|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
249-510 |
1.72e-135 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 400.52 E-value: 1.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 249 LQKIYAHRKAAVDAQKQIPSqrLSDLQAAYNlslAPPQISLVDRLRNSPFDVALCAEIKRASPSKGVFALDIDAPSQARK 328
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPP--LADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 329 YALAGASVISVLTEPEWFKGSIDDLRAVRQVLNGMpnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELLERLY 408
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 409 KYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDCKRDG 488
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 2130438548 489 VNGILVGEAIMRAPDATQFIRE 510
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
289-511 |
8.65e-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: 327.50 E-value: 8.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 289 LVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLngmpnRPA 368
Cdd:cd00331 1 FKAALKRPG-GLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 369 VLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLES 448
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130438548 449 FEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
246-511 |
6.13e-107 |
|
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: 326.99 E-value: 6.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 246 SNILQKIYAHRKAAVDAQKQIPSqrLSDLQAAynLSLAPPQISLVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQ 325
Cdd:COG0134 1 PTILDKIVAHKREEVAARKARVP--LAELEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 326 ARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgmpnRPaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELLE 405
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAAVD----LP-VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 406 RLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDCK 485
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*.
gi 2130438548 486 RDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALREL 256
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
245-511 |
1.92e-105 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 323.26 E-value: 1.92e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 245 KSNILQKIYAHRKAAVDAQKQIPSqrLSDLQAAynLSLAPPQISLVDRLRNSPfdVALCAEIKRASPSKGVFALDIDAPS 324
Cdd:PRK00278 1 MMDILDKIVAYKREEVAARKAQVP--LAELKAR--AAAAPPPRDFAAALRAGK--PAVIAEVKKASPSKGVIREDFDPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 325 QARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELL 404
Cdd:PRK00278 75 IAKAYEAGGAACLSVLTDERFFQGSLEYLRAARAAVS-LP----VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 405 ERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDC 484
Cdd:PRK00278 150 KELLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRL 229
|
250 260
....*....|....*....|....*..
gi 2130438548 485 KRDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:PRK00278 230 AKAGADAVLVGESLMRADDPGAALREL 256
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
23-217 |
1.73e-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: 312.74 E-value: 1.73e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTP-EEAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMGV 182
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAW--TED---GEIMGI 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQGG 217
Cdd:COG0512 155 RHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
22-214 |
8.26e-98 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 300.51 E-value: 8.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 22 NLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVC 101
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTP-AEAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 102 MGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMG 181
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW--TDD---GEIMG 154
|
170 180 190
....*....|....*....|....*....|...
gi 2130438548 182 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 214
Cdd:PRK05670 155 VRHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
23-212 |
2.61e-93 |
|
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: 288.66 E-value: 2.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHP-EDAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiakedGSKGVIMGV 182
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAS-----TEDGVIMAL 154
|
170 180 190
....*....|....*....|....*....|
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:cd01743 155 RHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
23-213 |
1.05e-71 |
|
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: 231.99 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTP-NEAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDgskgVIMGV 182
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI----EIMAI 156
|
170 180 190
....*....|....*....|....*....|.
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFLH 213
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLH 187
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
26-214 |
5.77e-63 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 208.73 E-value: 5.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 26 IDNYDSFTWNVYQYL--VLEGAKVTVFRNdQITIDDLIAKNPTQLVISPGPGHPGT--DSGISRDAIKHFAGKIPIFGVC 101
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKNdrDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 102 MGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVtlPECLEVTSwiAKEDGSKGVIMG 181
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEV--PDCFEVTA--TTDHDGEELVMG 156
|
170 180 190
....*....|....*....|....*....|...
gi 2130438548 182 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 214
Cdd:NF041322 157 IRHREHPIECVQFHPESVLTGVGHDVIENFLAA 189
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
24-213 |
6.17e-63 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 208.63 E-value: 6.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 24 ILIDNYDSFTWNVYQYLVLEGAKVTVFRNDqITIDDLIAKNPTQLVISPGPGHPGtDSGISRDAIKH-FAGKIPIFGVCM 102
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPG-AAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAG-EILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDGskGVIMG 181
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTAT--SEND--GTIMG 154
|
170 180 190
....*....|....*....|....*....|..
gi 2130438548 182 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLH 213
Cdd:pfam00117 155 IRHKKLPIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
529-753 |
2.18e-58 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 196.41 E-value: 2.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVdhetalsisqavhmskktgstevssqasksardfFNINAEVIRKR 608
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKAGADYLGLIFSESSKRQV----------------------------------SPEQAQELRSP 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 GPL-LVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFIP--VPVIRKFKPGQ----VGLATRGFHAV-PLLDSGA 680
Cdd:pfam00697 47 VPLlLVGVFVNQPIDDVLRIAQVLGLDVVQLHGDEDQEYENLLPtgVPVIKAIWVPDsvdtVDIARRADHVDlPLLDSGA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130438548 681 -GSGEMLNLESVKKELEKdeQVTVLLAGGLGPSNVAETVKSLGalaerVIGVDVSSGVEEGGKQSLEKIREFVK 753
Cdd:pfam00697 127 gGTGELFDWSLVSKWLKS--GLKVILAGGLNPDNVVEAIKTPG-----VIGVDVSSGVETNGIKDLNKIRKFVQ 193
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
529-755 |
1.54e-52 |
|
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: 180.85 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaevirkr 608
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKR--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 gpllVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFIP----VPVIRKFKPG-----QVGLATRGFHAVPLLDS- 678
Cdd:cd00405 54 ----VGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYCAQLRarlgLPVIKAIRVKdeedlEKAAAYAGEVDAILLDSk 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 679 ----GAGSGEMLNLESVKKELEKdeqVTVLLAGGLGPSNVAETVKSLgalaeRVIGVDVSSGVE-EGGKQSLEKIREFVK 753
Cdd:cd00405 130 sgggGGGTGKTFDWSLLRGLASR---KPVILAGGLTPDNVAEAIRLV-----RPYGVDVSSGVEtSPGIKDPEKIRAFIE 201
|
..
