILLIAAVLpdl 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 391 DIELLTRLyhySRSLGMEPLVEVNTPEEMKIAVDL-GSEVIGVNNRDLTSFEVDLGTTSRLM-----DQVPESTI-VCAL 463
Cdd:PLN02460 218 DIKYMLKI---CKSLGMAALIEVHDEREMDRVLGIeGVELIGINNRSLETFEVDISNTKKLLegergEQIREKGIiVVGE 294
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 211584265 464 SGISGPQDVEAYKKEGVKAILVGEALMRAPDTSAFVAQLLG 504
Cdd:PLN02460 295 SGLFTPDDVAYVQNAGVKAVLVGESLVKQDDPGKGIAGLFG 335
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
520-747 |
2.04e-46 |
|
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.
Pssm-ID: 238237 Cd Length: 203 Bit Score: 163.90 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 520 VKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVkstprpadtlqqpssatslewfdhstnilrhPS 599
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAAL-------------------------------PP 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 600 RALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLEW----SSLIPVPVIRKF---APGDIGIARRAYHT--LPLLDS- 669
Cdd:cd00405 50 FVKRVGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYcaqlRARLGLPVIKAIrvkDEEDLEKAAAYAGEvdAILLDSk 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 670 ---GAGGSGELLEESGVKKVldsDEGLRVILAGGLNPDNVAGTVKKLgqsgqKVVGLDVSSGVETN-GAQDLEKIRAFVK 745
Cdd:cd00405 130 sggGGGGTGKTFDWSLLRGL---ASRKPVILAGGLTPDNVAEAIRLV-----RPYGVDVSSGVETSpGIKDPEKIRAFIE 201
|
..
gi 211584265 746 SA 747
Cdd:cd00405 202 AA 203
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
22-268 |
6.27e-46 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 172.13 E-value: 6.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 22 SNVILIDNYDSFTWNIYQYLVLEGATVTVYRND---EVTVEDLVAKKPTQLVISPGPGHPdTDAGISNAVIKHFSGKVPI 98
Cdd:PRK09522 2 ADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVP-SEAGCMPELLTRLRGKLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 99 FGVCMGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGthSTIPDCLEVtsrvelgDASGK 178
Cdd:PRK09522 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVG--SNIPAGLTI-------NAHFN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 179 NIIMGVRHKEFAVEGVQFHPESILTQYGRKMFRNFLeltagTWdnkqGAAVAAPADKKLSILDKIYAHRKNAVDEQKKIP 258
Cdd:PRK09522 152 GMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTL-----AW----AQQKLEPTNTLQPILEKLYQAQTLSQQESHQLF 222
|
250
....*....|....*.
gi 211584265 259 A------LRPEALQAA 268
Cdd:PRK09522 223 SavvrgeLKPEQLAAA 238
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
15-219 |
1.35e-42 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 165.48 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 15 AAKLASASNVILIDNYDSFTWNIYQYLVLEGATVTVYRNDeVTVEDLVAKKPTQLVISPGPGHPDtDAGISNAVIKHFSG 94
Cdd:PRK13566 520 AAAVGEGKRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPS-DFDCKATIDAALAR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 95 KVPIFGVCMGQQCMITSFGGKVDVTGEILHGKTSELK-HDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSrvelg 173
Cdd:PRK13566 598 NLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFADPETLPDELLVTA----- 672
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 211584265 174 dASGKNIIMGVRHKEFAVEGVQFHPESILT---QYGRKMFRNFLELTAG 219
Cdd:PRK13566 673 -ETEDGVIMAIEHKTLPVAAVQFHPESIMTlggDVGLRIIENVVRLLAG 720
|
|
| PRK13957 |
PRK13957 |
indole-3-glycerol-phosphate synthase; Provisional |
239-494 |
6.39e-41 |
|
indole-3-glycerol-phosphate synthase; Provisional
Pssm-ID: 140013 Cd Length: 247 Bit Score: 150.42 E-value: 6.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 239 ILDKIYAHRKNavdEQKKIPALRPEALQAaydlniappqLSFPDRLRQSDYplSLMAEIKRASPSKGIISANVCAPAQAR 318
Cdd:PRK13957 4 VLREIIETKQN---EIEKISRWDPLPDRG----------LPLRDSLKSRSF--SIIAECKRKSPSAGELRADYHPVQIAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 319 EYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEgLPnrpaVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTRL 398
Cdd:PRK13957 69 TYETLGASAISVLTDQSYFGGSLEDLKSVSSELK-IP----VLRKDFILDEIQIREARAFGASAILLIVRILTPSQIKSF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 399 YHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKKE 478
Cdd:PRK13957 144 LKHASSLGMDVLVEVHTEDEAKLALDCGAEIIGINTRDLDTFQIHQNLVEEVAAFLPPNIVKVGESGIESRSDLDKFRKL 223
|
250
....*....|....*.
