|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
252-513 |
1.89e-136 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 402.83 E-value: 1.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 252 LQKIYAHRKAAVDAQKQIPSLrpSDLQAAYNlsiAPPQISLVDRLRNSPFDVALCAEIKRASPSKGVFALDIDAPSQARK 331
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPL--ADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 332 YALAGASVISVLTEPEWFKGSIDDLRAVRQVLNGMpnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLERLY 411
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 412 KYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDCKRDG 491
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 758991969 492 VNGILVGEAIMRAPDATQFIRE 513
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
292-514 |
1.45e-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: 329.81 E-value: 1.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 292 LVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLngmpnRPA 371
Cdd:cd00331 1 FKAALKRPG-GLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 372 VLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLES 451
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758991969 452 FEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
249-514 |
2.39e-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: 328.14 E-value: 2.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 249 SNILQKIYAHRKAAVDAQKQIPSLrpSDLQAAynLSIAPPQISLVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQ 328
Cdd:COG0134 1 PTILDKIVAHKREEVAARKARVPL--AELEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 329 ARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgmpnRPaVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLE 408
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAAVD----LP-VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 409 RLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDCK 488
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*.
gi 758991969 489 RDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALREL 256
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
248-514 |
2.17e-106 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 325.57 E-value: 2.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 248 KSNILQKIYAHRKAAVDAQKQIPSLRpsDLQAAynLSIAPPQISLVDRLRNSPfdVALCAEIKRASPSKGVFALDIDAPS 327
Cdd:PRK00278 1 MMDILDKIVAYKREEVAARKAQVPLA--ELKAR--AAAAPPPRDFAAALRAGK--PAVIAEVKKASPSKGVIREDFDPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 328 QARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELL 407
Cdd:PRK00278 75 IAKAYEAGGAACLSVLTDERFFQGSLEYLRAARAAVS-LP----VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 408 ERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDC 487
Cdd:PRK00278 150 KELLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRL 229
|
250 260
....*....|....*....|....*..
gi 758991969 488 KRDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:PRK00278 230 AKAGADAVLVGESLMRADDPGAALREL 256
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
26-220 |
1.17e-100 |
|
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: 308.12 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTP-EEAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMGV 185
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAW--TED---GEIMGI 154
|
170 180 190
....*....|....*....|....*....|....*
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQGG 220
Cdd:COG0512 155 RHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
25-217 |
2.12e-97 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 299.74 E-value: 2.12e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 25 NLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVC 104
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTP-AEAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 105 MGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMG 184
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW--TDD---GEIMG 154
|
170 180 190
....*....|....*....|....*....|...
gi 758991969 185 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 217
Cdd:PRK05670 155 VRHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
26-215 |
3.79e-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: 288.28 E-value: 3.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHP-EDAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiakedGSKGVIMGV 185
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAS-----TEDGVIMAL 154
|
170 180 190
....*....|....*....|....*....|
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:cd01743 155 RHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
26-216 |
1.86e-72 |
|
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: 234.30 E-value: 1.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTP-NEAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDgskgVIMGV 185
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI----EIMAI 156
|
170 180 190
....*....|....*....|....*....|.
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFLH 216
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLH 187
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
27-216 |
1.47e-63 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 210.17 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 27 ILIDNYDSFTWNVYQYLVLEGAKVTVFRNDqITIDELIAKNPTQLVISPGPGHPGtDSGISRDAIRH-FAGKIPIFGVCM 105
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPG-AAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAG-EILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDGskGVIMG 184
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTAT--SEND--GTIMG 154
|
170 180 190
....*....|....*....|....*....|..
gi 758991969 185 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLH 216
Cdd:pfam00117 155 IRHKKLPIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
29-217 |
9.26e-63 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 208.35 E-value: 9.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 29 IDNYDSFTWNVYQYL--VLEGAKVTVFRNdQITIDELIAKNPTQLVISPGPGHPGT--DSGISRDAIRHFAGKIPIFGVC 104
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKNdrDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 105 MGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVtlPECLEVTSwiAKEDGSKGVIMG 184
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEV--PDCFEVTA--TTDHDGEELVMG 156
|
170 180 190
....*....|....*....|....*....|...
gi 758991969 185 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 217
Cdd:NF041322 157 IRHREHPIECVQFHPESVLTGVGHDVIENFLAA 189
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
566-756 |
5.43e-60 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 201.04 E-value: 5.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 566 VDHETALSISQAVHMSKKtGSTEVSSQAS-KSARDFFNINAEIIRKRGPL-LVGVFMNQPLEEVLEKQHLYDLDIVQLHG 643
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKA-GADYLGLIFSeSSKRQVSPEQAQELRSPVPLlLVGVFVNQPIDDVLRIAQVLGLDVVQLHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 644 DEPLEWANLIP--VPVVRKFKPGQ----VGLATRGYHAV-PLLDSGA-GSGTLLDLESVKKELEKdeQVTVLLAGGLEPS 715
Cdd:pfam00697 80 DEDQEYENLLPtgVPVIKAIWVPDsvdtVDIARRADHVDlPLLDSGAgGTGELFDWSLVSKWLKS--GLKVILAGGLNPD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 758991969 716 NVVETVKSLGPlservIGVDVSSGVEEGGKQSLEKIREFVK 756
Cdd:pfam00697 158 NVVEAIKTPGV-----IGVDVSSGVETNGIKDLNKIRKFVQ 193
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
532-758 |
7.98e-43 |
|
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: 154.27 E-value: 7.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 532 VKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaeiirkr 611
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKR--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 612 gpllVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPLEWANLIP----VPVVRKFKPG-----QVGLATRGYHAVPLLDS- 681
Cdd:cd00405 54 ----VGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYCAQLRarlgLPVIKAIRVKdeedlEKAAAYAGEVDAILLDSk 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 682 ----GAGSGTLLDLESVKKELEKdeqVTVLLAGGLEPSNVVETVKSLGPlservIGVDVSSGVE-EGGKQSLEKIREFVK 756
Cdd:cd00405 130 sgggGGGTGKTFDWSLLRGLASR---KPVILAGGLTPDNVAEAIRLVRP-----YGVDVSSGVEtSPGIKDPEKIRAFIE 201
|
..
