|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
256-517 |
4.70e-131 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 389.35 E-value: 4.70e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 256 LERIYDHRRAAVAVQKTIPSQrpADLQAAYDlnlAPPQVPFPARLRQSPYPLSLMAEIKRASPSKGMIAENACAPAQARQ 335
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPL--ADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 336 YAKAGASVISVLTEPEWFKGSIDDLRAVRQSLEGLtnrpaILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLTRLY 415
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 416 HYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYKKEG 495
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 350629793 496 VKAILVGEALMRAADTAAFIAE 517
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
254-519 |
4.43e-109 |
|
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: 332.76 E-value: 4.43e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 254 SILERIYDHRRAAVAVQKtipSQRP-ADLQAAydLNLAPPQVPFPARLRQSPyPLSLMAEIKRASPSKGMIAENACAPAQ 332
Cdd:COG0134 2 TILDKIVAHKREEVAARK---ARVPlAELEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 333 ARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSleglTNRPaILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLT 412
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAA----VDLP-VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 413 RLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYK 492
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*..
gi 350629793 493 KEGVKAILVGEALMRAADTAAFIAELL 519
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALRELL 257
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
296-518 |
4.05e-108 |
|
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: 328.65 E-value: 4.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 296 FPARLRQSPYpLSLMAEIKRASPSKGMIAENACAPAQARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSLegltnRPA 375
Cdd:cd00331 1 FKAALKRPGG-LGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 376 ILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTS 455
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350629793 456 FEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYKKEGVKAILVGEALMRAADTAAFIAEL 518
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
254-521 |
1.68e-106 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 326.34 E-value: 1.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 254 SILERIYDHRRAAVAVQKtipSQRP-ADLQAAydLNLAPPQVPFPARLRQSPypLSLMAEIKRASPSKGMIAENACAPAQ 332
Cdd:PRK00278 3 DILDKIVAYKREEVAARK---AQVPlAELKAR--AAAAPPPRDFAAALRAGK--PAVIAEVKKASPSKGVIREDFDPVEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 333 ARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSleglTNRPaILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLT 412
Cdd:PRK00278 76 AKAYEAGGAACLSVLTDERFFQGSLEYLRAARAA----VSLP-VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 413 RLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYK 492
Cdd:PRK00278 151 ELLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRLA 230
|
250 260
....*....|....*....|....*....
gi 350629793 493 KEGVKAILVGEALMRAADTAAFIAELLGG 521
Cdd:PRK00278 231 KAGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
26-221 |
2.85e-102 |
|
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: 312.36 E-value: 2.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPE-EAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqlTDDsnkDVIMG 185
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAW---TED---GEIMG 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFLKLTAG 221
Cdd:COG0512 154 IRHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
25-220 |
6.06e-97 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 298.58 E-value: 6.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 25 NVILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVC 104
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPA-EAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 105 MGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSsvqLTDDsnkDVIM 184
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTA---WTDD---GEIM 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 350629793 185 GVRHKKLAVEGVQFHPESILTEYGRTMFRNFLKLTA 220
Cdd:PRK05670 154 GVRHKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
26-216 |
2.28e-91 |
|
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: 284.04 E-value: 2.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPE-DAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqlTDDsnkDVIMG 185
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAS---TED---GVIMA 153
|
170 180 190
....*....|....*....|....*....|.
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:cd01743 154 LRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
26-218 |
1.09e-69 |
|
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: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPN-EAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSsvqlTDDSNkDVIMG 185
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTA----WEEEN-IEIMA 155
|
170 180 190
....*....|....*....|....*....|...
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFLKL 218
Cdd:TIGR00566 156 IRHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
27-216 |
3.31e-62 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 206.70 E-value: 3.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 27 ILIDNYDSFTWNVYQYLVLEGATVNVFRNDqITLEELIAKKPTQLVISPGPGHPeTDAGISSAAIQY-FSGKIPIFGVCM 105
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSP-GAAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTG-EILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSsvqltDDSNKDVIM 184
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTA-----TSENDGTIM 153
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 185 GVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:pfam00117 154 GIRHKKLPIFGVQFHPESILTPHGPEILFNFF 185
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
570-765 |
1.05e-61 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 205.66 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 570 VPDDVALRISQVVKSTPKPAgqtPPTSQGTPAAASVEYFDHSARILRHPSRALLVGVFQNQPLDYILSQQQKLGLDVVQL 649
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKAGA---DYLGLIFSESSKRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 650 HGSEPLEWAKLIP--VPVIRKF----GLDEPAIARRAYH-SLPLLDSGVGGTGELLDQSRVQNVLdkDSGLRVILAGGLD 722
Cdd:pfam00697 78 HGDEDQEYENLLPtgVPVIKAIwvpdSVDTVDIARRADHvDLPLLDSGAGGTGELFDWSLVSKWL--KSGLKVILAGGLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 350629793 723 PTNVAGIVQKLG------ESGrkvvgvdvssgVESDGAQDVGKIRAFVQ 765
Cdd:pfam00697 156 PDNVVEAIKTPGvigvdvSSG-----------VETNGIKDLNKIRKFVQ 193
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
29-216 |
1.50e-56 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 191.78 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 29 IDNYDSFTWNVYQYL--VLEGATVNVFRNdQITLEELIAKKPTQLVISPGPGHPET--DAGISSAAIQYFSGKIPIFGVC 104
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKNdrDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 105 MGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGThaTIPDCLEVSSSvqlTDDSNKDVIM 184
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTAT---TDHDGEELVM 155
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 185 GVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:NF041322 156 GIRHREHPIECVQFHPESVLTGVGHDVIENFL 187
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
536-767 |
5.93e-33 |
|
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: 126.15 E-value: 5.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 536 VKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVPDDVALRISQVVKSTPKPagqtpptsqgtpaaasveyfdhsaril 615
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKR--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 616 rhpsrallVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLEWAKLIP----VPVIRKFGLDEP-----AIARRAYHSLPL 686
Cdd:cd00405 54 --------VGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYCAQLRarlgLPVIKAIRVKDEedlekAAAYAGEVDAIL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 687 LDSGV----GGTGELLDQSRVQNVldkDSGLRVILAGGLDPTNVAGIVQKLG----------ESgrkvvgvdvssgveSD 752
Cdd:cd00405 126 LDSKSggggGGTGKTFDWSLLRGL---ASRKPVILAGGLTPDNVAEAIRLVRpygvdvssgvET--------------SP 188
|
250
....*....|....*
gi 350629793 753 GAQDVGKIRAFVQAV 767
Cdd:cd00405 189 GIKDPEKIRAFIEAA 203
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
534-769 |
1.89e-28 |
|
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: 113.31 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 534 PLVKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVPDDVALRISQVVkstpkpagqtpptsqgtpaaasveyfdhsar 613
Cdd:COG0135 2 TRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAAL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 614 ilrhPSRALLVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLEW----AKLIPVPVIRKFGLDEPAIARRAYHSLP---- 685
Cdd:COG0135 51 ----PPFVKKVGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYcaalRERLGLPVIKAIRVGDGADLEEAAAYAPvada 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 686 -LLDSGV----GGTGELLDQSRVQNVldkDSGLRVILAGGLDPTNVAGIVQKLG----------ES--GRKvvgvdvssg 748
Cdd:COG0135 127 lLLDAKVpglyGGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVRpygvdvssgvESapGVK--------- 194
|
250 260
....*....|....*....|.