gi 211584265 479 gVKAILVGEALMRAPD 494
Cdd:PRK13957 224 -VDAALIGTYFMEKKD 238
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
518-749 |
3.14e-40 |
|
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; Phosphoribosylanthranilate isomerase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439905 Cd Length: 208 Bit Score: 146.82 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 518 PLVKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVkstprpadtlqqpssatslewfdhstnilrh 597
Cdd:COG0135 2 TRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAAL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 598 PSRALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLEW----SSLIPVPVIRKFAPGDIGIARRAYHTLP-----LLD 668
Cdd:COG0135 51 PPFVKKVGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYcaalRERLGLPVIKAIRVGDGADLEEAAAYAPvadalLLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 669 SGA----GGSGELLEESGVKKVldsDEGLRVILAGGLNPDNVAGTVKKLGqsgqkVVGLDVSSGVET-NGAQDLEKIRAF 743
Cdd:COG0135 131 AKVpglyGGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVR-----PYGVDVSSGVESaPGVKDPDKIRAF 202
|
....*.
gi 211584265 744 VKSAKS 749
Cdd:COG0135 203 VEAVRA 208
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
22-206 |
9.23e-34 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 128.42 E-value: 9.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 22 SNVILIDNYDSFTWNIYQYLVLEGATVTVYRNdEVTVEDLVAKKPTQLVISPGPGHPdTDAGISNAVIKHFSGKVPIFGV 101
Cdd:PRK05637 2 THVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHP-RDAGNMMALIDRTLGQIPLLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 102 CMGQQCMITSFGGKVDVTGEIlHGKTSELKHDSKG----VYQGLPTSLE------------VTRYHSLAGTHstIPDCLE 165
Cdd:PRK05637 80 CLGFQALLEHHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLATDVEpdhpeipgrkvpIARYHSLGCVV--APDGME 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 211584265 166 V--TSRVELGDasgknIIMGVRHKEFAVEGVQFHPESILTQYG 206
Cdd:PRK05637 157 SlgTCSSEIGP-----VIMAAETTDGKAIGLQFHPESVLSPTG 194
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
25-221 |
5.90e-33 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 136.52 E-value: 5.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 25 ILIDNYDSFTWNIYQYL-VLEGATVTVYRNDEVTVED----LVAKKP-TQLVISPGPGHP--DTDAGISNAVIKHfSGKV 96
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELsIVNGVPPVVVRNDEWTWEEvyhyLYEEKAfDNIVISPGPGSPtcPADIGICLRLLLE-CRDI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 97 PIFGVCMGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLP----TSLEVTRYHSL------------------- 153
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLvidaeslpkelvpiawtss 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 154 AGTHS--------TIPDCLE-----------VTSRVELGDAS---------GKNIIMGVRHKEFAVEGVQFHPESILTQY 205
Cdd:PLN02889 244 SDTLSflesqksgLVPDAYEsqigqsgssdpFSSKLKNGTSWpsshsermqNGKILMGIMHSTRPHYGLQFHPESIATCY 323
|
250
....*....|....*.