gi 758991969 757 AA 758
Cdd:cd00405 202 AA 203
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
532-760 |
9.77e-35 |
|
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: 131.41 E-value: 9.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 532 VKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaeiirkr 611
Cdd:COG0135 4 VKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKK--------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 612 gpllVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPLEW----ANLIPVPVVRKFKPGQVG--LATRGYHAVP---LLDSG 682
Cdd:COG0135 57 ----VGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYcaalRERLGLPVIKAIRVGDGAdlEEAAAYAPVAdalLLDAK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 683 A-----GSGTLLDLESVKKElekDEQVTVLLAGGLEPSNVVETVKSLGPLserviGVDVSSGVE-EGGKQSLEKIREFVK 756
Cdd:COG0135 133 VpglygGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVRPY-----GVDVSSGVEsAPGVKDPDKIRAFVE 204
|
....
gi 758991969 757 AAKS 760
Cdd:COG0135 205 AVRA 208
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
532-762 |
3.97e-28 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 112.59 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 532 VKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaeiirkr 611
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVKV--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 612 gpllVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPLE----WANLIPVPVVRKFKPGQVG--LATRGYHAVP---LLDSG 682
Cdd:PRK01222 58 ----VGVFVNASDEEIDEIVETVPLDLLQLHGDETPEfcrqLKRRYGLPVIKALRVRSAGdlEAAAAYYGDAdglLLDAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 683 A----GSGTLLDLESVKKELEKDeqvtVLLAGGLEPSNVVETVKSLGPLserviGVDVSSGVEEG-GKQSLEKIREFVKA 757
Cdd:PRK01222 134 VglpgGTGKTFDWSLLPAGLAKP----WILAGGLNPDNVAEAIRQVRPY-----GVDVSSGVESApGIKDPEKIRAFIEA 204
|
....*
gi 758991969 758 AKSVR 762
Cdd:PRK01222 205 VKSAD 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
252-513 |
1.89e-136 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 402.83 E-value: 1.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 252 LQKIYAHRKAAVDAQKQIPSLrpSDLQAAYNlsiAPPQISLVDRLRNSPFDVALCAEIKRASPSKGVFALDIDAPSQARK 331
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPL--ADLQAAAR---APPTRSFYDALRESRGRPALIAEVKKASPSKGLIREDFDPAEIARV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 332 YALAGASVISVLTEPEWFKGSIDDLRAVRQVLNGMpnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLERLY 411
Cdd:pfam00218 76 YEAAGASAISVLTDPKYFQGSIEYLRAVRQAVSLP-----VLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 412 KYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDCKRDG 491
Cdd:pfam00218 151 AYARSLGMEVLVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKEHG 230
|
250 260
....*....|....*....|..
gi 758991969 492 VNGILVGEAIMRAPDATQFIRE 513
Cdd:pfam00218 231 ANAFLVGESLMRQEDVRAAIRE 252
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
292-514 |
1.45e-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: 329.81 E-value: 1.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 292 LVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLngmpnRPA 371
Cdd:cd00331 1 FKAALKRPG-GLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAV-----SLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 372 VLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLES 451
Cdd:cd00331 75 VLRKDFIIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758991969 452 FEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:cd00331 155 FEVDLNTTERLAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
249-514 |
2.39e-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: 328.14 E-value: 2.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 249 SNILQKIYAHRKAAVDAQKQIPSLrpSDLQAAynLSIAPPQISLVDRLRNSPfDVALCAEIKRASPSKGVFALDIDAPSQ 328
Cdd:COG0134 1 PTILDKIVAHKREEVAARKARVPL--AELEAR--AAAAPPPRDFAAALRAAG-GPAVIAEIKKASPSKGLIREDFDPAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 329 ARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgmpnRPaVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLE 408
Cdd:COG0134 76 ARAYEAGGAAAISVLTDEKFFQGSLEDLRAVRAAVD----LP-VLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 409 RLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDCK 488
Cdd:COG0134 151 ELLALAHSLGMDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLA 230
|
250 260
....*....|....*....|....*.
gi 758991969 489 RDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:COG0134 231 AAGADAFLVGEALMRAPDPGAALREL 256
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
248-514 |
2.17e-106 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 325.57 E-value: 2.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 248 KSNILQKIYAHRKAAVDAQKQIPSLRpsDLQAAynLSIAPPQISLVDRLRNSPfdVALCAEIKRASPSKGVFALDIDAPS 327
Cdd:PRK00278 1 MMDILDKIVAYKREEVAARKAQVPLA--ELKAR--AAAAPPPRDFAAALRAGK--PAVIAEVKKASPSKGVIREDFDPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 328 QARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELL 407
Cdd:PRK00278 75 IAKAYEAGGAACLSVLTDERFFQGSLEYLRAARAAVS-LP----VLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 408 ERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDC 487
Cdd:PRK00278 150 KELLDYAHSLGLDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRL 229
|
250 260
....*....|....*....|....*..
gi 758991969 488 KRDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:PRK00278 230 AKAGADAVLVGESLMRADDPGAALREL 256
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
26-220 |
1.17e-100 |
|
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: 308.12 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEALAPDGIVLSPGPGTP-EEAGISLEVIRAFAGKIPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMGV 185
Cdd:COG0512 80 GHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDRETLPDELEVTAW--TED---GEIMGI 154
|
170 180 190
....*....|....*....|....*....|....*
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQGG 220
Cdd:COG0512 155 RHRELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
25-217 |
2.12e-97 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 299.74 E-value: 2.12e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 25 NLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVC 104
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTP-AEAGISLELIREFAGKVPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 105 MGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDgskGVIMG 184
Cdd:PRK05670 80 LGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW--TDD---GEIMG 154
|
170 180 190
....*....|....*....|....*....|...