gi 2130438548 754 AA 755
Cdd:cd00405 202 AA 203
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
529-757 |
2.60e-44 |
|
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: 158.38 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaevirkr 608
Cdd:COG0135 4 VKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKK--------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 gpllVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFI----PVPVIRKFKPGQ---VGLATRGFHAVP--LLDSG 679
Cdd:COG0135 57 ----VGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYCAALrerlGLPVIKAIRVGDgadLEEAAAYAPVADalLLDAK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 680 A-----GSGEMLNLESVKKElekDEQVTVLLAGGLGPSNVAETVKSLGALaerviGVDVSSGVE-EGGKQSLEKIREFVK 753
Cdd:COG0135 133 VpglygGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVRPY-----GVDVSSGVEsAPGVKDPDKIRAFVE 204
|
....
gi 2130438548 754 AAKS 757
Cdd:COG0135 205 AVRA 208
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
529-759 |
2.60e-37 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 138.79 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaevirkr 608
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVKV--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 gpllVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFI----PVPVIRKFK---PGQVGLATRGFHAV--PLLDSG 679
Cdd:PRK01222 58 ----VGVFVNASDEEIDEIVETVPLDLLQLHGDETPEFCRQLkrryGLPVIKALRvrsAGDLEAAAAYYGDAdgLLLDAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 680 A----GSGEMLNLESVKKELEKDeqvtVLLAGGLGPSNVAETVKSLGALaerviGVDVSSGVEEG-GKQSLEKIREFVKA 754
Cdd:PRK01222 134 VglpgGTGKTFDWSLLPAGLAKP----WILAGGLNPDNVAEAIRQVRPY-----GVDVSSGVESApGIKDPEKIRAFIEA 204
|
....*
gi 2130438548 755 AKSVR 759
Cdd:PRK01222 205 VKSAD 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
249-510 |
1.72e-135 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 400.52 E-value: 1.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 249 LQKIYAHRKAAVDAQKQIPSqrLSDLQAAYNlslAPPQISLVDRLRNSPFDVALCAEIKRASPSKGVFALDIDAPSQARK 328
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPP--LADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 329 YALAGASVISVLTEPEWFKGSIDDLRAVRQVLNGMpnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELLERLY 408
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 409 KYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDCKRDG 488
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 2130438548 489 VNGILVGEAIMRAPDATQFIRE 510
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
289-511 |
8.65e-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: 327.50 E-value: 8.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 289 LVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLngmpnRPA 368
Cdd:cd00331 1 FKAALKRPG-GLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 369 VLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLES 448
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130438548 449 FEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
246-511 |
6.13e-107 |
|
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: 326.99 E-value: 6.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 246 SNILQKIYAHRKAAVDAQKQIPSqrLSDLQAAynLSLAPPQISLVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQ 325
Cdd:COG0134 1 PTILDKIVAHKREEVAARKARVP--LAELEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 326 ARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgmpnRPaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELLE 405
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAAVD----LP-VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 406 RLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDCK 485
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*.
gi 2130438548 486 RDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALREL 256
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
245-511 |
1.92e-105 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 323.26 E-value: 1.92e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 245 KSNILQKIYAHRKAAVDAQKQIPSqrLSDLQAAynLSLAPPQISLVDRLRNSPfdVALCAEIKRASPSKGVFALDIDAPS 324
Cdd:PRK00278 1 MMDILDKIVAYKREEVAARKAQVP--LAELKAR--AAAAPPPRDFAAALRAGK--PAVIAEVKKASPSKGVIREDFDPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 325 QARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELL 404
Cdd:PRK00278 75 IAKAYEAGGAACLSVLTDERFFQGSLEYLRAARAAVS-LP----VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 405 ERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVLDC 484
Cdd:PRK00278 150 KELLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRL 229
|
250 260
....*....|....*....|....*..
gi 2130438548 485 KRDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:PRK00278 230 AKAGADAVLVGESLMRADDPGAALREL 256
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
23-217 |
1.73e-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: 312.74 E-value: 1.73e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTP-EEAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMGV 182
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAW--TED---GEIMGI 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQGG 217
Cdd:COG0512 155 RHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK09427 |
PRK09427 |
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
243-756 |
1.59e-100 |
|
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;
Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 317.53 E-value: 1.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 243 PKKSNILQKIYAHRKAAVDAQKQipSQRLSDLQAaynlSLAPPQISLVDRLRNSpfDVALCAEIKRASPSKGVFALDIDA 322
Cdd:PRK09427 1 TMMPTVLAKIVADKAIWVAARKQ--QQPLASFQN----EIQPSDRSFYDALKGP--KTAFILECKKASPSKGLIRDDFDP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 323 PSQARKYAlAGASVISVLTEPEWFKGSIDDLRAVRQVLNgmpnRPaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYE 402
Cdd:PRK09427 73 AEIARVYK-HYASAISVLTDEKYFQGSFDFLPIVRAIVT----QP-ILCKDFIIDPYQIYLARYYGADAILLMLSVLDDE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 403 LLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDVL 482
Cdd:PRK09427 147 QYRQLAAVAHSLNMGVLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPADVIVISESGIYTHAQVR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 483 DCKRdGVNGILVGEAIMRAPDATQFIRELCAGLtgpvpksaaepllVKICGTRSAEAATEAIKAGADLVGMILVPGTKRC 562
Cdd:PRK09427 227 ELSP-FANGFLIGSSLMAEDDLELAVRKLILGE-------------NKVCGLTRPQDAKAAYDAGAVYGGLIFVEKSPRY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 563 VDHETALSISQAVhmskktgstevssqasksardffninaevirkrgPL-LVGVFMNQPIEEVLEKQRLYDLDIVQLHGD 641
Cdd:PRK09427 293 VSLEQAQEIIAAA----------------------------------PLrYVGVFRNADIEDIVDIAKQLSLAAVQLHGD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 642 EPLEWAN----FIPVPV-IRKFKPGQVGLATRGFHAVP--LLDSGA-GSGEMLNLESVKKELEKDeqvtVLLAGGLGPSN 713
Cdd:PRK09427 339 EDQAYIDalreALPKTCqIWKAISVGDTLPARDLQHVDryLLDNGQgGTGQTFDWSLLPGQSLDN----VLLAGGLNPDN 414
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2130438548 714 VAEtvkslgALAERVIGVDVSSGVEEG-GKQSLEKIREFVKAAK 756
Cdd:PRK09427 415 CQQ------AAQLGCAGLDFNSGVESApGIKDAQKLASVFQTLR 452
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
22-214 |
8.26e-98 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 300.51 E-value: 8.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 22 NLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVC 101
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTP-AEAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 102 MGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMG 181
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW--TDD---GEIMG 154
|
170 180 190
....*....|....*....|....*....|...