gi 211584265 206 GRKMFRNFLELTAGTW 221
Cdd:PLN02889 324 GRQIFKNFREITQDYW 339
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
520-749 |
1.70e-32 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 124.92 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 520 VKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVkstprpadtlqqpssatslewfdhstnilrhPS 599
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAAL-------------------------------PP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 600 RALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLE----WSSLIPVPVIRKF---APGDIGIARRAYHT--LPLLDSG 670
Cdd:PRK01222 54 FVKVVGVFVNASDEEIDEIVETVPLDLLQLHGDETPEfcrqLKRRYGLPVIKALrvrSAGDLEAAAAYYGDadGLLLDAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 671 A---GGSGELLEESgvkkVLDSDEGLRVILAGGLNPDNVAGTVKKLGQSgqkvvGLDVSSGVET-NGAQDLEKIRAFVKS 746
Cdd:PRK01222 134 VglpGGTGKTFDWS----LLPAGLAKPWILAGGLNPDNVAEAIRQVRPY-----GVDVSSGVESaPGIKDPEKIRAFIEA 204
|
...
gi 211584265 747 AKS 749
Cdd:PRK01222 205 VKS 207
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
21-216 |
4.29e-32 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 123.31 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 21 ASNVILIDNYDSFTWNIYQYLVLEGATVTVyrndeVTVEDLV---AKKPTQLVISPGPGHPDTDAGISNAVIKHFSGKvP 97
Cdd:PRK06895 1 ATKLLIINNHDSFTFNLVDLIRKLGVPMQV-----VNVEDLDldeVENFSHILISPGPDVPRAYPQLFAMLERYHQHK-S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 98 IFGVCMGQQCMITSFGGKVDVTGEILHGKTSELKHDSKG-VYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVElgdas 176
Cdd:PRK06895 75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSpLFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCD----- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 211584265 177 gKNIIMGVRHKEFAVEGVQFHPESILTQYGRKMFRNFLEL 216
Cdd:PRK06895 150 -ENVVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWLAI 188
|
|
| PLN02363 |
PLN02363 |
phosphoribosylanthranilate isomerase |
505-751 |
7.03e-28 |
|
phosphoribosylanthranilate isomerase
Pssm-ID: 215207 Cd Length: 256 Bit Score: 113.03 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 505 GSNQNFAGASPSS----PLVKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVKStprpadtlqqps 580
Cdd:PLN02363 30 VSSENVAPKDDERgkdrPLVKMCGITSARDAAMAVEAGADFIGMILWPKSKRSISLSVAKEISQVARE------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 581 satslewfdhstnilrhpSRALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLEWSSLIP--VPVIRKFAPGDIGIAR 658
Cdd:PLN02363 98 ------------------GGAKPVGVFVDDDANTILRAADSSDLELVQLHGNGSRAAFSRLVreRKVIYVLNANEDGKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 659 RAYHTLP-------LLDSGAGGSGELLEESGVK-KVLDSDEGLrvILAGGLNPDNVAGTVkklgqSGQKVVGLDVSSGVE 730
Cdd:PLN02363 160 NVVPEEDchladwiLVDSATGGSGKGFNWQNFKlPSVRSRNGW--LLAGGLTPENVHEAV-----SLLKPTGVDVSSGIC 232
|
250 260
....*....|....*....|...