gi 758991969 185 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 217
Cdd:PRK05670 155 VRHKELPIYGVQFHPESILTEHGHKLLENFLEL 187
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
26-215 |
3.79e-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: 288.28 E-value: 3.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHP-EDAGISLEIIRALAGKVPILGVCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiakedGSKGVIMGV 185
Cdd:cd01743 80 GHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTAS-----TEDGVIMAL 154
|
170 180 190
....*....|....*....|....*....|
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:cd01743 155 RHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PRK09427 |
PRK09427 |
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
246-759 |
2.76e-89 |
|
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;
Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 288.25 E-value: 2.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 246 PKKSNILQKIYAHRKAAVDAQKQIPSLrpSDLQAaynlSIAPPQISLVDRLRNSpfDVALCAEIKRASPSKGVFALDIDA 325
Cdd:PRK09427 1 TMMPTVLAKIVADKAIWVAARKQQQPL--ASFQN----EIQPSDRSFYDALKGP--KTAFILECKKASPSKGLIRDDFDP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 326 PSQARKYAlAGASVISVLTEPEWFKGSIDDLRAVRQVLNgmpnRPaVLRKEFIFDEYQILEARLAGADTVLLIVKML--- 402
Cdd:PRK09427 73 AEIARVYK-HYASAISVLTDEKYFQGSFDFLPIVRAIVT----QP-ILCKDFIIDPYQIYLARYYGADAILLMLSVLdde 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 403 EYELLERLYKyslSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQ 482
Cdd:PRK09427 147 QYRQLAAVAH---SLNMGVLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPADVIVISESGIYTHA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 483 DVLDCKRdGVNGILVGEAIMRAPDATQFIRELCAGLtgpvpksaaepllVKICGTRSAEAAAEAIKAGADLVGMIMVPGT 562
Cdd:PRK09427 224 QVRELSP-FANGFLIGSSLMAEDDLELAVRKLILGE-------------NKVCGLTRPQDAKAAYDAGAVYGGLIFVEKS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 563 KRCVDHETALSISQAVhmskktgstevssqasksardffninaeiirkrgPL-LVGVFMNQPLEEVLEKQHLYDLDIVQL 641
Cdd:PRK09427 290 PRYVSLEQAQEIIAAA----------------------------------PLrYVGVFRNADIEDIVDIAKQLSLAAVQL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 642 HGDEPLEWAN----LIPVPV-VRKFKPGQVGLATRGYHAVP--LLDSGA-GSGTLLDLESVKKELEKDeqvtVLLAGGLE 713
Cdd:PRK09427 336 HGDEDQAYIDalreALPKTCqIWKAISVGDTLPARDLQHVDryLLDNGQgGTGQTFDWSLLPGQSLDN----VLLAGGLN 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 758991969 714 PSNVVETVKsLGPLserviGVDVSSGVEEG-GKQSLEKIREFVKAAK 759
Cdd:PRK09427 412 PDNCQQAAQ-LGCA-----GLDFNSGVESApGIKDAQKLASVFQTLR 452
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
26-218 |
1.35e-83 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 275.44 E-value: 1.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLV-LEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVC 104
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGeLGPEEIEVVRNDEITIEEIEALNPSHIVISPGPGRP-EEAGISVEVIRHFSGKVPILGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 105 MGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDGSkgvIMG 184
Cdd:PRK14607 81 LGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEASLPECLEVTAK--SDDGE---IMG 155
|
170 180 190
....*....|....*....|....*....|....
gi 758991969 185 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQ 218
Cdd:PRK14607 156 IRHKEHPIFGVQFHPESILTEEGKRILKNFLNYQ 189
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
26-215 |
9.60e-76 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 243.25 E-value: 9.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEALNPTHLVISPGPCTP-NEAGISLQAIEHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDGSKGVIMGV 185
Cdd:PRK08857 81 GHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFELTAWTELEDGSMDEIMGF 160
|
170 180 190
....*....|....*....|....*....|
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:PRK08857 161 QHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
26-216 |
1.88e-74 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 239.43 E-value: 1.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTP-DEAGISLDVIRHYAGRLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDgskgvIMGV 185
Cdd:PRK08007 81 GHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFEVTAWSETRE-----IMGI 155
|
170 180 190
....*....|....*....|....*....|.
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFLH 216
Cdd:PRK08007 156 RHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
26-216 |
1.86e-72 |
|
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: 234.30 E-value: 1.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTP-NEAGISLEAIRHFAGKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDgskgVIMGV 185
Cdd:TIGR00566 81 GHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENI----EIMAI 156
|
170 180 190
....*....|....*....|....*....|.
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFLH 216
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLH 187
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
26-215 |
7.97e-72 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 232.77 E-value: 7.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENMKPDFLMISPGPCSP-NEAGISMEVIRYFAGKIPIFGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAkedgsKGVIMGV 185
Cdd:PRK07649 81 GHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCLEVTSWTE-----EGEIMAI 155
|
170 180 190
....*....|....*....|....*....|
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:PRK07649 156 RHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
26-215 |
1.39e-70 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 229.36 E-value: 1.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSHLVISPGPCTP-NEAGISLAVIRHFADKLPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiAKEDGSKGVIMGV 185
Cdd:PRK06774 81 GHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAW-SERGGEMDEIMGI 159
|
170 180 190
....*....|....*....|....*....|
gi 758991969 186 RHKEYTIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:PRK06774 160 RHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
26-226 |
4.11e-65 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 215.82 E-value: 4.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKRKNPRGVLISPGPGTP-QDSGISLQTVLELGPLVPLFGVCM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGE-ILHGKTSPLRHDGKGA---YAGLSQDLPVTRYHSLAGTHVTLPE-CLEVTSWiaKEDgskG 180
Cdd:PLN02335 100 GLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDEKGEeglFSGLPNPFTAGRYHSLVIEKDTFPSdELEVTAW--TED---G 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 758991969 181 VIMGVRHKEYT-IEGVQFHPESILSAEGRGMFRNFLHMQGGTWAENE 226
Cdd:PLN02335 175 LIMAARHRKYKhIQGVQFHPESIITTEGKTIVRNFIKIIEKKESEKL 221
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
27-216 |
1.47e-63 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 210.17 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 27 ILIDNYDSFTWNVYQYLVLEGAKVTVFRNDqITIDELIAKNPTQLVISPGPGHPGtDSGISRDAIRH-FAGKIPIFGVCM 105
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPND-TPAEEILEENPDGIILSGGPGSPG-AAGGAIEAIREaRELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAG-EILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWiaKEDGskGVIMG 184
Cdd:pfam00117 79 GHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTAT--SEND--GTIMG 154
|
170 180 190
....*....|....*....|....*....|..
gi 758991969 185 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLH 216
Cdd:pfam00117 155 IRHKKLPIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
26-215 |
5.72e-63 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 208.82 E-value: 5.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCM 105
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNLNIRHIIISPGPGHP-RDSGISLDVISSYAPYIPILGVCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 106 GQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIakedgSKGVIMGV 185
Cdd:CHL00101 81 GHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAWT-----EDGLIMAC 155
|
170 180 190
....*....|....*....|....*....|.
gi 758991969 186 RHKEY-TIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:CHL00101 156 RHKKYkMLRGIQFHPESLLTTHGQQILRNFL 186
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
29-217 |
9.26e-63 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 208.35 E-value: 9.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 29 IDNYDSFTWNVYQYL--VLEGAKVTVFRNdQITIDELIAKNPTQLVISPGPGHPGT--DSGISRDAIRHFAGKIPIFGVC 104
Cdd:NF041322 2 VDNFDSFTYNLVEYVseQREHAETTVLKN-TASLAEVRAVDPDAIVISPGPGHPKNdrDVGVTADVLRELSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 105 MGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVtlPECLEVTSwiAKEDGSKGVIMG 184
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEV--PDCFEVTA--TTDHDGEELVMG 156
|
170 180 190
....*....|....*....|....*....|...