gi 2130438548 182 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 214
Cdd:PRK05670 155 VRHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
23-212 |
2.61e-93 |
|
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: 288.66 E-value: 2.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHP-EDAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiakedGSKGVIMGV 182
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAS-----TEDGVIMAL 154
|
170 180 190
....*....|....*....|....*....|
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:cd01743 155 RHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
23-215 |
1.91e-83 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 275.06 E-value: 1.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLV-LEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVC 101
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGeLGPEEIEVVRNDEITIEEIEALNPSHIVISPGPGRP-EEAGISVEVIRHFSGKVPILGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 102 MGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDGSkgvIMG 181
Cdd:PRK14607 81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAK--SDDGE---IMG 155
|
170 180 190
....*....|....*....|....*....|....
gi 2130438548 182 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQ 215
Cdd:PRK14607 156 IRHKEHPIFGVQFHPESILTEEGKRILKNFLNYQ 189
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
23-212 |
5.30e-75 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 240.93 E-value: 5.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTP-NEAGISLQAIEHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDGSKGVIMGV 182
Cdd:PRK08857 81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGSMDEIMGF 160
|
170 180 190
....*....|....*....|....*....|
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
23-213 |
7.90e-74 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 237.89 E-value: 7.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTP-DEAGISLDVIRHYAGRLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDgskgvIMGV 182
Cdd:PRK08007 81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETRE-----IMGI 155
|
170 180 190
....*....|....*....|....*....|.
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFLH 213
Cdd:PRK08007 156 RHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
23-212 |
2.04e-72 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 234.31 E-value: 2.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSP-NEAGISMEVIRYFAGKIPIFGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIAkedgsKGVIMGV 182
Cdd:PRK07649 81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTE-----EGEIMAI 155
|
170 180 190
....*....|....*....|....*....|
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:PRK07649 156 RHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
23-213 |
1.05e-71 |
|
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: 231.99 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTP-NEAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDgskgVIMGV 182
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI----EIMAI 156
|
170 180 190
....*....|....*....|....*....|.
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFLH 213
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLH 187
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
23-212 |
2.51e-70 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 228.59 E-value: 2.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTP-NEAGISLAVIRHFADKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiAKEDGSKGVIMGV 182
Cdd:PRK06774 81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAW-SERGGEMDEIMGI 159
|
170 180 190
....*....|....*....|....*....|
gi 2130438548 183 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:PRK06774 160 RHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
23-212 |
7.04e-65 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 213.82 E-value: 7.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCM 102
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHP-RDSGISLDVISSYAPYIPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIakedgSKGVIMGV 182
Cdd:CHL00101 81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWT-----EDGLIMAC 155
|
170 180 190
....*....|....*....|....*....|.
gi 2130438548 183 RHKEY-TIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:CHL00101 156 RHKKYkMLRGIQFHPESLLTTHGQQILRNFL 186
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
10-223 |
1.84e-64 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 213.89 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 10 DSDPSPLVETASN---LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDLIAKNPTQLVISPGPGHPgTDSGISRD 86
Cdd:PLN02335 5 NSIPSVVINSSKQngpIIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTP-QDSGISLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 87 AIKHFAGKIPIFGVCMGQQCIFDVYGGDVSFAGE-ILHGKTSPLCHDGKGA---YAGLPQDLPVTRYHSLAGTHVTLPE- 161
Cdd:PLN02335 84 TVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDEKGEeglFSGLPNPFTAGRYHSLVIEKDTFPSd 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130438548 162 CLEVTSWiaKEDgskGVIMGVRHKEYT-IEGVQFHPESILSAEGRGMFRNFLHMQGGTWAENE 223
Cdd:PLN02335 164 ELEVTAW--TED---GLIMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKIIEKKESEKL 221
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
26-214 |
5.77e-63 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 208.73 E-value: 5.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 26 IDNYDSFTWNVYQYL--VLEGAKVTVFRNdQITIDDLIAKNPTQLVISPGPGHPGT--DSGISRDAIKHFAGKIPIFGVC 101
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKNdrDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 102 MGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVtlPECLEVTSwiAKEDGSKGVIMG 181
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEV--PDCFEVTA--TTDHDGEELVMG 156
|
170 180 190
....*....|....*....|....*....|...
gi 2130438548 182 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 214
Cdd:NF041322 157 IRHREHPIECVQFHPESVLTGVGHDVIENFLAA 189
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
24-213 |
6.17e-63 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 208.63 E-value: 6.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 24 ILIDNYDSFTWNVYQYLVLEGAKVTVFRNDqITIDDLIAKNPTQLVISPGPGHPGtDSGISRDAIKH-FAGKIPIFGVCM 102
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPG-AAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 103 GQQCIFDVYGGDVSFAG-EILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDGskGVIMG 181
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTAT--SEND--GTIMG 154
|
170 180 190
....*....|....*....|....*....|..