gi 211584265 731 -TNGAQ-DLEKIRAFVKSAKSIR 751
Cdd:PLN02363 233 gPDGIRkDPSKISSFISAVKSVA 255
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
23-216 |
2.39e-26 |
|
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: 115.39 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 23 NVILIDNYDSFTWNIYQYL--VLE-GATVTVYRNDEVTvEDLVAKKP--TQLVISPGPGHPDT--DAGISNAVIK-HFSG 94
Cdd:TIGR01823 7 HVLFIDSYDSFTYNVVRLLeqQTDiSVHVTTVHSDTFQ-DQLLELLPlfDAIVVGPGPGNPNNaqDMGIISELWElANLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 95 KVPIFGVCMGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLpTSLEVTRYHSL----AGTHSTIPDCLevtsrv 170
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLyanpEGIDTLLPLCL------ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 211584265 171 eLGDASGkNIIMGVRHKEFAVEGVQFHPESILTQYGR-KMFRNFLEL 216
Cdd:TIGR01823 159 -TEDEEG-IILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKL 203
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
55-214 |
3.24e-20 |
|
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: 88.75 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 55 EVTVEDLVAKKPTQLVISPGPgHPDTDAGISNAVIKHFSGKVPIFGVCMGQQCMITSFGGKVD--VTGEilHGKTSELKH 132
Cdd:cd01742 31 TTPLEEIKLKNPKGIILSGGP-SSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVErgDKRE--YGKAEIEID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 133 DSKGVYQGLPTSLEVtryhsLAgTH----STIPDCLEVTSRvelgdaSGKNIIMGVRHKEFAVEGVQFHPESILTQYGRK 208
Cdd:cd01742 108 DSSPLFEGLPDEQTV-----WM-SHgdevVKLPEGFKVIAS------SDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKE 175
|
....*.
gi 211584265 209 MFRNFL 214
Cdd:cd01742 176 ILKNFL 181
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
56-219 |
6.03e-18 |
|
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: 82.36 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 56 VTVEDLVAKKPTQLVISPGP------GHPDTDAGISNAvikhfsgKVPIFGVCMGQQCMITSFGGKVDVTGEILHGKTS- 128
Cdd:TIGR00888 32 TPLEEIREKNPKGIILSGGPssvyaeNAPRADEKIFEL-------GVPVLGICYGMQLMAKQLGGEVGRAEKREYGKAEl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 129 ELKHDSKgVYQGLPTSLEVTRYHSLAGTHstIPDCLEVTSRvelgdaSGKNIIMGVRHKEFAVEGVQFHPESILTQYGRK 208
Cdd:TIGR00888 105 EILDEDD-LFRGLPDESTVWMSHGDKVKE--LPEGFKVLAT------SDNCPVAAMAHEEKPIYGVQFHPEVTHTEYGNE 175
|
170
....*....|.
gi 211584265 209 MFRNFLELTAG 219
Cdd:TIGR00888 176 LLENFVYDVCG 186
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
24-216 |
7.34e-18 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 82.21 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTWNIY---QYLVLEGATVTvyrnDEVTVEDLVAKKpTQLVISpgpGHPDTD-AGISNAVIKHFsgKVPIF 99
Cdd:PRK00758 2 IVVVDNGGQYNHLIHrtlRYLGVDAKIIP----NTTPVEEIKAFE-DGLILS---GGPDIErAGNCPEYLKEL--DVPIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 100 GVCMGQQCMITSFGGKV---------DVTGEILhgktselkhDSKGVYQGLPTSLEVTRYHslAGTHSTIPDCLEVTSRV 170
Cdd:PRK00758 72 GICLGHQLIAKAFGGEVgrgeygeyaLVEVEIL---------DEDDILKGLPPEIRVWASH--ADEVKELPDGFEILARS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 211584265 171 ELGDasgkniIMGVRHKEFAVEGVQFHPESILTQYGRKMFRNFLEL 216
Cdd:PRK00758 141 DICE------VEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFLEI 180
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
517-750 |
4.66e-16 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 82.17 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 517 SPLVKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVAlgISRVVKSTPrpadtlqqpssatslewfdhstnilr 596
Cdd:PRK13803 2 QPKIKICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVGNKFL--APNLEKAIR-------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 597 hPSRALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSE----PLEWSSLI--PVPVIRKFAPGDIGI-----ARRAYHTLP 665
Cdd:PRK13803 54 -KAGGRPVGVFVNESAKAMLKFSKKNGIDFVQLHGAEskaePAYCQRIYkkSIKKIGSFLIDDAFGfevldEYRDHVKYF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 666 LLDS---GAGGSGELLEesgVKKVLDSDEGLRVILAGGLNPDNVAgTVKKLGQSgqKVVGLDVSSGVE-TNGAQDLEKIR 741
Cdd:PRK13803 133 LFDNktkIYGGSGKSFD---WEKFYNYNFKFPFFLSGGLSPTNFD-RIINLTHP--QILGIDVSSGFEdSPGNKKLTLLK 206
|
....*....