gi 350629793 749 vesdgaqDVGKIRAFVQAVRG 769
Cdd:COG0135 195 -------DPDKIRAFVEAVRA 208
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
536-770 |
7.27e-21 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 91.41 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 536 VKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVpddvalrisqvvkstpkpagqtpptsqgTPAAAsveyfdhsARIL 615
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYV----------------------------SPEQA--------AELA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 616 R-HPSRALLVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLE----WAKLIPVPVIRKFGLDEPAIARRAYHSLP----- 685
Cdd:PRK01222 49 AaLPPFVKVVGVFVNASDEEIDEIVETVPLDLLQLHGDETPEfcrqLKRRYGLPVIKALRVRSAGDLEAAAAYYGdadgl 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 686 LLDSGV---GGTGELLDQSrvqnVLDKDSGLRVILAGGLDPTNVAGIVQKLG----------ESgrkvvgvdvssgveSD 752
Cdd:PRK01222 129 LLDAYVglpGGTGKTFDWS----LLPAGLAKPWILAGGLNPDNVAEAIRQVRpygvdvssgvES--------------AP 190
|
250
....*....|....*...
gi 350629793 753 GAQDVGKIRAFVQAVRGL 770
Cdd:PRK01222 191 GIKDPEKIRAFIEAVKSA 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
256-517 |
4.70e-131 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 389.35 E-value: 4.70e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 256 LERIYDHRRAAVAVQKTIPSQrpADLQAAYDlnlAPPQVPFPARLRQSPYPLSLMAEIKRASPSKGMIAENACAPAQARQ 335
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPL--ADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 336 YAKAGASVISVLTEPEWFKGSIDDLRAVRQSLEGLtnrpaILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLTRLY 415
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 416 HYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYKKEG 495
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 350629793 496 VKAILVGEALMRAADTAAFIAE 517
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
254-519 |
4.43e-109 |
|
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: 332.76 E-value: 4.43e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 254 SILERIYDHRRAAVAVQKtipSQRP-ADLQAAydLNLAPPQVPFPARLRQSPyPLSLMAEIKRASPSKGMIAENACAPAQ 332
Cdd:COG0134 2 TILDKIVAHKREEVAARK---ARVPlAELEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 333 ARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSleglTNRPaILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLT 412
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAA----VDLP-VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 413 RLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYK 492
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*..
gi 350629793 493 KEGVKAILVGEALMRAADTAAFIAELL 519
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALRELL 257
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
296-518 |
4.05e-108 |
|
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: 328.65 E-value: 4.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 296 FPARLRQSPYpLSLMAEIKRASPSKGMIAENACAPAQARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSLegltnRPA 375
Cdd:cd00331 1 FKAALKRPGG-LGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 376 ILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTS 455
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350629793 456 FEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYKKEGVKAILVGEALMRAADTAAFIAEL 518
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
254-521 |
1.68e-106 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 326.34 E-value: 1.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 254 SILERIYDHRRAAVAVQKtipSQRP-ADLQAAydLNLAPPQVPFPARLRQSPypLSLMAEIKRASPSKGMIAENACAPAQ 332
Cdd:PRK00278 3 DILDKIVAYKREEVAARK---AQVPlAELKAR--AAAAPPPRDFAAALRAGK--PAVIAEVKKASPSKGVIREDFDPVEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 333 ARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSleglTNRPaILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLT 412
Cdd:PRK00278 76 AKAYEAGGAACLSVLTDERFFQGSLEYLRAARAA----VSLP-VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 413 RLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYK 492
Cdd:PRK00278 151 ELLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRLA 230
|
250 260
....*....|....*....|....*....
gi 350629793 493 KEGVKAILVGEALMRAADTAAFIAELLGG 521
Cdd:PRK00278 231 KAGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
26-221 |
2.85e-102 |
|
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: 312.36 E-value: 2.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTPE-EAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqlTDDsnkDVIMG 185
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAW---TED---GEIMG 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFLKLTAG 221
Cdd:COG0512 154 IRHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
25-220 |
6.06e-97 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 298.58 E-value: 6.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 25 NVILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVC 104
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPA-EAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 105 MGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSsvqLTDDsnkDVIM 184
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTA---WTDD---GEIM 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 350629793 185 GVRHKKLAVEGVQFHPESILTEYGRTMFRNFLKLTA 220
Cdd:PRK05670 154 GVRHKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
26-216 |
2.28e-91 |
|
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: 284.04 E-value: 2.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPE-DAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqlTDDsnkDVIMG 185
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAS---TED---GVIMA 153
|
170 180 190
....*....|....*....|....*....|.