gi 758991969 185 VRHKEYTIEGVQFHPESILSAEGRGMFRNFLHM 217
Cdd:NF041322 157 IRHREHPIECVQFHPESVLTGVGHDVIENFLAA 189
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
566-756 |
5.43e-60 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 201.04 E-value: 5.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 566 VDHETALSISQAVHMSKKtGSTEVSSQAS-KSARDFFNINAEIIRKRGPL-LVGVFMNQPLEEVLEKQHLYDLDIVQLHG 643
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKA-GADYLGLIFSeSSKRQVSPEQAQELRSPVPLlLVGVFVNQPIDDVLRIAQVLGLDVVQLHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 644 DEPLEWANLIP--VPVVRKFKPGQ----VGLATRGYHAV-PLLDSGA-GSGTLLDLESVKKELEKdeQVTVLLAGGLEPS 715
Cdd:pfam00697 80 DEDQEYENLLPtgVPVIKAIWVPDsvdtVDIARRADHVDlPLLDSGAgGTGELFDWSLVSKWLKS--GLKVILAGGLNPD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 758991969 716 NVVETVKSLGPlservIGVDVSSGVEEGGKQSLEKIREFVK 756
Cdd:pfam00697 158 NVVEAIKTPGV-----IGVDVSSGVETNGIKDLNKIRKFVQ 193
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
26-224 |
3.76e-58 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 196.81 E-value: 3.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDEL--IAKNPTQLVISPGPGHPgTDSGISRDAIRHFAG-KIPIFG 102
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEaaVAAQFDGVLLSPGPGTP-ERAGASIDMVRACAAaGTPLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 103 VCMGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAkedgsKGVI 182
Cdd:PRK07765 82 VCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPETLPAELEVTARTD-----SGVI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 758991969 183 MGVRHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQGGTWAE 224
Cdd:PRK07765 157 MAVRHRELPIHGVQFHPESVLTEGGHRMLANWLTVCGWAPDE 198
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
24-280 |
1.61e-47 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 176.76 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 24 SNLILIDNYDSFTWNVYQYLVLEGAKVTVFRND---QITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPI 100
Cdd:PRK09522 2 ADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVP-SEAGCMPELLTRLRGKLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 101 FGVCMGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVtlPECLEVTSWIakedgsKG 180
Cdd:PRK09522 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNI--PAGLTINAHF------NG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 181 VIMGVRHKEYTIEGVQFHPESILSAEGRGMFRNFLhmqggTWAenerLQKAAQAQAANTksdaptpkksnILQKIYAHRK 260
Cdd:PRK09522 153 MVMAVRHDADRVCGFQFHPESILTTQGARLLEQTL-----AWA----QQKLEPTNTLQP-----------ILEKLYQAQT 212
|
250 260
....*....|....*....|....*.
gi 758991969 261 AAVDAQKQIPS------LRPSDLQAA 280
Cdd:PRK09522 213 LSQQESHQLFSavvrgeLKPEQLAAA 238
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
303-514 |
1.57e-45 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 174.06 E-value: 1.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 303 VALCAEIKRASPSKGVFAlDIDAPSQ-ARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDE 381
Cdd:PRK13802 50 IPVIAEIKRASPSKGHLS-DIPDPAAlAREYEQGGASAISVLTEGRRFLGSLDDFDKVRAAVH-IP----VLRKDFIVTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 382 YQILEARLAGADTVLLIVKMLEYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGR 461
Cdd:PRK13802 124 YQIWEARAHGADLVLLIVAALDDAQLKHLLDLAHELGMTVLVETHTREEIERAIAAGAKVIGINARNLKDLKVDVNKYNE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 758991969 462 LRSMVPSDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:PRK13802 204 LAADLPDDVIKVAESGVFGAVEVEDYARAGADAVLVGEGVATADDHELAVERL 256
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
532-758 |
7.98e-43 |
|
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: 154.27 E-value: 7.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 532 VKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaeiirkr 611
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKR--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 612 gpllVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPLEWANLIP----VPVVRKFKPG-----QVGLATRGYHAVPLLDS- 681
Cdd:cd00405 54 ----VGVFVNEDLEEILEIAEELGLDVVQLHGDESPEYCAQLRarlgLPVIKAIRVKdeedlEKAAAYAGEVDAILLDSk 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 682 ----GAGSGTLLDLESVKKELEKdeqVTVLLAGGLEPSNVVETVKSLGPlservIGVDVSSGVE-EGGKQSLEKIREFVK 756
Cdd:cd00405 130 sgggGGGTGKTFDWSLLRGLASR---KPVILAGGLTPDNVAEAIRLVRP-----YGVDVSSGVEtSPGIKDPEKIRAFIE 201
|
..