gi 211584265 742 AFVKSAKSI 750
Cdd:PRK13803 207 SFITNVKKK 215
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
35-200 |
3.20e-15 |
|
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: 74.07 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 35 WNIYQYLVLEGATVTVYRNDeVTVEDLVAKKPTQLVISPGPGHP-DTDAGISNaVIKHFSGKVPIFGVCMGQQcmitsfg 113
Cdd:cd01744 10 HNILRELLKRGCEVTVVPYN-TDAEEILKLDPDGIFLSNGPGDPaLLDEAIKT-VRKLLGKKIPIFGICLGHQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 114 gkvdVTGEILHGKTSELKHDSKG----VYQGLPTSLEVT-RYHSLAGTHSTIPDCLEVTsRVELGDasgkNIIMGVRHKE 188
Cdd:cd01744 81 ----LLALALGAKTYKMKFGHRGsnhpVKDLITGRVYITsQNHGYAVDPDSLPGGLEVT-HVNLND----GTVEGIRHKD 151
|
170
....*....|..
gi 211584265 189 FAVEGVQFHPES 200
Cdd:cd01744 152 LPVFSVQFHPEA 163
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
55-222 |
7.73e-15 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 77.78 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 55 EVTVEDLVAKKPTQLVISPGP------GHPDTDAGIsnavikhFSGKVPIFGVCMGQQCMITSFGGKVDVTGEILHGKTS 128
Cdd:PRK00074 36 DISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEI-------FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 129 ELKHDSKGVYQGLPTSLEVTRYHslaGTH-STIPDCLEVTsrvelgdASGKNI-IMGVRHKEFAVEGVQFHPESILTQYG 206
Cdd:PRK00074 109 LEVDNDSPLFKGLPEEQDVWMSH---GDKvTELPEGFKVI-------ASTENCpIAAIANEERKFYGVQFHPEVTHTPQG 178
|
170
....*....|....*....
gi 211584265 207 RKMFRNFLELTAG---TWD 222
Cdd:PRK00074 179 KKLLENFVFDICGckgDWT 197
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
35-200 |
6.85e-13 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 70.87 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 35 WNIYQYLVLEGATVTVYRNDeVTVEDLVAKKPTQLVISPGPGHP-DTDAGISNavIKHF-SGKVPIFGVCMGQQCMITSF 112
Cdd:PRK12564 189 RNILRELAERGCRVTVVPAT-TTAEEILALNPDGVFLSNGPGDPaALDYAIEM--IRELlEKKIPIFGICLGHQLLALAL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 113 GgkvdvtgeilhGKTSELKH------------DSKGVY---QGlptslevtryHSLAGTHSTIPDCLEVTsRVELGDasg 177
Cdd:PRK12564 266 G-----------AKTYKMKFghrganhpvkdlETGKVEitsQN----------HGFAVDEDSLPANLEVT-HVNLND--- 320
|
170 180
....*....|....*....|...