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:cd01743 154 LRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PRK09427 |
PRK09427 |
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
251-727 |
2.52e-80 |
|
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;
Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 264.75 E-value: 2.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 251 KKLSILERIYDHRRAAVAVQKTipsQRP-ADLQAaydlNLAPPQVPFPARLRQSPYplSLMAEIKRASPSKGMIAENACA 329
Cdd:PRK09427 2 MMPTVLAKIVADKAIWVAARKQ---QQPlASFQN----EIQPSDRSFYDALKGPKT--AFILECKKASPSKGLIRDDFDP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 330 PAQARQYaKAGASVISVLTEPEWFKGSIDDLRAVRQSleglTNRPaILRKEFVFDEYQILEARLAGADTVLLivkMLSV- 408
Cdd:PRK09427 73 AEIARVY-KHYASAISVLTDEKYFQGSFDFLPIVRAI----VTQP-ILCKDFIIDPYQIYLARYYGADAILL---MLSVl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 409 --ELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPK 486
Cdd:PRK09427 144 ddEQYRQLAAVAHSLNMGVLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPADVIVISESGIYTHA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 487 DVEAYKKeGVKAILVGEALMRAADTAAFIAELLGGssQNvskesrssplvKICGTRSEEAARAAIEAGADLIGIIMVQGR 566
Cdd:PRK09427 224 QVRELSP-FANGFLIGSSLMAEDDLELAVRKLILG--EN-----------KVCGLTRPQDAKAAYDAGAVYGGLIFVEKS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 567 TRCVpddvalrisqvvkstpkpagqTPPTSQGTPAAASVEYfdhsarilrhpsrallVGVFQNQPLDYILSQQQKLGLDV 646
Cdd:PRK09427 290 PRYV---------------------SLEQAQEIIAAAPLRY----------------VGVFRNADIEDIVDIAKQLSLAA 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 647 VQLHGSEPLEW----AKLIPVPV-IRK-FGLDEPAIARRAYH-SLPLLDSGVGGTGELLDQSRVQNVLdKDsglRVILAG 719
Cdd:PRK09427 333 VQLHGDEDQAYidalREALPKTCqIWKaISVGDTLPARDLQHvDRYLLDNGQGGTGQTFDWSLLPGQS-LD---NVLLAG 408
|
....*...
gi 350629793 720 GLDPTNVA 727
Cdd:PRK09427 409 GLNPDNCQ 416
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
26-216 |
3.88e-76 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 255.80 E-value: 3.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLV-LEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVC 104
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGeLGPEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPE-EAGISVEVIRHFSGKVPILGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 105 MGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqlTDDSNkdvIM 184
Cdd:PRK14607 81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAK---SDDGE---IM 154
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 185 GVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:PRK14607 155 GIRHKEHPIFGVQFHPESILTEEGKRILKNFL 186
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
26-218 |
1.09e-69 |
|
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: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPN-EAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSsvqlTDDSNkDVIMG 185
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTA----WEEEN-IEIMA 155
|
170 180 190
....*....|....*....|....*....|...
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFLKL 218
Cdd:TIGR00566 156 IRHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
26-216 |
1.11e-69 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 227.07 E-value: 1.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTPN-EAGISLQAIEHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSVQLTDDSnKDVIMG 185
Cdd:PRK08857 81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGS-MDEIMG 159
|
170 180 190
....*....|....*....|....*....|.
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:PRK08857 160 FQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
26-217 |
1.24e-69 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 226.99 E-value: 1.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSPN-EAGISMEVIRYFAGKIPIFGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqltddSNKDVIMG 185
Cdd:PRK07649 81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSW------TEEGEIMA 154
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFLK 217
Cdd:PRK07649 155 IRHKTLPIEGVQFHPESIMTSHGKELLQNFIR 186
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
26-217 |
4.68e-69 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 225.51 E-value: 4.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTPN-EAGISLAVIRHFADKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSVQltDDSNKDVIMG 185
Cdd:PRK06774 81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSE--RGGEMDEIMG 158
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFLK 217
Cdd:PRK06774 159 IRHRTLPLEGVQFHPESILSEQGHQLLDNFLK 190
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
26-217 |
1.02e-66 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 219.02 E-value: 1.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPD-EAGISLDVIRHYAGRLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqltddSNKDVIMG 185
Cdd:PRK08007 81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAW------SETREIMG 154
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 186 VRHKKLAVEGVQFHPESILTEYGRTMFRNFLK 217
Cdd:PRK08007 155 IRHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
27-216 |
3.31e-62 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 206.70 E-value: 3.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 27 ILIDNYDSFTWNVYQYLVLEGATVNVFRNDqITLEELIAKKPTQLVISPGPGHPeTDAGISSAAIQY-FSGKIPIFGVCM 105
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSP-GAAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTG-EILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSsvqltDDSNKDVIM 184
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTA-----TSENDGTIM 153
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 185 GVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:pfam00117 154 GIRHKKLPIFGVQFHPESILTPHGPEILFNFF 185
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
570-765 |
1.05e-61 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 205.66 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 570 VPDDVALRISQVVKSTPKPAgqtPPTSQGTPAAASVEYFDHSARILRHPSRALLVGVFQNQPLDYILSQQQKLGLDVVQL 649
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKAGA---DYLGLIFSESSKRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 650 HGSEPLEWAKLIP--VPVIRKF----GLDEPAIARRAYH-SLPLLDSGVGGTGELLDQSRVQNVLdkDSGLRVILAGGLD 722
Cdd:pfam00697 78 HGDEDQEYENLLPtgVPVIKAIwvpdSVDTVDIARRADHvDLPLLDSGAGGTGELFDWSLVSKWL--KSGLKVILAGGLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 350629793 723 PTNVAGIVQKLG------ESGrkvvgvdvssgVESDGAQDVGKIRAFVQ 765
Cdd:pfam00697 156 PDNVVEAIKTPGvigvdvSSG-----------VETNGIKDLNKIRKFVQ 193
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
26-218 |
9.33e-61 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 204.26 E-value: 9.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTPQ-DSGISLQTVLELGPLVPLFGVCM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGK-VDVTGEILHGKTSALKHDGKGA---YEGLPDSLAVTRYHSLAGTHATIP-DCLEVSSsvqLTDDSnk 180
Cdd:PLN02335 100 GLQCIGEAFGGKiVRSPFGVMHGKSSPVHYDEKGEeglFSGLPNPFTAGRYHSLVIEKDTFPsDELEVTA---WTEDG-- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 350629793 181 dVIMGVRHKKLA-VEGVQFHPESILTEYGRTMFRNFLKL 218
Cdd:PLN02335 175 -LIMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKI 212
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
26-218 |
3.75e-60 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 201.50 E-value: 3.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPR-DSGISLDVISSYAPYIPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSsvqLTDDSnkdVIMG 185
Cdd:CHL00101 81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITA---WTEDG---LIMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 350629793 186 VRHKKL-AVEGVQFHPESILTEYGRTMFRNFLKL 218
Cdd:CHL00101 155 CRHKKYkMLRGIQFHPESLLTTHGQQILRNFLSL 188
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
26-216 |
5.13e-60 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 201.82 E-value: 5.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEEL--IAKKPTQLVISPGPGHPETdAGISSAAIQYFSG-KIPIFG 102
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEaaVAAQFDGVLLSPGPGTPER-AGASIDMVRACAAaGTPLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 103 VCMGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqlTDDSnkdV 182
Cdd:PRK07765 82 VCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTAR---TDSG---V 155
|
170 180 190
....*....|....*....|....*....|....