gi 758991969 757 AA 758
Cdd:cd00405 202 AA 203
|
|
| PLN02460 |
PLN02460 |
indole-3-glycerol-phosphate synthase |
241-514 |
2.84e-42 |
|
indole-3-glycerol-phosphate synthase
Pssm-ID: 215254 Cd Length: 338 Bit Score: 156.86 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 241 SDAPTPKksNILQKIYAHRKAAVDAQKQIPSLrpSDLQAAynLSIAPPQISLVDRLRNS------PfdvALCAEIKRASP 314
Cdd:PLN02460 60 NEGNTPR--NILEEIVWYKDVEVAQMKERKPL--YLLKKA--LQNAPPARDFVGALRAAhkrtgqP---GLIAEVKKASP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 315 SKGVFALDIDAPSQARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNGMPnrpaVLRKEFIFDEYQILEARLAGADT 394
Cdd:PLN02460 131 SRGVLRENFDPVEIAQAYEKGGAACLSVLTDEKYFQGSFENLEAIRNAGVKCP----LLCKEFIVDAWQIYYARSKGADA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 395 VLLIVKMLEYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKL-GAKVIGVNNRNLESFEVDLGTTGRL------RSMVP 467
Cdd:PLN02460 207 ILLIAAVLPDLDIKYMLKICKSLGMAALIEVHDEREMDRVLGIeGVELIGINNRSLETFEVDISNTKKLlegergEQIRE 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 758991969 468 SDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIREL 514
Cdd:PLN02460 287 KGIIVVGESGLFTPDDVAYVQNAGVKAVLVGESLVKQDDPGKGIAGL 333
|
|
| PRK13957 |
PRK13957 |
indole-3-glycerol-phosphate synthase; Provisional |
267-506 |
7.43e-39 |
|
indole-3-glycerol-phosphate synthase; Provisional
Pssm-ID: 140013 Cd Length: 247 Bit Score: 144.64 E-value: 7.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 267 KQIPSLRPSDLQAAYNLSIAPPQ-ISLVDRLRNSPFDValCAEIKRASPSKGVFALDIDAPSQARKYALAGASVISVLTE 345
Cdd:PRK13957 6 REIIETKQNEIEKISRWDPLPDRgLPLRDSLKSRSFSI--IAECKRKSPSAGELRADYHPVQIAKTYETLGASAISVLTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 346 PEWFKGSIDDLRAVRQVLNgMPnrpaVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLERLYKYSLSLGMEPLVEV 425
Cdd:PRK13957 84 QSYFGGSLEDLKSVSSELK-IP----VLRKDFILDEIQIREARAFGASAILLIVRILTPSQIKSFLKHASSLGMDVLVEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 426 QNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDvLDCKRDGVNGILVGEAIMRAP 505
Cdd:PRK13957 159 HTEDEAKLALDCGAEIIGINTRDLDTFQIHQNLVEEVAAFLPPNIVKVGESGIESRSD-LDKFRKLVDAALIGTYFMEKK 237
|
.
gi 758991969 506 D 506
Cdd:PRK13957 238 D 238
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
10-210 |
1.23e-37 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 150.45 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 10 SPHDSAPSPLVPTASNLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDqITIDELIAKNPTQLVISPGPGHPgTDSGISR- 88
Cdd:PRK13566 513 LSAEEPDAAAVGEGKRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYG-FAEEMLDRVNPDLVVLSPGPGRP-SDFDCKAt 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 89 -DAIRhfAGKIPIFGVCMGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGA-YAGLSQDLPVTRYHSLAGTHVTLPECL 166
Cdd:PRK13566 591 iDAAL--ARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGRlFSGLPEEFTVGRYHSLFADPETLPDEL 668
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 758991969 167 EVTSwiAKEDGskgVIMGVRHKEYTIEGVQFHPESILSAEGR-GM 210
Cdd:PRK13566 669 LVTA--ETEDG---VIMAIEHKTLPVAAVQFHPESIMTLGGDvGL 708
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
532-760 |
9.77e-35 |
|
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: 131.41 E-value: 9.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 532 VKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaeiirkr 611
Cdd:COG0135 4 VKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKK--------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 612 gpllVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPLEW----ANLIPVPVVRKFKPGQVG--LATRGYHAVP---LLDSG 682
Cdd:COG0135 57 ----VGVFVNADPEEILEIVEAVGLDAVQLHGDESPEYcaalRERLGLPVIKAIRVGDGAdlEEAAAYAPVAdalLLDAK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 683 A-----GSGTLLDLESVKKElekDEQVTVLLAGGLEPSNVVETVKSLGPLserviGVDVSSGVE-EGGKQSLEKIREFVK 756
Cdd:COG0135 133 VpglygGTGKTFDWSLLAGL---ALPKPVILAGGLTPENVAEAIRLVRPY-----GVDVSSGVEsAPGVKDPDKIRAFVE 204
|
....
gi 758991969 757 AAKS 760
Cdd:COG0135 205 AVRA 208
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
24-207 |
3.27e-33 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 126.88 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 24 SNLILIDNYDSFTWNVYQYLVLEGAKVTVFRNdQITIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGV 103
Cdd:PRK05637 2 THVVLIDNHDSFVYNLVDAFAVAGYKCTVFRN-TVPVEEILAANPDLICLSPGPGHP-RDAGNMMALIDRTLGQIPLLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 104 CMGQQCIFDVYGGDVCFAGEIlHGKTSPLRHDGKGA----YAGLSQD------------LPVTRYHSLAGTHVtlPECLE 167
Cdd:PRK05637 80 CLGFQALLEHHGGKVEPCGPV-HGTTDNMILTDAGVqspvFAGLATDvepdhpeipgrkVPIARYHSLGCVVA--PDGME 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 758991969 168 VTSWIAKEDGSkgVIMGVRHKEYTIEGVQFHPESILSAEG 207
Cdd:PRK05637 157 SLGTCSSEIGP--VIMAAETTDGKAIGLQFHPESVLSPTG 194
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
27-222 |
8.98e-31 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 129.97 E-value: 8.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 27 ILIDNYDSFTWNVYQYL-VLEGAKVTVFRNDQITIDE----LIAKNP-TQLVISPGPGHP--GTDSGISRDAIRHfAGKI 98
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELsIVNGVPPVVVRNDEWTWEEvyhyLYEEKAfDNIVISPGPGSPtcPADIGICLRLLLE-CRDI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 99 PIFGVCMGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAY----AGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAK 174
Cdd:PLN02889 164 PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVIDAESLPKELVPIAWTSS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 175 ED------------------------------------------------GSKGVIMGVRHKEYTIEGVQFHPESILSAE 206
Cdd:PLN02889 244 SDtlsflesqksglvpdayesqigqsgssdpfssklkngtswpsshsermQNGKILMGIMHSTRPHYGLQFHPESIATCY 323
|
250
....*....|....*.