gi 211584265 178 kNIIMGVRHKEFAVEGVQFHPES 200
Cdd:PRK12564 321 -GTVEGLRHKDLPAFSVQYHPEA 342
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
35-200 |
9.89e-11 |
|
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: 64.27 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 35 WNIYQYLVLEGATVTVYRNDeVTVEDLVAKKPTQLVISPGPGHP-DTDAGIsnAVIKHFSGK-VPIFGVCMGQQCMITSF 112
Cdd:COG0505 188 RNILRELAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPaALDYAI--ETIRELLGKgIPIFGICLGHQLLALAL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 113 GgkvdvtgeilhGKTSELKH------------DSKGVY---QGlptslevtryHSLAGTHSTIPD-CLEVTsRVELGDas 176
Cdd:COG0505 265 G-----------AKTYKLKFghrganhpvkdlETGRVEitsQN----------HGFAVDEDSLPAtDLEVT-HVNLND-- 320
|
170 180
....*....|....*....|....
gi 211584265 177 gkNIIMGVRHKEFAVEGVQFHPES 200
Cdd:COG0505 321 --GTVEGLRHKDLPAFSVQYHPEA 342
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
25-216 |
1.05e-10 |
|
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: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 25 ILI----DNYDSFTWNIYQYLVLEGATVTVYR--NDEVTVEDLVAKKPTQLVISPGPGHP-DTDAGISNA--VIKH-FSG 94
Cdd:COG0518 2 ILIldhdPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVyDEDPWLEDEpaLIREaFEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 95 KVPIFGVCMGQQCMITSFGGKVDVTG--EIlhGKTSELKHDSKGVYQGLPTSLEVtrYHSlagtH----STIPDCLEVTs 168
Cdd:COG0518 82 GKPVLGICYGAQLLAHALGGKVEPGPgrEI--GWAPVELTEADPLFAGLPDEFTV--WMS----HgdtvTELPEGAEVL- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211584265 169 rvelgdASGKNI-IMGVRHKEFAVeGVQFHPE------------------------------SILTQYGRKMFRNFLEL 216
Cdd:COG0518 153 ------ASSDNCpNQAFRYGRRVY-GVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
36-200 |
1.41e-10 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 63.84 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 36 NIYQYLVLEGATVTVYRNDEVTVEDLvAKKPTQLVISPGPGHPdtdAGISNAV--IKHFSGKVPIFGVCMGQQCMitsfg 113
Cdd:PLN02771 253 NILRRLASYGCKITVVPSTWPASEAL-KMKPDGVLFSNGPGDP---SAVPYAVetVKELLGKVPVFGICMGHQLL----- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 114 gkvdvtGEILHGKTSELKHDSKG----VYQGLPTSLEVT-RYHSLAGTHSTIPDCLEVTsRVELGDASgkniIMGVRHKE 188
Cdd:PLN02771 324 ------GQALGGKTFKMKFGHHGgnhpVRNNRTGRVEISaQNHNYAVDPASLPEGVEVT-HVNLNDGS----CAGLAFPA 392
|
170
....*....|..
gi 211584265 189 FAVEGVQFHPES 200
Cdd:PLN02771 393 LNVMSLQYHPEA 404
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
24-200 |
2.61e-10 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 62.89 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNydSFTWNIYQYLVLEGATVTVYrNDEVTVEDLVAKKPTQLVISPGPGHPDT-DAGISNaVIKHFSGKVPIFGVC 102
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAiHYGIKT-VKKLLKYNIPIFGIC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 103 MGQQCMITSFGgkvdvtgeilhGKTSELKHDSKGVYQ--GLPTSLEVT-RYHSLA-GTHSTIPDCLEVTsRVELGDASgk 178
Cdd:CHL00197 271 MGHQILSLALE-----------AKTFKLKFGHRGLNHpsGLNQQVEITsQNHGFAvNLESLAKNKFYIT-HFNLNDGT-- 336
|
170 180
....*....|....*....|..