gi 2130438548 182 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLH 213
Cdd:pfam00117 155 IRHKKLPIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
23-236 |
5.24e-59 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 199.12 E-value: 5.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDL--IAKNPTQLVISPGPGHPgTDSGISRDAIKHFAG-KIPIFG 99
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEaaVAAQFDGVLLSPGPGTP-ERAGASIDMVRACAAaGTPLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 100 VCMGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIAkedgsKGVI 179
Cdd:PRK07765 82 VCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTD-----SGVI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2130438548 180 MGVRHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQGGTWAEN--ERLQKETrAKAART 236
Cdd:PRK07765 157 MAVRHRELPIHGVQFHPESVLTEGGHRMLANWLTVCGWAPDEAlvRRLENEV-AAAVAP 214
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
529-753 |
2.18e-58 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 196.41 E-value: 2.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVdhetalsisqavhmskktgstevssqasksardfFNINAEVIRKR 608
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKAGADYLGLIFSESSKRQV----------------------------------SPEQAQELRSP 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 GPL-LVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFIP--VPVIRKFKPGQ----VGLATRGFHAV-PLLDSGA 680
Cdd:pfam00697 47 VPLlLVGVFVNQPIDDVLRIAQVLGLDVVQLHGDEDQEYENLLPtgVPVIKAIWVPDsvdtVDIARRADHVDlPLLDSGA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130438548 681 -GSGEMLNLESVKKELEKdeQVTVLLAGGLGPSNVAETVKSLGalaerVIGVDVSSGVEEGGKQSLEKIREFVK 753
Cdd:pfam00697 127 gGTGELFDWSLVSKWLKS--GLKVILAGGLNPDNVVEAIKTPG-----VIGVDVSSGVETNGIKDLNKIRKFVQ 193
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
529-755 |
1.54e-52 |
|
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: 180.85 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaevirkr 608
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKR--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 gpllVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFIP----VPVIRKFKPG-----QVGLATRGFHAVPLLDS- 678
Cdd:cd00405 54 ----VGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYCAQLRarlgLPVIKAIRVKdeedlEKAAAYAGEVDAILLDSk 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 679 ----GAGSGEMLNLESVKKELEKdeqVTVLLAGGLGPSNVAETVKSLgalaeRVIGVDVSSGVE-EGGKQSLEKIREFVK 753
Cdd:cd00405 130 sgggGGGTGKTFDWSLLRGLASR---KPVILAGGLTPDNVAEAIRLV-----RPYGVDVSSGVEtSPGIKDPEKIRAFIE 201
|
..
gi 2130438548 754 AA 755
Cdd:cd00405 202 AA 203
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
300-511 |
2.08e-46 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 176.37 E-value: 2.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 300 VALCAEIKRASPSKGVFAlDIDAPSQ-ARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDE 378
Cdd:PRK13802 50 IPVIAEIKRASPSKGHLS-DIPDPAAlAREYEQGGASAISVLTEGRRFLGSLDDFDKVRAAVH-IP----VLRKDFIVTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 379 YQILEARLAGADTVLLIVKMLDYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGR 458
Cdd:PRK13802 124 YQIWEARAHGADLVLLIVAALDDAQLKHLLDLAHELGMTVLVETHTREEIERAIAAGAKVIGINARNLKDLKVDVNKYNE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2130438548 459 LRSMVPNDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:PRK13802 204 LAADLPDDVIKVAESGVFGAVEVEDYARAGADAVLVGEGVATADDHELAVERL 256
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
21-311 |
6.16e-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: 6.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 21 SNLILIDNYDSFTWNVYQYLVLEGAKVTVFRND---QITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPI 97
Cdd:PRK09522 2 ADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVP-SEAGCMPELLTRLRGKLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 98 FGVCMGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLPQDLPVTRYHSLAGTHVtlPECLEVTSWIakedgsKG 177
Cdd:PRK09522 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNI--PAGLTINAHF------NG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 178 VIMGVRHKEYTIEGVQFHPESILSAEGRGMFRNFLhmqggTWAenerLQKetrakaaRTKSGTSTPkksnILQKIYahrk 257
Cdd:PRK09522 153 MVMAVRHDADRVCGFQFHPESILTTQGARLLEQTL-----AWA----QQK-------LEPTNTLQP----ILEKLY---- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130438548 258 aavdaQKQIPSQRLSD--LQAAYNLSLAPPQI--SLVD-RLR-NSPFDV--ALCAEIKRASP 311
Cdd:PRK09522 209 -----QAQTLSQQESHqlFSAVVRGELKPEQLaaALVSmKIRgEHPNEIagAATALLENAAP 265
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
529-757 |
2.60e-44 |
|
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: 158.38 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaevirkr 608
Cdd:COG0135 4 VKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKK--------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 gpllVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFI----PVPVIRKFKPGQ---VGLATRGFHAVP--LLDSG 679
Cdd:COG0135 57 ----VGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYCAALrerlGLPVIKAIRVGDgadLEEAAAYAPVADalLLDAK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 680 A-----GSGEMLNLESVKKElekDEQVTVLLAGGLGPSNVAETVKSLGALaerviGVDVSSGVE-EGGKQSLEKIREFVK 753
Cdd:COG0135 133 VpglygGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVRPY-----GVDVSSGVEsAPGVKDPDKIRAFVE 204
|
....
gi 2130438548 754 AAKS 757
Cdd:COG0135 205 AVRA 208
|
|
| PLN02460 |
PLN02460 |
indole-3-glycerol-phosphate synthase |
235-511 |
4.92e-42 |
|
indole-3-glycerol-phosphate synthase
Pssm-ID: 215254 Cd Length: 338 Bit Score: 156.48 E-value: 4.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 235 RTKSGTSTPKksNILQKIYAHRKAAVDAQKQipSQRLSDLQAAynLSLAPPQISLVDRLRNS------PfdvALCAEIKR 308
Cdd:PLN02460 57 RLQNEGNTPR--NILEEIVWYKDVEVAQMKE--RKPLYLLKKA--LQNAPPARDFVGALRAAhkrtgqP---GLIAEVKK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 309 ASPSKGVFALDIDAPSQARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNGMPnrpaVLRKEFIFDEYQILEARLAG 388
Cdd:PLN02460 128 ASPSRGVLRENFDPVEIAQAYEKGGAACLSVLTDEKYFQGSFENLEAIRNAGVKCP----LLCKEFIVDAWQIYYARSKG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 389 ADTVLLIVKMLDYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKL-GAKVIGVNNRNLESFEVDLGTTGRL------RS 461
Cdd:PLN02460 204 ADAILLIAAVLPDLDIKYMLKICKSLGMAALIEVHDEREMDRVLGIeGVELIGINNRSLETFEVDISNTKKLlegergEQ 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2130438548 462 MVPNDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 511
Cdd:PLN02460 284 IREKGIIVVGESGLFTPDDVAYVQNAGVKAVLVGESLVKQDDPGKGIAGL 333
|
|
| PRK13957 |
PRK13957 |
indole-3-glycerol-phosphate synthase; Provisional |
264-503 |
1.11e-38 |
|
indole-3-glycerol-phosphate synthase; Provisional
Pssm-ID: 140013 Cd Length: 247 Bit Score: 143.87 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 264 KQIPSQRLSDLQAAYNLSLAPPQ-ISLVDRLRNSPFDValCAEIKRASPSKGVFALDIDAPSQARKYALAGASVISVLTE 342
Cdd:PRK13957 6 REIIETKQNEIEKISRWDPLPDRgLPLRDSLKSRSFSI--IAECKRKSPSAGELRADYHPVQIAKTYETLGASAISVLTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 343 PEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLDYELLERLYKYSLSLGMEPLVEV 422
Cdd:PRK13957 84 QSYFGGSLEDLKSVSSELK-IP----VLRKDFILDEIQIREARAFGASAILLIVRILTPSQIKSFLKHASSLGMDVLVEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 423 QNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPNDTFLCALSGINTHQDvLDCKRDGVNGILVGEAIMRAP 502
Cdd:PRK13957 159 HTEDEAKLALDCGAEIIGINTRDLDTFQIHQNLVEEVAAFLPPNIVKVGESGIESRSD-LDKFRKLVDAALIGTYFMEKK 237
|
.