gi 758991969 207 GRGMFRNFLHMQGGTW 222
Cdd:PLN02889 324 GRQIFKNFREITQDYW 339
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
532-762 |
3.97e-28 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 112.59 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 532 VKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHETALSISQAVHMSKKTgstevssqasksardffninaeiirkr 611
Cdd:PRK01222 5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVKV--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 612 gpllVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPLE----WANLIPVPVVRKFKPGQVG--LATRGYHAVP---LLDSG 682
Cdd:PRK01222 58 ----VGVFVNASDEEIDEIVETVPLDLLQLHGDETPEfcrqLKRRYGLPVIKALRVRSAGdlEAAAAYYGDAdglLLDAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 683 A----GSGTLLDLESVKKELEKDeqvtVLLAGGLEPSNVVETVKSLGPLserviGVDVSSGVEEG-GKQSLEKIREFVKA 757
Cdd:PRK01222 134 VglpgGTGKTFDWSLLPAGLAKP----WILAGGLNPDNVAEAIRQVRPY-----GVDVSSGVESApGIKDPEKIRAFIEA 204
|
....*
gi 758991969 758 AKSVR 762
Cdd:PRK01222 205 VKSAD 209
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
25-217 |
9.77e-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: 116.54 E-value: 9.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 25 NLILIDNYDSFTWNVYQYL--VLE-GAKVTVFRNDQITiDELIAKNP--TQLVISPGPGHPGT--DSGISRDAIR-HFAG 96
Cdd:TIGR01823 7 HVLFIDSYDSFTYNVVRLLeqQTDiSVHVTTVHSDTFQ-DQLLELLPlfDAIVVGPGPGNPNNaqDMGIISELWElANLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 97 KIPIFGVCMGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLsQDLPVTRYHSLagtHVTLPECLEVTSWIAKED 176
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSL---YANPEGIDTLLPLCLTED 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 758991969 177 GSKGVIMGVRHKEYTIEGVQFHPESILSAEGRG-MFRNFLHM 217
Cdd:TIGR01823 162 EEGIILMSAQTKKKPWFGVQYHPESCCSELGSGkLVSNFLKL 203
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
23-215 |
3.96e-26 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 105.97 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 23 ASNLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDEliAKNPTQLVISPGPGHPGTDSGISRDAIRHFAGKiPIFG 102
Cdd:PRK06895 1 ATKLLIINNHDSFTFNLVDLIRKLGVPMQVVNVEDLDLDE--VENFSHILISPGPDVPRAYPQLFAMLERYHQHK-SILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 103 VCMGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGA-YAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEdgskgV 181
Cdd:PRK06895 78 VCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPlFDGLPEEFNIGLYHSWAVSEENFPTPLEITAVCDEN-----V 152
|
170 180 190
....*....|....*....|....*....|....
gi 758991969 182 IMGVRHKEYTIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:PRK06895 153 VMAMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| PLN02363 |
PLN02363 |
phosphoribosylanthranilate isomerase |
502-762 |
2.17e-24 |
|
phosphoribosylanthranilate isomerase
Pssm-ID: 215207 Cd Length: 256 Bit Score: 103.02 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 502 MRAPDATQFIRELC---------AGLTGPVPKSAAEPL---------LVKICGTRSAEAAAEAIKAGADLVGMIMVPGTK 563
Cdd:PLN02363 1 SKTSKSGLSNRKVSfsrvgyaqnRKLSCSVSSENVAPKddergkdrpLVKMCGITSARDAAMAVEAGADFIGMILWPKSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 564 RCVDHETALSISQAVhmskktgstevssqasksardffninaeiiRKRGPLLVGVFMNQPLEEVLEKQHLYDLDIVQLHG 643
Cdd:PLN02363 81 RSISLSVAKEISQVA------------------------------REGGAKPVGVFVDDDANTILRAADSSDLELVQLHG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 644 DEPLEWANLIP--VPVVRKFKPGQVGLATRGYHAVP-------LLDSG-AGSGTLLDLESVKKELEKDEQVTvLLAGGLE 713
Cdd:PLN02363 131 NGSRAAFSRLVreRKVIYVLNANEDGKLLNVVPEEDchladwiLVDSAtGGSGKGFNWQNFKLPSVRSRNGW-LLAGGLT 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 758991969 714 PSNVVETVKSLGPlservIGVDVSSGVE--EGGKQSLEKIREFVKAAKSVR 762
Cdd:PLN02363 210 PENVHEAVSLLKP-----TGVDVSSGICgpDGIRKDPSKISSFISAVKSVA 255
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
59-216 |
7.20e-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: 85.06 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 59 TIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGKIPIFGVCMGQQCIFDVYGGDVCFAGEILHGKTSpLRHDGKG 138
Cdd:TIGR00888 33 PLEEIREKNPKGIILSGGPSSV-YAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKREYGKAE-LEILDED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 139 A-YAGLSQDLPVTRYHslaGTHVT-LPECLEVtswIAKEDGSKGVIMgvRHKEYTIEGVQFHPESILSAEGRGMFRNFLH 216
Cdd:TIGR00888 111 DlFRGLPDESTVWMSH---GDKVKeLPEGFKV---LATSDNCPVAAM--AHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
58-215 |
1.59e-16 |
|
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: 77.96 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 58 ITIDELIAKNPTQLVISPGPgHPGTDSGISRDAIRHFAGKIPIFGVCMGQQCIFDVYGGDV--CFAGEilHGKTSPLRHD 135
Cdd:cd01742 32 TPLEEIKLKNPKGIILSGGP-SSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVerGDKRE--YGKAEIEIDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 136 GKGAYAGLSQDLPVTRYHslaGTHVT-LPECLEVtswIAKEDGSKgvIMGVRHKEYTIEGVQFHPESILSAEGRGMFRNF 214
Cdd:cd01742 109 SSPLFEGLPDEQTVWMSH---GDEVVkLPEGFKV---IASSDNCP--VAAIANEEKKIYGVQFHPEVTHTEKGKEILKNF 180
|
.
gi 758991969 215 L 215
Cdd:cd01742 181 L 181
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
37-215 |
2.90e-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: 71.37 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 37 WNVYQYLVLEGAKVTVFRNDQiTIDELIAKNPTQLVISPGPGHPgTDSGISRDAIRHFAGK-IPIFGVCMGQQCIFDVYG 115
Cdd:cd01744 10 HNILRELLKRGCEVTVVPYNT-DAEEILKLDPDGIFLSNGPGDP-ALLDEAIKTVRKLLGKkIPIFGICLGHQLLALALG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 116 gdvcfageilhGKTSPLRHdgkgAYAGLSQdlPVTRY-----------HSLAGTHVTLPECLEVTsWIAKEDGSkgvIMG 184
Cdd:cd01744 88 -----------AKTYKMKF----GHRGSNH--PVKDLitgrvyitsqnHGYAVDPDSLPGGLEVT-HVNLNDGT---VEG 146
|
170 180 190
....*....|....*....|....*....|....
gi 758991969 185 VRHKEYTIEGVQFHPESilSA---EGRGMFRNFL 215
Cdd:cd01744 147 IRHKDLPVFSVQFHPEA--SPgphDTEYLFDEFL 178
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
57-216 |
6.63e-14 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 75.08 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 57 QITIDELIAKNPTQLVISPGP------GHPGTDSGIsrdairhFAGKIPIFGVCMGQQCIFDVYGGDVCFAGEILHGKTS 130
Cdd:PRK00074 36 DISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEI-------FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 131 pLRHDGKGA-YAGLSQDLPVTRYHslaGTHVT-LPECLEVtswIAKEDGSKgvIMGVRHKEYTIEGVQFHPESILSAEGR 208
Cdd:PRK00074 109 -LEVDNDSPlFKGLPEEQDVWMSH---GDKVTeLPEGFKV---IASTENCP--IAAIANEERKFYGVQFHPEVTHTPQGK 179
|
....*...