gi 350629793 183 IMGVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:PRK07765 156 IMAVRHRELPIHGVQFHPESVLTEGGHRMLANWL 189
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
29-216 |
1.50e-56 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 191.78 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 29 IDNYDSFTWNVYQYL--VLEGATVNVFRNdQITLEELIAKKPTQLVISPGPGHPET--DAGISSAAIQYFSGKIPIFGVC 104
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKNdrDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 105 MGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGThaTIPDCLEVSSSvqlTDDSNKDVIM 184
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVAT--EVPDCFEVTAT---TDHDGEELVM 155
|
170 180 190
....*....|....*....|....*....|..
gi 350629793 185 GVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:NF041322 156 GIRHREHPIECVQFHPESVLTGVGHDVIENFL 187
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
307-535 |
6.16e-48 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 181.00 E-value: 6.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 307 LSLMAEIKRASPSKGMIAENACAPAQARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSLegltnRPAILRKEFVFDEY 386
Cdd:PRK13802 50 IPVIAEIKRASPSKGHLSDIPDPAALAREYEQGGASAISVLTEGRRFLGSLDDFDKVRAAV-----HIPVLRKDFIVTDY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 387 QILEARLAGADTVLLIVKMLSVELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVNNRDLTSFEVDLGTTSRL 466
Cdd:PRK13802 125 QIWEARAHGADLVLLIVAALDDAQLKHLLDLAHELGMTVLVETHTREEIERAIAAGAKVIGINARNLKDLKVDVNKYNEL 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 350629793 467 MDQVPSSTIVCALSGISGPKDVEAYKKEGVKAILVGEALMRAADTAAFIAELLGGSSQnvSKESRSSPL 535
Cdd:PRK13802 205 AADLPDDVIKVAESGVFGAVEVEDYARAGADAVLVGEGVATADDHELAVERLVKAGAR--VKASETTPL 271
|
|
| PLN02460 |
PLN02460 |
indole-3-glycerol-phosphate synthase |
255-520 |
6.88e-48 |
|
indole-3-glycerol-phosphate synthase
Pssm-ID: 215254 Cd Length: 338 Bit Score: 173.04 E-value: 6.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 255 ILERIYDHRRAAVAVQKtipSQRPADLQAAYDLNlAPPQVPFPARLRQS----PYPlSLMAEIKRASPSKGMIAENACAP 330
Cdd:PLN02460 68 ILEEIVWYKDVEVAQMK---ERKPLYLLKKALQN-APPARDFVGALRAAhkrtGQP-GLIAEVKKASPSRGVLRENFDPV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 331 AQARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSleGLTNrpAILRKEFVFDEYQILEARLAGADTVLLIVKMLSVEL 410
Cdd:PLN02460 143 EIAQAYEKGGAACLSVLTDEKYFQGSFENLEAIRNA--GVKC--PLLCKEFIVDAWQIYYARSKGADAILLIAAVLPDLD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 411 LTRLYHYSRSLGMEPLVEVNTPEEMKIAVDL-GAEVIGVNNRDLTSFEVDLGTTSRLM-----DQVPSSTI-VCALSGIS 483
Cdd:PLN02460 219 IKYMLKICKSLGMAALIEVHDEREMDRVLGIeGVELIGINNRSLETFEVDISNTKKLLegergEQIREKGIiVVGESGLF 298
|
250 260 270
....*....|....*....|....*....|....*..
gi 350629793 484 GPKDVEAYKKEGVKAILVGEALMRAADTAAFIAELLG 520
Cdd:PLN02460 299 TPDDVAYVQNAGVKAVLVGESLVKQDDPGKGIAGLFG 335
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
24-216 |
5.70e-44 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 166.74 E-value: 5.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 24 SNVILIDNYDSFTWNVYQYLVLEGATVNVFRND---QITLEELIAKKPTQLVISPGPGHPeTDAGISSAAIQYFSGKIPI 100
Cdd:PRK09522 2 ADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVP-SEAGCMPELLTRLRGKLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 101 FGVCMGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDSLAVTRYHSLAGTHatIPDCLEVSSSVQltddsnk 180
Cdd:PRK09522 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSN--IPAGLTINAHFN------- 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 350629793 181 DVIMGVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:PRK09522 152 GMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTL 187
|
|
| PRK13957 |
PRK13957 |
indole-3-glycerol-phosphate synthase; Provisional |
295-510 |
1.93e-41 |
|
indole-3-glycerol-phosphate synthase; Provisional
Pssm-ID: 140013 Cd Length: 247 Bit Score: 151.96 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 295 PFPAR---LRQS--PYPLSLMAEIKRASPSKGMIAENACAPAQARQYAKAGASVISVLTEPEWFKGSIDDLRAVRQSLeg 369
Cdd:PRK13957 24 PLPDRglpLRDSlkSRSFSIIAECKRKSPSAGELRADYHPVQIAKTYETLGASAISVLTDQSYFGGSLEDLKSVSSEL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 370 ltnRPAILRKEFVFDEYQILEARLAGADTVLLIVKMLSVELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVN 449
Cdd:PRK13957 102 ---KIPVLRKDFILDEIQIREARAFGASAILLIVRILTPSQIKSFLKHASSLGMDVLVEVHTEDEAKLALDCGAEIIGIN 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350629793 450 NRDLTSFEVDLGTTSRLMDQVPSSTIVCALSGISGPKDVEAYKKEgVKAILVGEALMRAAD 510
Cdd:PRK13957 179 TRDLDTFQIHQNLVEEVAAFLPPNIVKVGESGIESRSDLDKFRKL-VDAALIGTYFMEKKD 238
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
25-221 |
2.63e-41 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 161.62 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 25 NVILIDNYDSFTWNVYQYLVLEGATVNVFRNDqITLEELIAKKPTQLVISPGPGHPEtDAGISS---AAIqyfSGKIPIF 101