gi 2130438548 503 D 503
Cdd:PRK13957 238 D 238
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
7-207 |
1.13e-37 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 150.45 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 7 SPHDSDPSPLVETASNLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDqITIDDLIAKNPTQLVISPGPGHPgTDSGISRD 86
Cdd:PRK13566 513 LSAEEPDAAAVGEGKRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRP-SDFDCKAT 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 87 AIKHFAGKIPIFGVCMGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGA-YAGLPQDLPVTRYHSLAGTHVTLPECLEV 165
Cdd:PRK13566 591 IDAALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGRlFSGLPEEFTVGRYHSLFADPETLPDELLV 670
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2130438548 166 TSwiAKEDGskgVIMGVRHKEYTIEGVQFHPESILSAEGR-GM 207
Cdd:PRK13566 671 TA--ETEDG---VIMAIEHKTLPVAAVQFHPESIMTLGGDvGL 708
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
529-759 |
2.60e-37 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 138.79 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 529 VKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaevirkr 608
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVKV--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 609 gpllVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPLEWANFI----PVPVIRKFK---PGQVGLATRGFHAV--PLLDSG 679
Cdd:PRK01222 58 ----VGVFVNASDEEIDEIVETVPLDLLQLHGDETPEFCRQLkrryGLPVIKALRvrsAGDLEAAAAYYGDAdgLLLDAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 680 A----GSGEMLNLESVKKELEKDeqvtVLLAGGLGPSNVAETVKSLGALaerviGVDVSSGVEEG-GKQSLEKIREFVKA 754
Cdd:PRK01222 134 VglpgGTGKTFDWSLLPAGLAKP----WILAGGLNPDNVAEAIRQVRPY-----GVDVSSGVESApGIKDPEKIRAFIEA 204
|
....*
gi 2130438548 755 AKSVR 759
Cdd:PRK01222 205 VKSAD 209
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
21-204 |
8.71e-33 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 125.73 E-value: 8.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 21 SNLILIDNYDSFTWNVYQYLVLEGAKVTVFRNdQITIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGV 100
Cdd:PRK05637 2 THVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHP-RDAGNMMALIDRTLGQIPLLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 101 CMGQQCIFDVYGGDVSFAGEIlHGKTSPLCHDGKGA----YAGLPQD------------LPVTRYHSLAGTHVtlPECLE 164
Cdd:PRK05637 80 CLGFQALLEHHGGKVEPCGPV-HGTTDNMILTDAGVqspvFAGLATDvepdhpeipgrkVPIARYHSLGCVVA--PDGME 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2130438548 165 VTSWIAKEDGSkgVIMGVRHKEYTIEGVQFHPESILSAEG 204
Cdd:PRK05637 157 SLGTCSSEIGP--VIMAAETTDGKAIGLQFHPESVLSPTG 194
|
|
| PLN02363 |
PLN02363 |
phosphoribosylanthranilate isomerase |
499-759 |
3.08e-32 |
|
phosphoribosylanthranilate isomerase
Pssm-ID: 215207 Cd Length: 256 Bit Score: 125.74 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 499 MRAPDATQFIRELC---------AGLTGPVPKSAAEPL---------LVKICGTRSAEAATEAIKAGADLVGMILVPGTK 560
Cdd:PLN02363 1 SKTSKSGLSNRKVSfsrvgyaqnRKLSCSVSSENVAPKddergkdrpLVKMCGITSARDAAMAVEAGADFIGMILWPKSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 561 RCVDHETALSISQAVhmskktgstevssqasksardffninaeviRKRGPLLVGVFMNQPIEEVLEKQRLYDLDIVQLHG 640
Cdd:PLN02363 81 RSISLSVAKEISQVA------------------------------REGGAKPVGVFVDDDANTILRAADSSDLELVQLHG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 641 DEPLEWANFIP--VPVIRKFKPGQVGLATRGFHAVP-------LLDSG-AGSGEMLNLESVKKELEKDEQVTvLLAGGLG 710
Cdd:PLN02363 131 NGSRAAFSRLVreRKVIYVLNANEDGKLLNVVPEEDchladwiLVDSAtGGSGKGFNWQNFKLPSVRSRNGW-LLAGGLT 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2130438548 711 PSNVAETVKSLgalaeRVIGVDVSSGVE--EGGKQSLEKIREFVKAAKSVR 759
Cdd:PLN02363 210 PENVHEAVSLL-----KPTGVDVSSGICgpDGIRKDPSKISSFISAVKSVA 255
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
24-219 |
4.31e-30 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 127.66 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 24 ILIDNYDSFTWNVYQYL-VLEGAKVTVFRNDQITIDD----LIAKNP-TQLVISPGPGHP--GTDSGIS-------RDai 88
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELsIVNGVPPVVVRNDEWTWEEvyhyLYEEKAfDNIVISPGPGSPtcPADIGIClrlllecRD-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 89 khfagkIPIFGVCMGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLP----QDLPVTRYHSLAGTHVTLPECLE 164
Cdd:PLN02889 163 ------IPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAESLPKELV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 165 VTSWIAKED------------------------------------------------GSKGVIMGVRHKEYTIEGVQFHP 196
Cdd:PLN02889 237 PIAWTSSSDtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermQNGKILMGIMHSTRPHYGLQFHP 316
|
250 260
....*....|....*....|...
gi 2130438548 197 ESILSAEGRGMFRNFLHMQGGTW 219
Cdd:PLN02889 317 ESIATCYGRQIFKNFREITQDYW 339
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
22-248 |
1.30e-27 |
|
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate.