gi 211584265 179 niIMGVRHKEFAVEGVQFHPES 200
Cdd:CHL00197 337 --VAGISHSPKPYFSVQYHPEA 356
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
36-199 |
3.41e-10 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 62.22 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 36 NIYQYLVLEGATVTVYRNDeVTVEDLVAKKPTQLVISPGPGHPDTDAGISNAVIKHFSGkVPIFGVCMGQQCMITSFGgk 115
Cdd:PRK12838 180 SILRSLSKRGCKVTVLPYD-TSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISS-YPILGICLGHQLIALALG-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 116 vdvtgeilhGKTSELKHDSKG------------VYQglpTSlevtRYHSLAGTHSTIPDCLEVTSRVELGDASgkniIMG 183
Cdd:PRK12838 256 ---------ADTEKLPFGHRGanhpvidlttgrVWM---TS----QNHGYVVDEDSLDGTPLSVRFFNVNDGS----IEG 315
|
170
....*....|....*.
gi 211584265 184 VRHKEFAVEGVQFHPE 199
Cdd:PRK12838 316 LRHKKKPVLSVQFHPE 331
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
24-114 |
1.27e-09 |
|
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: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTW---NIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQ-LVISPGPGHPDT---DAGISNAVIKHFSGKV 96
Cdd:cd01653 1 VAVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVESDVDLDDYDgLILPGGPGTPDDlarDEALLALLREAAAAGK 80
|
90
....*....|....*...
gi 211584265 97 PIFGVCMGQQCMITSFGG 114
Cdd:cd01653 81 PILGICLGAQLLVLGVQF 98
|
|
| PRK13958 |
PRK13958 |
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional |
520-748 |
5.96e-09 |
|
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
Pssm-ID: 184418 Cd Length: 207 Bit Score: 56.66 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 520 VKICGTRTEEGALAAIQAGADLIGII------------MVQGRSRLVPDDvalgISRVVkstprpadtlqqpssatslew 587
Cdd:PRK13958 3 LKFCGFTTIKDVTAASQLPIDAIGFIhyekskrhqtitQIKKLASAVPNH----IDKVC--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 588 fdhstnILRHPSRALLvgvfmNQPLSYVvsqqqklGLDVVQLHGSEPLEWSSLIP-----VPVIRKFAPGDIGIARRAYH 662
Cdd:PRK13958 58 ------VVVNPDLTTI-----EHILSNT-------SINTIQLHGTESIDFIQEIKkkyssIKIIKALPADENIIQNINKY 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 663 T----LPLLDSGA---GGSGELLEEsgvkKVLDSDEGLRVILAGGLNPDNVagtvKKLGQSGQKVVGLDVSSGVETNGAQ 735
Cdd:PRK13958 120 KgfvdLFIIDTPSvsyGGTGQTYDW----TILKHIKDIPYLIAGGINSENI----QTVEQLKLSHQGYDIASGIETNGRK 191
|
250
....*....|...
gi 211584265 736 DLEKIRAFVKSAK 748
Cdd:PRK13958 192 DINKMTAIVNIVK 204
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
24-108 |
2.90e-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: 51.82 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 24 VILIDNYDSFTW---NIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQ-LVISPGPGHPDT---DAGISNAVIKHFSGKV 96
Cdd:cd03128 1 VAVLLFGGSEELelaSPLDALREAGAEVDVVSPDGGPVESDVDLDDYDgLILPGGPGTPDDlawDEALLALLREAAAAGK 80
|
90
....*....|..
gi 211584265 97 PIFGVCMGQQCM 108
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
56-214 |
4.70e-08 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 56.23 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 56 VTVEDLVAKKPTQLVISPGPG--HPDTDAGISNAVIKHF-SGKVPIFGVCMGQQCMITSFGGKVDVTGEILHGKTSELKH 132
Cdd:PLN02347 44 ASLDRIASLNPRVVILSGGPHsvHVEGAPTVPEGFFDYCrERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 133 DSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDasgkniIMGVRHKEFAVEGVQFHPESILTQYGRKMFRN 212
Cdd:PLN02347 124 CGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGA------VVAIENRERRIYGLQYHPEVTHSPKGMETLRH 197
|
..