Cdd:PRK13566 528 RVLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRPS-DFDCKAtidAAL---ARNLPIF 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 102 GVCMGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGA-YEGLPDSLAVTRYHSLAGTHATIPDCLEVSSSvqlTDDsnk 180
Cdd:PRK13566 603 GVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGRlFSGLPEEFTVGRYHSLFADPETLPDELLVTAE---TED--- 676
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 350629793 181 DVIMGVRHKKLAVEGVQFHPESILT---EYGRTMFRNFLKLTAG 221
Cdd:PRK13566 677 GVIMAIEHKTLPVAAVQFHPESIMTlggDVGLRIIENVVRLLAG 720
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
536-767 |
5.93e-33 |
|
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: 126.15 E-value: 5.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 536 VKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVPDDVALRISQVVKSTPKPagqtpptsqgtpaaasveyfdhsaril 615
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKR--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 616 rhpsrallVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLEWAKLIP----VPVIRKFGLDEP-----AIARRAYHSLPL 686
Cdd:cd00405 54 --------VGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYCAQLRarlgLPVIKAIRVKDEedlekAAAYAGEVDAIL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 687 LDSGV----GGTGELLDQSRVQNVldkDSGLRVILAGGLDPTNVAGIVQKLG----------ESgrkvvgvdvssgveSD 752
Cdd:cd00405 126 LDSKSggggGGTGKTFDWSLLRGL---ASRKPVILAGGLTPDNVAEAIRLVRpygvdvssgvET--------------SP 188
|
250
....*....|....*
gi 350629793 753 GAQDVGKIRAFVQAV 767
Cdd:cd00405 189 GIKDPEKIRAFIEAA 203
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
24-208 |
4.36e-32 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 123.80 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 24 SNVILIDNYDSFTWNVYQYLVLEGATVNVFRNdQITLEELIAKKPTQLVISPGPGHPEtDAGISSAAIQYFSGKIPIFGV 103
Cdd:PRK05637 2 THVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHPR-DAGNMMALIDRTLGQIPLLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 104 CMGQQCIITCFGGKVDVTGEIlHGKTSALKHDGKGA----YEGL-----PDS-------LAVTRYHSLAGTHAtiPDCLE 167
Cdd:PRK05637 80 CLGFQALLEHHGGKVEPCGPV-HGTTDNMILTDAGVqspvFAGLatdvePDHpeipgrkVPIARYHSLGCVVA--PDGME 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 350629793 168 vssSVQLTDDSNKDVIMGVRHKKLAVEGVQFHPESILTEYG 208
Cdd:PRK05637 157 ---SLGTCSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTG 194
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
23-216 |
1.71e-30 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 118.69 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 23 ASNVILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEEliAKKPTQLVISPGPGHPETDAGISSAAIQYFSGKiPIFG 102
Cdd:PRK06895 1 ATKLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDE--VENFSHILISPGPDVPRAYPQLFAMLERYHQHK-SILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 103 VCMGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGA-YEGLPDSLAVTRYHSLAGTHATIPDCLEVsssvqlTDDSNKD 181
Cdd:PRK06895 78 VCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPlFDGLPEEFNIGLYHSWAVSEENFPTPLEI------TAVCDEN 151
|
170 180 190
....*....|....*....|....*....|....*
gi 350629793 182 VIMGVRHKKLAVEGVQFHPESILTEYGRTMFRNFL 216
Cdd:PRK06895 152 VVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
27-223 |
1.58e-29 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 125.73 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 27 ILIDNYDSFTWNVYQYL-VLEGATVNVFRNDQITLEE----LIAKKP-TQLVISPGPGHPETDAGISSAAIQYFSGK-IP 99
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELsIVNGVPPVVVRNDEWTWEEvyhyLYEEKAfDNIVISPGPGSPTCPADIGICLRLLLECRdIP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 100 IFGVCMGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLP----DSLAVTRYHSL-------------------A 156
Cdd:PLN02889 165 ILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLvidaeslpkelvpiawtssS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 157 GTHA--------TIPDCLEVSSSVQLTDDS--------------------NKDVIMGVRHKKLAVEGVQFHPESILTEYG 208
Cdd:PLN02889 245 DTLSflesqksgLVPDAYESQIGQSGSSDPfssklkngtswpsshsermqNGKILMGIMHSTRPHYGLQFHPESIATCYG 324
|
250
....*....|....*
gi 350629793 209 RTMFRNFLKLTAGTW 223
Cdd:PLN02889 325 RQIFKNFREITQDYW 339
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
534-769 |
1.89e-28 |
|
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: 113.31 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 534 PLVKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVPDDVALRISQVVkstpkpagqtpptsqgtpaaasveyfdhsar 613
Cdd:COG0135 2 TRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAAL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 614 ilrhPSRALLVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLEW----AKLIPVPVIRKFGLDEPAIARRAYHSLP---- 685
Cdd:COG0135 51 ----PPFVKKVGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYcaalRERLGLPVIKAIRVGDGADLEEAAAYAPvada 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 686 -LLDSGV----GGTGELLDQSRVQNVldkDSGLRVILAGGLDPTNVAGIVQKLG----------ES--GRKvvgvdvssg 748
Cdd:COG0135 127 lLLDAKVpglyGGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVRpygvdvssgvESapGVK--------- 194
|
250 260
....*....|....*....|.