Pssm-ID: 273821 [Multi-domain] Cd Length: 742 Bit Score: 119.24 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 22 NLILIDNYDSFTWNVYQYL--VLE-GAKVTVFRNDQITiDDLIAKNP--TQLVISPGPGHPGT--DSGISRDAIK-HFAG 93
Cdd:TIGR01823 7 HVLFIDSYDSFTYNVVRLLeqQTDiSVHVTTVHSDTFQ-DQLLELLPlfDAIVVGPGPGNPNNaqDMGIISELWElANLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 94 KIPIFGVCMGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGAYAGLpQDLPVTRYHSLagtHVTLPECLEVTSWIAKED 173
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSL---YANPEGIDTLLPLCLTED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 174 GSKGVIMGVRHKEYTIEGVQFHPESILSAEGRG-MFRNFLHM------QGGTWaENERLQKE--------TRAKAART-- 236
Cdd:TIGR01823 162 EEGIILMSAQTKKKPWFGVQYHPESCCSELGSGkLVSNFLKLafinnvKTGRW-EKKKLNGSfsdissrlDRTDDRDPiy 240
|
250
....*....|..
gi 2130438548 237 KSGTSTPKKSNI 248
Cdd:TIGR01823 241 KVKEKYPSGTTY 252
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
20-212 |
6.38e-27 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 108.29 E-value: 6.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 20 ASNLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDDliAKNPTQLVISPGP----GHPGTDSGISRdaikhFAGKI 95
Cdd:PRK06895 1 ATKLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDE--VENFSHILISPGPdvprAYPQLFAMLER-----YHQHK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 96 PIFGVCMGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKGA-YAGLPQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEdg 174
Cdd:PRK06895 74 SILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPlFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDEN-- 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 2130438548 175 skgVIMGVRHKEYTIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:PRK06895 152 ---VVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
56-213 |
4.56e-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: 85.83 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 56 TIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGKIPIFGVCMGQQCIFDVYGGDVSFAGEILHGKTSPLCHDGKG 135
Cdd:TIGR00888 33 PLEEIREKNPKGIILSGGPSSV-YAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKREYGKAELEILDEDD 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130438548 136 AYAGLPQDLPVTRYHslaGTHVT-LPECLEVtswIAKEDGSKGVIMgvRHKEYTIEGVQFHPESILSAEGRGMFRNFLH 213
Cdd:TIGR00888 112 LFRGLPDESTVWMSH---GDKVKeLPEGFKV---LATSDNCPVAAM--AHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
55-212 |
8.37e-17 |
|
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: 78.73 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 55 ITIDDLIAKNPTQLVISPGPgHPGTDSGISRDAIKHFAGKIPIFGVCMGQQCIFDVYGGDVSFAG-------EILHGKTS 127
Cdd:cd01742 32 TPLEEIKLKNPKGIILSGGP-SSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDkreygkaEIEIDDSS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 128 PLchdgkgaYAGLPQDLPVTRYHslaGTHVT-LPECLEVtswIAKEDGSKgvIMGVRHKEYTIEGVQFHPESILSAEGRG 206
Cdd:cd01742 111 PL-------FEGLPDEQTVWMSH---GDEVVkLPEGFKV---IASSDNCP--VAAIANEEKKIYGVQFHPEVTHTEKGKE 175
|
....*.
gi 2130438548 207 MFRNFL 212
Cdd:cd01742 176 ILKNFL 181
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
54-213 |
3.33e-14 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 75.85 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 54 QITIDDLIAKNPTQLVISPGP------GHPGTDSGIsrdaikhFAGKIPIFGVCMGQQCIFDVYGGDVSFAGEILHGKTS 127
Cdd:PRK00074 36 DISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEI-------FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 128 PLCHDGKGAYAGLPQDLPVTRYHslaGTHVT-LPECLEVtswIAKEDGSKgvIMGVRHKEYTIEGVQFHPESILSAEGRG 206
Cdd:PRK00074 109 LEVDNDSPLFKGLPEEQDVWMSH---GDKVTeLPEGFKV---IASTENCP--IAAIANEERKFYGVQFHPEVTHTPQGKK 180
|
....*..
gi 2130438548 207 MFRNFLH 213
Cdd:PRK00074 181 LLENFVF 187
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
23-212 |
8.86e-14 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 70.27 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 23 LILIDNYDSFT---WNVYQYLvleGAKVTVFRNDqITIDDlIAKNPTQLVISPGPGHpgTDSGISRDAIKHFagKIPIFG 99
Cdd:PRK00758 2 IVVVDNGGQYNhliHRTLRYL---GVDAKIIPNT-TPVEE-IKAFEDGLILSGGPDI--ERAGNCPEYLKEL--DVPILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 100 VCMGQQCIFDVYGGDVSFA--GEILHGKTSPLCHDGkgAYAGLPQDLPVTRYHslAGTHVTLPECLEVTswiAKEDGSKg 177
Cdd:PRK00758 73 ICLGHQLIAKAFGGEVGRGeyGEYALVEVEILDEDD--ILKGLPPEIRVWASH--ADEVKELPDGFEIL---ARSDICE- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 2130438548 178 vIMGVRHKEYTIEGVQFHPESILSAEGRGMFRNFL 212
Cdd:PRK00758 145 -VEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFL 178
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
34-212 |
9.12e-14 |
|
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: 70.22 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 34 WNVYQYLVLEGAKVTVFRNDQiTIDDLIAKNPTQLVISPGPGHPgTDSGISRDAIKHFAGK-IPIFGVCMGQQCIFDVYG 112
Cdd:cd01744 10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDP-ALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 113 GDvsfageilhgktsplCHDGKGAYAGLPQdlPVTRY-----------HSLAGTHVTLPECLEVTsWIAKEDGSkgvIMG 181
Cdd:cd01744 88 AK---------------TYKMKFGHRGSNH--PVKDLitgrvyitsqnHGYAVDPDSLPGGLEVT-HVNLNDGT---VEG 146
|
170 180 190
....*....|....*....|....*....|....