gi 211584265 213 FL 214
Cdd:PLN02347 198 FL 199
|
|
| hisH |
PRK14004 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
48-216 |
5.28e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 44.89 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 48 VTVYRNDEVTVEDLVAKKPTQLVISPGPGHPD------TDAGISNAVIKHFSGKVPIFGVCMGQQCMI-----TSFGGKV 116
Cdd:PRK14004 19 VSLYTKDFVFTSDPETIENSKALILPGDGHFDkamenlNSTGLRSTIDKHVESGKPLFGICIGFQILFesseeTNQGTKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 117 D-------VTGEI--LHGKTSELKH-----------DSKGVYQGLPTslEVTRYHslagTHSTIPDCLEVTSRVELGDAS 176
Cdd:PRK14004 99 EqieglgyIKGKIkkFEGKDFKVPHigwnrlqirrkDKSKLLKGIGD--QSFFYF----IHSYRPTGAEGNAITGLCDYY 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 211584265 177 GKNiIMGVRHKEfAVEGVQFHPESILTqYGRKMFRNFLEL 216
Cdd:PRK14004 173 QEK-FPAVVEKE-NIFGTQFHPEKSHT-HGLKLLENFIEF 209
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
95-215 |
1.09e-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: 44.39 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 95 KVPIFGVCMGQQCMITSFGGKV------DVTGEILHGKTSELKHDSKGVyqglptSLEV-TRYHSLAGTHS--------- 158
Cdd:COG2071 96 GKPVLGICRGMQLLNVALGGTLyqdlpdQVPGALDHRQPAPRYAPRHTV------EIEPgSRLARILGEEEirvnslhhq 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211584265 159 ---TIPDCLEVTSRvelgDASGknIIMGVRHKE--FAVeGVQFHPESILTQYG--RKMFRNFLE 215
Cdd:COG2071 170 avkRLGPGLRVSAR----APDG--VIEAIESPGapFVL-GVQWHPEWLAASDPlsRRLFEAFVE 226
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
95-213 |
6.02e-04 |
|
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: 41.41 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 95 KVPIFGVCMGQQCMITSFGGKvdvtgeilhgktselkhdskgVYQglptSLEVTRYHSLAgtHSTIPDCLEVTSRVELGd 174
Cdd:cd01745 100 GKPILGICRGMQLLNVALGGT---------------------LYQ----DIRVNSLHHQA--IKRLADGLRVEARAPDG- 151
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 211584265 175 asgknIIMGVRHKEFA-VEGVQFHPESILTQY--GRKMFRNF 213
Cdd:cd01745 152 -----VIEAIESPDRPfVLGVQWHPEWLADTDpdSLKLFEAF 188
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
95-199 |
1.55e-03 |
|
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: 40.70 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211584265 95 KVPIFGVCMGQQCMITSFGG----KVDVTGEILHGktseLKHDSKGVYQG----------------LPTSLEVTRYHsla 154
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGtlyqDIQEQPGFTDH----REHCQVAPYAPshavnvepgsllasllGSEEFRVNSLH--- 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 211584265 155 gtHSTI---PDCLEVTSRvelgDASGknIIMGVR---HKEFAVeGVQFHPE 199
Cdd:pfam07722 178 --HQAIdrlAPGLRVEAV----APDG--TIEAIEspnAKGFAL-GVQWHPE 219
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
442-489 |
7.15e-03 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 38.79 E-value: 7.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 211584265 442 VDLGTTSRLMDQVPEStiVCALSGISGPQDVEAYKKEGVKAILVGEAL 489
Cdd:cd04723 176 PDLELLERLAARADIP--VIAAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| |