gi 350629793 749 vesdgaqDVGKIRAFVQAVRG 769
Cdd:COG0135 195 -------DPDKIRAFVEAVRA 208
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
25-218 |
6.05e-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: 110.77 E-value: 6.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 25 NVILIDNYDSFTWNVYQYL--VLE-GATVNVFRND--QITLEELIAKKPTqLVISPGPGHPET--DAGISSAAIQY-FSG 96
Cdd:TIGR01823 7 HVLFIDSYDSFTYNVVRLLeqQTDiSVHVTTVHSDtfQDQLLELLPLFDA-IVVGPGPGNPNNaqDMGIISELWELaNLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 97 KIPIFGVCMGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYEGLPDsLAVTRYHSLagtHATiPDCLEVSSSVQLTD 176
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSL---YAN-PEGIDTLLPLCLTE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 350629793 177 DSNKDVIMGVRHKKLAVEGVQFHPESILTEYGR-TMFRNFLKL 218
Cdd:TIGR01823 161 DEEGIILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKL 203
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
536-770 |
7.27e-21 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 91.41 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 536 VKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVpddvalrisqvvkstpkpagqtpptsqgTPAAAsveyfdhsARIL 615
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYV----------------------------SPEQA--------AELA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 616 R-HPSRALLVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLE----WAKLIPVPVIRKFGLDEPAIARRAYHSLP----- 685
Cdd:PRK01222 49 AaLPPFVKVVGVFVNASDEEIDEIVETVPLDLLQLHGDETPEfcrqLKRRYGLPVIKALRVRSAGDLEAAAAYYGdadgl 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 686 LLDSGV---GGTGELLDQSrvqnVLDKDSGLRVILAGGLDPTNVAGIVQKLG----------ESgrkvvgvdvssgveSD 752
Cdd:PRK01222 129 LLDAYVglpGGTGKTFDWS----LLPAGLAKPWILAGGLNPDNVAEAIRQVRpygvdvssgvES--------------AP 190
|
250
....*....|....*...
gi 350629793 753 GAQDVGKIRAFVQAVRGL 770
Cdd:PRK01222 191 GIKDPEKIRAFIEAVKSA 208
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
59-221 |
1.99e-19 |
|
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: 86.60 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 59 TLEELIAKKPTQLVISPGPGhPETDAGISSAAIQYFSGKIPIFGVCMGQQCIITCFGGKVDVTGEILHGKTSaLKHDGKG 138
Cdd:TIGR00888 33 PLEEIREKNPKGIILSGGPS-SVYAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKREYGKAE-LEILDED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 139 A-YEGLPDSLAVTRYHSLAGTHatIPDCLEVSSSvqlTDDSNkdvIMGVRHKKLAVEGVQFHPESILTEYGRTMFRNFLK 217
Cdd:TIGR00888 111 DlFRGLPDESTVWMSHGDKVKE--LPEGFKVLAT---SDNCP---VAAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
|
....
gi 350629793 218 LTAG 221
Cdd:TIGR00888 183 DVCG 186
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
58-216 |
2.11e-18 |
|
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: 83.74 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 58 ITLEELIAKKPTQLVISPGPgHPETDAGISSAAIQYFSGKIPIFGVCMGQQCIITCFGGKVD--VTGEilHGKTSALKHD 135
Cdd:cd01742 32 TPLEEIKLKNPKGIILSGGP-SSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVErgDKRE--YGKAEIEIDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 136 GKGAYEGLPDSLAVtryhsLAgTHA----TIPDCLEVSSSvqlTDDSNkdvIMGVRHKKLAVEGVQFHPESILTEYGRTM 211
Cdd:cd01742 109 SSPLFEGLPDEQTV-----WM-SHGdevvKLPEGFKVIAS---SDNCP---VAAIANEEKKIYGVQFHPEVTHTEKGKEI 176
|
....*
gi 350629793 212 FRNFL 216
Cdd:cd01742 177 LKNFL 181
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
26-218 |
4.05e-17 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 79.90 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFT---WNVYQYLvleGATVNVFRNDqITLEElIAKKPTQLVISpgpGHPETD-AGISSAAIQYFsgKIPIF 101
Cdd:PRK00758 2 IVVVDNGGQYNhliHRTLRYL---GVDAKIIPNT-TPVEE-IKAFEDGLILS---GGPDIErAGNCPEYLKEL--DVPIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 102 GVCMGQQCIITCFGGKV---------DVTGEILHgktsalkHDGkgAYEGLPDSLAVTRYHslAGTHATIPDCLEVSSSV 172
Cdd:PRK00758 72 GICLGHQLIAKAFGGEVgrgeygeyaLVEVEILD-------EDD--ILKGLPPEIRVWASH--ADEVKELPDGFEILARS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 350629793 173 QLTDdsnkdvIMGVRHKKLAVEGVQFHPESILTEYGRTMFRNFLKL 218
Cdd:PRK00758 141 DICE------VEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFLEI 180
|
|
| PLN02363 |
PLN02363 |
phosphoribosylanthranilate isomerase |
534-770 |
2.19e-16 |
|
phosphoribosylanthranilate isomerase
Pssm-ID: 215207 Cd Length: 256 Bit Score: 79.52 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 534 PLVKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVPDDVALRISQVVKStpkpAGQTPptsqgtpaaasveyfdhsar 613
Cdd:PLN02363 47 PLVKMCGITSARDAAMAVEAGADFIGMILWPKSKRSISLSVAKEISQVARE----GGAKP-------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 614 ilrhpsrallVGVFQNQPLDYILSQQQKLGLDVVQLHGSEPLEWAKLIP--VPVIRKFGLDEPAIARRAYHSLP------ 685
Cdd:PLN02363 103 ----------VGVFVDDDANTILRAADSSDLELVQLHGNGSRAAFSRLVreRKVIYVLNANEDGKLLNVVPEEDchladw 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 686 -LLDSGVGGTGELLDQSRVQnVLDKDSGLRVILAGGLDPTNVAGIVQKLGESGrkvvGVDVSSGVESDGAQ-DVGKIRAF 763
Cdd:PLN02363 173 iLVDSATGGSGKGFNWQNFK-LPSVRSRNGWLLAGGLTPENVHEAVSLLKPTG----VDVSSGICGPDGIRkDPSKISSF 247
|
....*..