gi 758991969 209 GMFRNFLH 216
Cdd:PRK00074 180 KLLENFVF 187
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
43-217 |
4.41e-13 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 71.26 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 43 LVLEGAKVTVFRNDqITIDELIAKNPTQLVISPGPGHP-GTDSGIsrDAIRHFAG-KIPIFGVCMGQQCIfdvyggdvcf 120
Cdd:PRK12564 195 LAERGCRVTVVPAT-TTAEEILALNPDGVFLSNGPGDPaALDYAI--EMIRELLEkKIPIFGICLGHQLL---------- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 121 aGEILHGKTSPLRH-------------DGKGAYAglSQDlpvtryHSLAGTHVTLPECLEVTsWIAKEDGSkgvIMGVRH 187
Cdd:PRK12564 262 -ALALGAKTYKMKFghrganhpvkdleTGKVEIT--SQN------HGFAVDEDSLPANLEVT-HVNLNDGT---VEGLRH 328
|
170 180 190
....*....|....*....|....*....|...
gi 758991969 188 KEYTIEGVQFHPESilSA---EGRGMFRNFLHM 217
Cdd:PRK12564 329 KDLPAFSVQYHPEA--SPgphDSAYLFDEFVEL 359
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
26-215 |
1.22e-12 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 66.80 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 26 LILIDNYDSFT---WNVYQYLvleGAKVTVFRNDqITIDElIAKNPTQLVISPGPGHpgTDSGISRDAIRHFagKIPIFG 102
Cdd:PRK00758 2 IVVVDNGGQYNhliHRTLRYL---GVDAKIIPNT-TPVEE-IKAFEDGLILSGGPDI--ERAGNCPEYLKEL--DVPILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 103 VCMGQQCIFDVYGGDVCFA--GEILHGKTSPLRHDGkgAYAGLSQDLPVTRYHslAGTHVTLPECLEVTswiAKEDGSKg 180
Cdd:PRK00758 73 ICLGHQLIAKAFGGEVGRGeyGEYALVEVEILDEDD--ILKGLPPEIRVWASH--ADEVKELPDGFEIL---ARSDICE- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 758991969 181 vIMGVRHKEYTIEGVQFHPESILSAEGRGMFRNFL 215
Cdd:PRK00758 145 -VEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFL 178
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
528-759 |
5.61e-10 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 62.52 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 528 EPLLVKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHET-ALSISQAVhmskktgstevssqasksardffninae 606
Cdd:PRK13803 1 KQPKIKICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVGNKFlAPNLEKAI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 607 iiRKRGPLLVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPL---EWANLIPVPVVRKFKPGQVGLAT--------RGYHA 675
Cdd:PRK13803 53 --RKAGGRPVGVFVNESAKAMLKFSKKNGIDFVQLHGAESKaepAYCQRIYKKSIKKIGSFLIDDAFgfevldeyRDHVK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 676 VPLLDSGA----GSGTLLDLESVKkelEKDEQVTVLLAGGLEPSNVvETVKSLGplSERVIGVDVSSGVE-EGGKQSLEK 750
Cdd:PRK13803 131 YFLFDNKTkiygGSGKSFDWEKFY---NYNFKFPFFLSGGLSPTNF-DRIINLT--HPQILGIDVSSGFEdSPGNKKLTL 204
|
....*....
gi 758991969 751 IREFVKAAK 759
Cdd:PRK13803 205 LKSFITNVK 213
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
38-201 |
5.99e-10 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 61.92 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 38 NVYQYLVLEGAKVTVFRNdQITIDELIAKNPTQLVISPGPGHPgtdSGI--SRDAIRHFAGKIPIFGVCMGQQCIFDVYG 115
Cdd:PLN02771 253 NILRRLASYGCKITVVPS-TWPASEALKMKPDGVLFSNGPGDP---SAVpyAVETVKELLGKVPVFGICMGHQLLGQALG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 116 GDVCFAGEILHGKTSPLRHDGKGAYAGLSQDlpvtryHSLAGTHVTLPECLEVTSwIAKEDGSkgvIMGVRHKEYTIEGV 195
Cdd:PLN02771 329 GKTFKMKFGHHGGNHPVRNNRTGRVEISAQN------HNYAVDPASLPEGVEVTH-VNLNDGS---CAGLAFPALNVMSL 398
|
....*.
gi 758991969 196 QFHPES 201
Cdd:PLN02771 399 QYHPEA 404
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
37-201 |
1.19e-09 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 60.97 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 37 WNVYQYLVLEGAKVTVFrNDQITIDELIAKNPTQLVISPGPGHPGT-DSGISR--DAIRHfagKIPIFGVCMGQQCIfdv 113
Cdd:CHL00197 204 YNILRRLKSFGCSITVV-PATSPYQDILSYQPDGILLSNGPGDPSAiHYGIKTvkKLLKY---NIPIFGICMGHQIL--- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 114 yggDVCFageilHGKTSPLR--HDGKGAYAGLSQDLPVT-RYHSLAgthVTLPECLEVTSWIAKEDGSKGVIMGVRHKEY 190
Cdd:CHL00197 277 ---SLAL-----EAKTFKLKfgHRGLNHPSGLNQQVEITsQNHGFA---VNLESLAKNKFYITHFNLNDGTVAGISHSPK 345
|
170
....*....|.