gi 2130438548 182 VRHKEYTIEGVQFHPESilSA---EGRGMFRNFL 212
Cdd:cd01744 147 IRHKDLPVFSVQFHPEA--SPgphDTEYLFDEFL 178
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
525-756 |
1.18e-12 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 71.38 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 525 EPLLVKICGTRSAEAATEAIKAGADLVGMILVPGTKRCVDHET-ALSISQAVhmskktgstevssqasksardffninae 603
Cdd:PRK13803 1 KQPKIKICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVGNKFlAPNLEKAI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 604 viRKRGPLLVGVFMNQPIEEVLEKQRLYDLDIVQLHGDEPL---EWANFIPVPVIRKFKPGQVGLAT--------RGFHA 672
Cdd:PRK13803 53 --RKAGGRPVGVFVNESAKAMLKFSKKNGIDFVQLHGAESKaepAYCQRIYKKSIKKIGSFLIDDAFgfevldeyRDHVK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 673 VPLLDSGA----GSGEMLNLESVKkelEKDEQVTVLLAGGLGPSNVAeTVKSLGalAERVIGVDVSSGVE-EGGKQSLEK 747
Cdd:PRK13803 131 YFLFDNKTkiygGSGKSFDWEKFY---NYNFKFPFFLSGGLSPTNFD-RIINLT--HPQILGIDVSSGFEdSPGNKKLTL 204
|
....*....
gi 2130438548 748 IREFVKAAK 756
Cdd:PRK13803 205 LKSFITNVK 213
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
40-214 |
1.19e-11 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 67.02 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 40 LVLEGAKVTVFRNDqITIDDLIAKNPTQLVISPGPGHP-GTDSGIsrDAIKHFAG-KIPIFGVCMGQQCIfdvyggdvSF 117
Cdd:PRK12564 195 LAERGCRVTVVPAT-TTAEEILALNPDGVFLSNGPGDPaALDYAI--EMIRELLEkKIPIFGICLGHQLL--------AL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 118 AgeiLHGKTSPLchdgKGAYAGLPQdlPVTRyhsLAGTHV--------------TLPECLEVTsWIAKEDGSkgvIMGVR 183
Cdd:PRK12564 264 A---LGAKTYKM----KFGHRGANH--PVKD---LETGKVeitsqnhgfavdedSLPANLEVT-HVNLNDGT---VEGLR 327
|
170 180 190
....*....|....*....|....*....|....
gi 2130438548 184 HKEYTIEGVQFHPESilSA---EGRGMFRNFLHM 214
Cdd:PRK12564 328 HKDLPAFSVQYHPEA--SPgphDSAYLFDEFVEL 359
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
34-198 |
3.91e-10 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 62.51 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 34 WNVYQYLVLEGAKVTVFrNDQITIDDLIAKNPTQLVISPGPGHPGT-DSGISR--DAIKHfagKIPIFGVCMGQQCIfdv 110
Cdd:CHL00197 204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAiHYGIKTvkKLLKY---NIPIFGICMGHQIL--- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 111 yggdvSFAgeiLHGKTSPL--CHDGKGAYAGLPQDLPVT-RYHSLAgthVTLPECLEVTSWIAKEDGSKGVIMGVRHKEY 187
Cdd:CHL00197 277 -----SLA---LEAKTFKLkfGHRGLNHPSGLNQQVEITsQNHGFA---VNLESLAKNKFYITHFNLNDGTVAGISHSPK 345
|
170
....*....|.
gi 2130438548 188 TIEGVQFHPES 198
Cdd:CHL00197 346 PYFSVQYHPEA 356
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
35-198 |
9.49e-10 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 61.53 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 35 NVYQYLVLEGAKVTVFRNDQITIDDLiAKNPTQLVISPGPGHPgtdSGI--SRDAIKHFAGKIPIFGVCMGQQCIFDVYG 112
Cdd:PLN02771 253 NILRRLASYGCKITVVPSTWPASEAL-KMKPDGVLFSNGPGDP---SAVpyAVETVKELLGKVPVFGICMGHQLLGQALG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 113 GDVSFAGEILHGKTSPLCHDGKGAYAGLPQDlpvtryHSLAGTHVTLPECLEVTSwIAKEDGSkgvIMGVRHKEYTIEGV 192
Cdd:PLN02771 329 GKTFKMKFGHHGGNHPVRNNRTGRVEISAQN------HNYAVDPASLPEGVEVTH-VNLNDGS---CAGLAFPALNVMSL 398
|
....*.
gi 2130438548 193 QFHPES 198
Cdd:PLN02771 399 QYHPEA 404
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
24-197 |
1.28e-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: 59.19 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 24 ILI----DNYDSFTWNVYQYLVLEGAKVTVFR--NDQITIDDLIAKNPTQLVISPGPGHPGTDSGISRDA---IKH-FAG 93
Cdd:COG0518 2 ILIldhdPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEpalIREaFEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 94 KIPIFGVCMGQQCIFDVYGGDVSFAG--EIlhGKT-------SPLChdgkgayAGLPQDLPVtrYHSlagtH----VTLP 160
Cdd:COG0518 82 GKPVLGICYGAQLLAHALGGKVEPGPgrEI--GWApvelteaDPLF-------AGLPDEFTV--WMS----HgdtvTELP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 2130438548 161 ECLEVtswIAKEDGSKgvIMGVRHKEYTIeGVQFHPE 197
Cdd:COG0518 147 EGAEV---LASSDNCP--NQAFRYGRRVY-GVQFHPE 177
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
40-198 |
4.26e-09 |
|
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: 58.88 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 40 LVLEGAKVTVFRNDqITIDDLIAKNPTQLVISPGPGHPG-TDSGIsrDAIKHFAGK-IPIFGVCMGQQCI-----FDVY- 111
Cdd:COG0505 194 LAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAaLDYAI--ETIRELLGKgIPIFGICLGHQLLalalgAKTYk 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 112 ------GG-----DVSfAGEIL-----HGktsplchdgkgaYAGLPQDLPVTRyhsLAGTHVTLpeclevtswiakEDGS 175
Cdd:COG0505 271 lkfghrGAnhpvkDLE-TGRVEitsqnHG------------FAVDEDSLPATD---LEVTHVNL------------NDGT 322
|
170 180
....*....|....*....|...