gi 350629793 764 VQAVRGL 770
Cdd:PLN02363 248 ISAVKSV 254
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
57-223 |
1.08e-15 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 80.48 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 57 QITLEELIAKKPTQLVISPGP------GHPETDAGIssaaiqyFSGKIPIFGVCMGQQCIITCFGGKVDVTGEILHGKTS 130
Cdd:PRK00074 36 DISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEI-------FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 131 aLKHDGKGA-YEGLPDSLAVTRYHslaGTHAT-IPDCLEVSSSvqlTDDSnkdVIMGVRHKKLAVEGVQFHPESILTEYG 208
Cdd:PRK00074 109 -LEVDNDSPlFKGLPEEQDVWMSH---GDKVTeLPEGFKVIAS---TENC---PIAAIANEERKFYGVQFHPEVTHTPQG 178
|
170
....*....|....*...
gi 350629793 209 RTMFRNFLKLTAG---TW 223
Cdd:PRK00074 179 KKLLENFVFDICGckgDW 196
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
37-202 |
6.80e-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: 67.52 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 37 WNVYQYLVLEGATVNVFRNDQiTLEELIAKKPTQLVISPGPGHPETDAGISSAAIQYFSGKIPIFGVCMGQQCIITCFGg 116
Cdd:cd01744 10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQLLALALG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 117 kvdvtgeilhGKTSALKHDGKGA----YEGLPDSLAVT-RYHSLAGTHATIPDCLEVsSSVQLTDDSNKdvimGVRHKKL 191
Cdd:cd01744 88 ----------AKTYKMKFGHRGSnhpvKDLITGRVYITsQNHGYAVDPDSLPGGLEV-THVNLNDGTVE----GIRHKDL 152
|
170
....*....|.
gi 350629793 192 AVEGVQFHPES 202
Cdd:cd01744 153 PVFSVQFHPEA 163
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
43-202 |
1.01e-11 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 67.02 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 43 LVLEGATVNVFRNDqITLEELIAKKPTQLVISPGPGHPE-TDAGIssAAIQYF-SGKIPIFGVCMGQQCIITCFGGKV-- 118
Cdd:PRK12564 195 LAERGCRVTVVPAT-TTAEEILALNPDGVFLSNGPGDPAaLDYAI--EMIRELlEKKIPIFGICLGHQLLALALGAKTyk 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 119 -------------DV-TGEIL-----HGktsalkhdgkgaYeglpdslAVTRyhslagthATIPDCLEVsSSVQLTDDSn 179
Cdd:PRK12564 272 mkfghrganhpvkDLeTGKVEitsqnHG------------F-------AVDE--------DSLPANLEV-THVNLNDGT- 322
|
170 180
....*....|....*....|...
gi 350629793 180 kdvIMGVRHKKLAVEGVQFHPES 202
Cdd:PRK12564 323 ---VEGLRHKDLPAFSVQYHPEA 342
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
60-241 |
2.00e-10 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 63.94 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 60 LEELIAKKPTQLVISPGPgHPETDAGISSAAIQYF----SGKIPIFGVCMGQQCIITCFGGKVDVTGEILHGKTSALKHD 135
Cdd:PLN02347 46 LDRIASLNPRVVILSGGP-HSVHVEGAPTVPEGFFdycrERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVC 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 136 GKGAYEGLPDSLAVTRYHSLAGTHATIPDCLE-VSSSVQLTddsnkdvIMGVRHKKLAVEGVQFHPESILTEYGRTMFRN 214
Cdd:PLN02347 125 GSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEvVAKSVQGA-------VVAIENRERRIYGLQYHPEVTHSPKGMETLRH 197
|
170 180 190
....*....|....*....|....*....|.
gi 350629793 215 FL----KLTAGtWEgNGKHFDEQSNTTKATV 241
Cdd:PLN02347 198 FLfdvcGVTAD-WK-MQDVLEEQIELIKATV 226
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
27-218 |
1.67e-09 |
|
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: 58.80 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 27 ILI----DNYDSFTWNVYQYLVLEGATVNVFR--NDQITLEELIAKKPTQLVISPGPGHPETDAGISSAAIQY----FSG 96
Cdd:COG0518 2 ILIldhdPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALireaFEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 97 KIPIFGVCMGQQCIITCFGGKVDVTG--EIlhGKTSALKHDGKGAYEGLPDSLAVtrYHSlagtH----ATIPDCLEVSS 170
Cdd:COG0518 82 GKPVLGICYGAQLLAHALGGKVEPGPgrEI--GWAPVELTEADPLFAGLPDEFTV--WMS----HgdtvTELPEGAEVLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 350629793 171 SvqltddSNKDVIMGVRHKKLAVeGVQFHPE------------------------------SILTEYGRTMFRNFLKL 218
Cdd:COG0518 154 S------SDNCPNQAFRYGRRVY-GVQFHPEvthtmmeawleeradelaaeellaeaslhdPELREAGRRLLRNFLRE 224
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
533-731 |
1.36e-08 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 58.28 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 533 SPLVKICGTRSEEAARAAIEAGADLIGIIMVQGRTRCVPDDVALRisQVVKSTPkpagqtpptsqgtpaaasveyfdhsa 612
Cdd:PRK13803 2 QPKIKICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVGNKFLAP--NLEKAIR-------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 613 rilrhPSRALLVGVFQNQPLDYILSQQQKLGLDVVQLHGSE----PLEWAKLI--PVPVIRKFGLD-----EPAIARRAY 681
Cdd:PRK13803 54 -----KAGGRPVGVFVNESAKAMLKFSKKNGIDFVQLHGAEskaePAYCQRIYkkSIKKIGSFLIDdafgfEVLDEYRDH 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 350629793 682 HSLPLLDS---GVGGTGELLDQSRVQNVLDKdsgLRVILAGGLDPTNVAGIVQ 731
Cdd:PRK13803 129 VKYFLFDNktkIYGGSGKSFDWEKFYNYNFK---FPFFLSGGLSPTNFDRIIN 178
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
26-202 |
2.03e-08 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 57.11 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNydSFTWNVYQYLVLEGATVNVFrNDQITLEELIAKKPTQLVISPGPGHPETDAGISSAAIQYFSGKIPIFGVCM 105
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYNIPIFGICM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 106 GQQCIITCFGgkvdvtgeilhGKTSALK--HDGKGAYEGLPDSLAVT-RYHSLAGTHATIpdcleVSSSVQLTD-DSNKD 181
Cdd:CHL00197 272 GHQILSLALE-----------AKTFKLKfgHRGLNHPSGLNQQVEITsQNHGFAVNLESL-----AKNKFYITHfNLNDG 335
|
170 180
....*....|....*....|.