gi 758991969 191 TIEGVQFHPES 201
Cdd:CHL00197 346 PYFSVQYHPEA 356
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
43-201 |
1.73e-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: 60.42 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 43 LVLEGAKVTVFRNDqITIDELIAKNPTQLVISPGPGHPG-TDSGIsrDAIRHFAGK-IPIFGVCMGQQCIfdvyggdvcf 120
Cdd:COG0505 194 LAERGCRVTVVPAT-TSAEEILALNPDGVFLSNGPGDPAaLDYAI--ETIRELLGKgIPIFGICLGHQLL---------- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 121 aGEILHGKTSPLRH-------------DGKGAYAglSQDlpvtryHSLAGTHVTLPE-CLEVTsWIAKEDGSkgvIMGVR 186
Cdd:COG0505 261 -ALALGAKTYKLKFghrganhpvkdleTGRVEIT--SQN------HGFAVDEDSLPAtDLEVT-HVNLNDGT---VEGLR 327
|
170
....*....|....*
gi 758991969 187 HKEYTIEGVQFHPES 201
Cdd:COG0505 328 HKDLPAFSVQYHPEA 342
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
27-200 |
2.69e-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: 58.03 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 27 ILI----DNYDSFTWNVYQYLVLEGAKVTVFR--NDQITIDELIAKNPTQLVISPGPGHPGTDSGISRDA---IRH-FAG 96
Cdd:COG0518 2 ILIldhdPFGGQYPGLIARRLREAGIELDVLRvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEpalIREaFEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 97 KIPIFGVCMGQQCIFDVYGGDVCFAG--EIlhGKTsPLR-HDGKGAYAGLSQDLPVtrYHSlagtH----VTLPECLEVt 169
Cdd:COG0518 82 GKPVLGICYGAQLLAHALGGKVEPGPgrEI--GWA-PVElTEADPLFAGLPDEFTV--WMS----HgdtvTELPEGAEV- 151
|
170 180 190
....*....|....*....|....*....|.
gi 758991969 170 swIAKEDGSKgvIMGVRHKEYTIeGVQFHPE 200
Cdd:COG0518 152 --LASSDNCP--NQAFRYGRRVY-GVQFHPE 177
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
43-200 |
7.31e-09 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 58.36 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 43 LVLEGAKVTVFRNDQiTIDELIAKNPTQLVISPGPGHPGTDSGISrDAIRHFAGKIPIFGVCMGQQCIFDVYGGDVcfag 122
Cdd:PRK12838 185 LSKRGCKVTVLPYDT-SLEEIKNLNPDGIVLSNGPGDPKELQPYL-PEIKKLISSYPILGICLGHQLIALALGADT---- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 123 EIL----HGKTSPLRHDGKGAYAGLSQDlpvtryHSlagtHVTLPECLEVTSWIAK-EDGSKGVIMGVRHKEYTIEGVQF 197
Cdd:PRK12838 259 EKLpfghRGANHPVIDLTTGRVWMTSQN------HG----YVVDEDSLDGTPLSVRfFNVNDGSIEGLRHKKKPVLSVQF 328
|
...
gi 758991969 198 HPE 200
Cdd:PRK12838 329 HPE 331
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
60-215 |
9.19e-09 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 58.54 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 60 IDELIAKNPTQLVISPGP------GHPGTDSGISrDAIRhfAGKIPIFGVCMGQQCIFDVYGGDVCFAGEILHGKTSPLR 133
Cdd:PLN02347 46 LDRIASLNPRVVILSGGPhsvhveGAPTVPEGFF-DYCR--ERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 134 HDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVtswIAKEDgsKGVIMGVRHKEYTIEGVQFHPESILSAEGRGMFRN 213
Cdd:PLN02347 123 VCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEV---VAKSV--QGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRH 197
|
..
gi 758991969 214 FL 215
Cdd:PLN02347 198 FL 199
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
88-214 |
1.18e-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: 52.58 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 88 RDA-----IRHF-AGKIPIFGVCMGQQCIFDVYGGDvcfageilhgktsplrhdgkgayagLSQDLPVTRYHSLAgthV- 160
Cdd:cd01745 85 RDAfelalLRAAlERGKPILGICRGMQLLNVALGGT-------------------------LYQDIRVNSLHHQA---Ik 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 758991969 161 TLPECLEVTSWiaKEDgskGVIMGVRHKEYT-IEGVQFHPESIL--SAEGRGMFRNF 214
Cdd:cd01745 137 RLADGLRVEAR--APD---GVIEAIESPDRPfVLGVQWHPEWLAdtDPDSLKLFEAF 188
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
27-111 |
1.33e-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: 50.67 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 27 ILIDNYDSFTW---NVYQYLVLEGAKVTVFRNDQITIDELI-AKNPTQLVISPGPGHPGTDSGISR--DAIRHFAG-KIP 99
Cdd:cd01653 2 AVLLFPGFEELelaSPLDALREAGAEVDVVSPDGGPVESDVdLDDYDGLILPGGPGTPDDLARDEAllALLREAAAaGKP 81
|
90
....*....|..
gi 758991969 100 IFGVCMGQQCIF 111
Cdd:cd01653 82 ILGICLGAQLLV 93
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
27-110 |
5.44e-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: 48.35 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 27 ILIDNYDSFTW---NVYQYLVLEGAKVTVFRNDQITIDELI-AKNPTQLVISPGPGHPGTDSGISR--DAIRHFAG-KIP 99
Cdd:cd03128 2 AVLLFGGSEELelaSPLDALREAGAEVDVVSPDGGPVESDVdLDDYDGLILPGGPGTPDDLAWDEAllALLREAAAaGKP 81
|
90
....*....|.
gi 758991969 100 IFGVCMGQQCI 110
Cdd:cd03128 82 VLGICLGAQLL 92
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
75-214 |
5.51e-05 |
|
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: 45.16 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 75 PGPGHPGTDSGisRDA-----IRHF-AGKIPIFGVCMGQQcIFDVY-GGDvcfageiLH-----GKTSPLRHDGKGAYAG 142
Cdd:COG2071 70 PHPELGPIDPE--RDAfelalIRAAlERGKPVLGICRGMQ-LLNVAlGGT-------LYqdlpdQVPGALDHRQPAPRYA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 143 LSQDL---PVTRYHSLAGTHV------------TLPECLEVTSWiAkEDgskGVIMGVRHKEYT-IEGVQFHPE--SILS 204
Cdd:COG2071 140 PRHTVeiePGSRLARILGEEEirvnslhhqavkRLGPGLRVSAR-A-PD---GVIEAIESPGAPfVLGVQWHPEwlAASD 214
|
170
....*....|
gi 758991969 205 AEGRGMFRNF 214
Cdd:COG2071 215 PLSRRLFEAF 224
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
97-200 |
2.95e-03 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 39.93 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758991969 97 KIPIFGVCMGQQCIFDVYGG----DVCFAGEILHGktsplRHDGKGAYAGLSQDLPV---TRYHSLAG---THVT----- 161
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGtlyqDIQEQPGFTDH-----REHCQVAPYAPSHAVNVepgSLLASLLGseeFRVNslhhq 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 758991969 162 ----LPECLEVTSWiakedGSKGVIMGVRHKEYT--IEGVQFHPE 200
Cdd:pfam07722 180 aidrLAPGLRVEAV-----APDGTIEAIESPNAKgfALGVQWHPE 219
|
|
| |