gi 2130438548 176 kgvIMGVRHKEYTIEGVQFHPES 198
Cdd:COG0505 323 ---VEGLRHKDLPAFSVQYHPEA 342
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
57-212 |
4.86e-09 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 59.70 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 57 IDDLIAKNPTQLVISPGP------GHPGTDSGIsrdaIKHFAGK-IPIFGVCMGQQCIFDVYGGDVSFAGEILHGKTSPL 129
Cdd:PLN02347 46 LDRIASLNPRVVILSGGPhsvhveGAPTVPEGF----FDYCRERgVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 130 CHDGKGAYAGLPQDLPVTRYHSLAGTHVTLPECLEVtswIAKEDgsKGVIMGVRHKEYTIEGVQFHPESILSAEGRGMFR 209
Cdd:PLN02347 122 VVCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEV---VAKSV--QGAVVAIENRERRIYGLQYHPEVTHSPKGMETLR 196
|
...
gi 2130438548 210 NFL 212
Cdd:PLN02347 197 HFL 199
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
40-197 |
5.37e-09 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 58.75 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 40 LVLEGAKVTVFRNDQiTIDDLIAKNPTQLVISPGPGHPGTDSGISRDAIKHFAGkIPIFGVCMGQQCIFDVYGGDVsfag 119
Cdd:PRK12838 185 LSKRGCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISS-YPILGICLGHQLIALALGADT---- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 120 eilhgKTSPLCHDGkgayAGLP-QDLPVTRYHSLAGTH--VTLPECLEVTSWIAK-EDGSKGVIMGVRHKEYTIEGVQFH 195
Cdd:PRK12838 259 -----EKLPFGHRG----ANHPvIDLTTGRVWMTSQNHgyVVDEDSLDGTPLSVRfFNVNDGSIEGLRHKKKPVLSVQFH 329
|
..
gi 2130438548 196 PE 197
Cdd:PRK12838 330 PE 331
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
24-108 |
1.72e-07 |
|
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: 50.29 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 24 ILIDNYDSFTW---NVYQYLVLEGAKVTVFRNDQITIDDLI-AKNPTQLVISPGPGHPGT---DSGISRDAIKHFAGKIP 96
Cdd:cd01653 2 AVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVESDVdLDDYDGLILPGGPGTPDDlarDEALLALLREAAAAGKP 81
|
90
....*....|..
gi 2130438548 97 IFGVCMGQQCIF 108
Cdd:cd01653 82 ILGICLGAQLLV 93
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
85-211 |
4.43e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 51.04 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 85 RDA-----IKHF-AGKIPIFGVCMGQQCIFDVYGGDvsfageiLHgktsplchdgkgayaglpQDLPVTRYHSLAgthV- 157
Cdd:cd01745 85 RDAfelalLRAAlERGKPILGICRGMQLLNVALGGT-------LY------------------QDIRVNSLHHQA---Ik 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2130438548 158 TLPECLEVTSWiaKEDgskGVIMGVRHKEYT-IEGVQFHPESIL--SAEGRGMFRNF 211
Cdd:cd01745 137 RLADGLRVEAR--APD---GVIEAIESPDRPfVLGVQWHPEWLAdtDPDSLKLFEAF 188
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
24-107 |
9.26e-07 |
|
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: 47.58 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 24 ILIDNYDSFTW---NVYQYLVLEGAKVTVFRNDQITIDDLI-AKNPTQLVISPGPGHPGTDSGISR--DAIKHFAG-KIP 96
Cdd:cd03128 2 AVLLFGGSEELelaSPLDALREAGAEVDVVSPDGGPVESDVdLDDYDGLILPGGPGTPDDLAWDEAllALLREAAAaGKP 81
|
90
....*....|.
gi 2130438548 97 IFGVCMGQQCI 107
Cdd:cd03128 82 VLGICLGAQLL 92
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
85-212 |
1.57e-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: 153212 [Multi-domain] Cd Length: 188 Bit Score: 43.39 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 85 RDAIKHfagKIPIFGVCMGQQCIFDVYGGDV---SFAGEILH--------GKTSPLchdgkgaYAGLPQDLPVtrYHSLA 153
Cdd:cd01741 75 RQALAA---GKPVLGICLGHQLLARALGGKVgrnPKGWEIGWfpvtlteaGKADPL-------FAGLPDEFPV--FHWHG 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2130438548 154 GTHVTLPECLEVtswIAKEDGSKgvIMGVRHKEYTIeGVQFHPEsilsaegRGMFRNFL 212
Cdd:cd01741 143 DTVVELPPGAVL---LASSEACP--NQAFRYGDRAL-GLQFHPE-------ERLLRNFL 188
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
72-211 |
6.07e-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: 42.08 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 72 PGPGHPGTDSGisRDA-----IKHF-AGKIPIFGVCMGQQcIFDVY-GG----DVS--FAGEILHGKTSplchdgkgaya 138
Cdd:COG2071 70 PHPELGPIDPE--RDAfelalIRAAlERGKPVLGICRGMQ-LLNVAlGGtlyqDLPdqVPGALDHRQPA----------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130438548 139 glPQDLPV--------TRYHSLAGTHV------------TLPECLEVTSWiAkEDgskGVIMGVRHKEYT-IEGVQFHPE 197
Cdd:COG2071 136 --PRYAPRhtveiepgSRLARILGEEEirvnslhhqavkRLGPGLRVSAR-A-PD---GVIEAIESPGAPfVLGVQWHPE 208
|
170
....*....|....*.
gi 2130438548 198 --SILSAEGRGMFRNF 211
Cdd:COG2071 209 wlAASDPLSRRLFEAF 224
|
|
| |