gi 350629793 182 VIMGVRHKKLAVEGVQFHPES 202
Cdd:CHL00197 336 TVAGISHSPKPYFSVQYHPEA 356
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
43-202 |
2.38e-08 |
|
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: 56.57 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 43 LVLEGATVNVFRNDqITLEELIAKKPTQLVISPGPGHPE-TDAGIssAAIQYFSGK-IPIFGVCMGQQCIITCFGGKV-- 118
Cdd:COG0505 194 LAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAaLDYAI--ETIRELLGKgIPIFGICLGHQLLALALGAKTyk 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 119 -------------DV-TG--EIlhgkTS-----ALKhdgkgayeglPDSLAVTRyhsLAGTHatipdclevsssVQLTDD 177
Cdd:COG0505 271 lkfghrganhpvkDLeTGrvEI----TSqnhgfAVD----------EDSLPATD---LEVTH------------VNLNDG 321
|
170 180
....*....|....*....|....*
gi 350629793 178 SnkdvIMGVRHKKLAVEGVQFHPES 202
Cdd:COG0505 322 T----VEGLRHKDLPAFSVQYHPEA 342
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
26-116 |
6.50e-08 |
|
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: 51.45 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTW---NVYQYLVLEGATVNVFRNDQITLEELIAKKPTQ-LVISPGPGHPET---DAGISSAAIQYFSGKI 98
Cdd:cd01653 1 VAVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVESDVDLDDYDgLILPGGPGTPDDlarDEALLALLREAAAAGK 80
|
90
....*....|....*...
gi 350629793 99 PIFGVCMGQQCIITCFGG 116
Cdd:cd01653 81 PILGICLGAQLLVLGVQF 98
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
62-202 |
1.25e-07 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 54.60 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 62 ELIAKKPTQLVISPGPGHPETdAGISSAAIQYFSGKIPIFGVCMGQQCIITCFGGKVDVTGEILHGKTSALKHDGKGAYE 141
Cdd:PLN02771 276 EALKMKPDGVLFSNGPGDPSA-VPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVE 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350629793 142 glpdslAVTRYHSLAGTHATIPDCLEVsSSVQLTDDSnkdvIMGVRHKKLAVEGVQFHPES 202
Cdd:PLN02771 355 ------ISAQNHNYAVDPASLPEGVEV-THVNLNDGS----CAGLAFPALNVMSLQYHPEA 404
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
43-201 |
2.56e-07 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 53.36 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 43 LVLEGATVNVFRNDQiTLEELIAKKPTQLVISPGPGHPETDAGISSAAIQYFSGkIPIFGVCMGQQCIITCFGG------ 116
Cdd:PRK12838 185 LSKRGCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISS-YPILGICLGHQLIALALGAdteklp 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 117 ----------KVDVTGEILhgkTSALKHDgkgaYEGLPDSLAVT----RYHSLagthatipdclevsssvqltddsNKDV 182
Cdd:PRK12838 263 fghrganhpvIDLTTGRVW---MTSQNHG----YVVDEDSLDGTplsvRFFNV-----------------------NDGS 312
|
170
....*....|....*....
gi 350629793 183 IMGVRHKKLAVEGVQFHPE 201
Cdd:PRK12838 313 IEGLRHKKKPVLSVQFHPE 331
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
26-110 |
2.16e-06 |
|
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: 46.42 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 26 VILIDNYDSFTW---NVYQYLVLEGATVNVFRNDQITLEELIAKKPTQ-LVISPGPGHPET---DAGISSAAIQYFSGKI 98
Cdd:cd03128 1 VAVLLFGGSEELelaSPLDALREAGAEVDVVSPDGGPVESDVDLDDYDgLILPGGPGTPDDlawDEALLALLREAAAAGK 80
|
90
....*....|..
gi 350629793 99 PIFGVCMGQQCI 110
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
458-505 |
4.32e-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: 39.56 E-value: 4.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 350629793 458 VDLGTTSRLMDQVPSStiVCALSGISGPKDVEAYKKEGVKAILVGEAL 505
Cdd:cd04723 176 PDLELLERLAARADIP--VIAAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| PRK13958 |
PRK13958 |
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional |
628-769 |
6.52e-03 |
|
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
Pssm-ID: 184418 Cd Length: 207 Bit Score: 38.55 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 628 QNQPLDYILSQQQklgLDVVQLHGSEPLEWAKLIP-----VPVIRKFGLDEPAIARRAYH----SLPLLDS---GVGGTG 695
Cdd:PRK13958 63 DLTTIEHILSNTS---INTIQLHGTESIDFIQEIKkkyssIKIIKALPADENIIQNINKYkgfvDLFIIDTpsvSYGGTG 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350629793 696 ELLDQSrvqnVLDKDSGLRVILAGGLDPTNVAGIVQ-KLGESGRKVVGvdvssGVESDGAQDVGKIRAFVQAVRG 769
Cdd:PRK13958 140 QTYDWT----ILKHIKDIPYLIAGGINSENIQTVEQlKLSHQGYDIAS-----GIETNGRKDINKMTAIVNIVKG 205
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
324-518 |
8.07e-03 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 38.27 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 324 AENACAPAQArqYAKAGASVISV-LTEPEWfkgsIDDLRAVRQSLEGL-----TnrpailrkefVFDEYQILEARLAGAD 397
Cdd:cd00452 15 AEDALALAEA--LIEGGIRAIEItLRTPGA----LEAIRALRKEFPEAligagT----------VLTPEQADAAIAAGAQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350629793 398 tvlLIVK-MLSVELLTrlyhYSRSLGMEPLVEVNTPEEMKIAVDLGAEVIGVnnrdltsFEVD-LGTT-----SRLMDQV 470
Cdd:cd00452 79 ---FIVSpGLDPEVVK----AANRAGIPLLPGVATPTEIMQALELGADIVKL-------FPAEaVGPAyikalKGPFPQV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 350629793 471 PsstiVCALSGISgPKDVEAYKKEGVKAILVGEALMRAADTAAFIAEL 518
Cdd:cd00452 145 R----FMPTGGVS-LDNAAEWLAAGVVAVGGGSLLPKDAVAAGDWAAI 187
|
|
| |
