|
Name |
Accession |
Description |
Interval |
E-value |
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
1-250 |
4.41e-123 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 350.61 E-value: 4.41e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 1 MGTILDKIVNQKKKEVAALYETYTPVKEKRK------TRSLVKAL--EQFTVIAEVKRASPSKGDINLHVDVRKQVKTYE 72
Cdd:PRK00278 1 MMDILDKIVAYKREEVAARKAQVPLAELKARaaaappPRDFAAALraGKPAVIAEVKKASPSKGVIREDFDPVEIAKAYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 73 ECGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKG 152
Cdd:PRK00278 81 AGGAACLSVLTDERFFQGSLEYLRAARAAVSLPVLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQLKELLDYAHSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 153 LEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLV 232
Cdd:PRK00278 161 LDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLV-VSESGIFTPEDLKRLAKAGADAVLV 239
|
250
....*....|....*...
gi 226707950 233 GEALMTSSSIHTFFEDCK 250
Cdd:PRK00278 240 GESLMRADDPGAALRELL 257
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
3-242 |
1.42e-117 |
|
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: 336.23 E-value: 1.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 3 TILDKIVNQKKKEVAALYETYTP------VKEKRKTRSLVKALE---QFTVIAEVKRASPSKGDINLHVDVRKQVKTYEE 73
Cdd:COG0134 2 TILDKIVAHKREEVAARKARVPLaelearAAAAPPPRDFAAALRaagGPAVIAEIKKASPSKGLIREDFDPAEIARAYEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 74 CGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGL 153
Cdd:COG0134 82 GGAAAISVLTDEKFFQGSLEDLRAVRAAVDLPVLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLKELLALAHSLGM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 154 EAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLVG 233
Cdd:COG0134 162 DVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLV-VSESGIRTPEDVARLAAAGADAFLVG 240
|
....*....
gi 226707950 234 EALMTSSSI 242
Cdd:COG0134 241 EALMRAPDP 249
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
36-248 |
2.18e-109 |
|
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: 314.02 E-value: 2.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 36 VKALEQFTVIAEVKRASPSKGDINLHVDVRKQVKTYEECGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDK 115
Cdd:cd00331 5 LKRPGGLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAVSLPVLRKDFIIDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 116 IQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGLEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEK 195
Cdd:cd00331 85 YQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKTFEVDLNTTER 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226707950 196 LGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLVGEALMTSSSIHTFFED 248
Cdd:cd00331 165 LAPLIPKDVIL-VSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALRE 216
|
|
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
5-248 |
4.89e-92 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 271.48 E-value: 4.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 5 LDKIVNQKKKEVAAL-----YETYTPVKEKRKTRSLVKALEQFT----VIAEVKRASPSKGDINLHVDVRKQVKTYEECG 75
Cdd:pfam00218 1 LEKIVADKRAEVAARkarppLADLQAAARAPPTRSFYDALRESRgrpaLIAEVKKASPSKGLIREDFDPAEIARVYEAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 76 AGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGLEA 155
Cdd:pfam00218 81 ASAISVLTDPKYFQGSIEYLRAVRQAVSLPVLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELYAYARSLGMEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 156 IVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLVGEA 235
Cdd:pfam00218 161 LVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLL-VAESGIYTPADVRELKEHGANAFLVGES 239
|
250
....*....|...
gi 226707950 236 LMTSSSIHTFFED 248
Cdd:pfam00218 240 LMRQEDVRAAIRE 252
|
|
| Indglycph_syn_Halo_TrpC |
NF041303 |
indole-3-glycerol phosphate synthase; |
33-237 |
8.16e-43 |
|
indole-3-glycerol phosphate synthase;
Pssm-ID: 469200 Cd Length: 250 Bit Score: 145.89 E-value: 8.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 33 RSLVKALE------QFTVIAEVKRASPSKgDINLHVDVRKQVKTYEECGAGAVSVLTDGQFFKGSFYDLQTAREESSIPL 106
Cdd:NF041303 32 RSLPDAFAaaeadgRVPVIAEVKPTSPTT-DGTRDDDPVELAEAMVAGGAAALSVLTEPEHFGGSPETLRRVREAVDVPV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 107 LCKDFIIDKIQIDrAYEAgaDIILLIvAALTKEKLKELYSYVLEKGLEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTF 186
Cdd:NF041303 111 LRKDFLLREAQLD-AVEA--DVVLLI-ARFVGDDLEGLVAAARERGFQPLVEVHTRAELERALDAGADIIGVNNRDLAKL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 226707950 187 EVDLSQTEKLGKRLNEEKLLWISESGIHSKEDIIRVKRAGAKGVLVGEALM 237
Cdd:NF041303 187 EVDLGTFESVAPHVPDDDVTLIAESGISTPADVRRMREAGADALLVGSAIM 237
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
188-236 |
4.08e-03 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 37.56 E-value: 4.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226707950 188 VDLSQTEKLGKRLNEEKllwISESGIHSKEDIIRVKRAGAKGVLVGEAL 236
Cdd:TIGR00007 176 PNFELTKELVKAVNVPV---IASGGVSSIDDLIALKKLGVYGVIVGKAL 221
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
1-250 |
4.41e-123 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 350.61 E-value: 4.41e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 1 MGTILDKIVNQKKKEVAALYETYTPVKEKRK------TRSLVKAL--EQFTVIAEVKRASPSKGDINLHVDVRKQVKTYE 72
Cdd:PRK00278 1 MMDILDKIVAYKREEVAARKAQVPLAELKARaaaappPRDFAAALraGKPAVIAEVKKASPSKGVIREDFDPVEIAKAYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 73 ECGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKG 152
Cdd:PRK00278 81 AGGAACLSVLTDERFFQGSLEYLRAARAAVSLPVLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQLKELLDYAHSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 153 LEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLV 232
Cdd:PRK00278 161 LDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLV-VSESGIFTPEDLKRLAKAGADAVLV 239
|
250
....*....|....*...
gi 226707950 233 GEALMTSSSIHTFFEDCK 250
Cdd:PRK00278 240 GESLMRADDPGAALRELL 257
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
3-242 |
1.42e-117 |
|
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: 336.23 E-value: 1.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 3 TILDKIVNQKKKEVAALYETYTP------VKEKRKTRSLVKALE---QFTVIAEVKRASPSKGDINLHVDVRKQVKTYEE 73
Cdd:COG0134 2 TILDKIVAHKREEVAARKARVPLaelearAAAAPPPRDFAAALRaagGPAVIAEIKKASPSKGLIREDFDPAEIARAYEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 74 CGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGL 153
Cdd:COG0134 82 GGAAAISVLTDEKFFQGSLEDLRAVRAAVDLPVLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLKELLALAHSLGM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 154 EAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLVG 233
Cdd:COG0134 162 DVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLV-VSESGIRTPEDVARLAAAGADAFLVG 240
|
....*....
gi 226707950 234 EALMTSSSI 242
Cdd:COG0134 241 EALMRAPDP 249
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
36-248 |
2.18e-109 |
|
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: 314.02 E-value: 2.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 36 VKALEQFTVIAEVKRASPSKGDINLHVDVRKQVKTYEECGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDK 115
Cdd:cd00331 5 LKRPGGLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAGAAAISVLTEPKYFQGSLEDLRAVREAVSLPVLRKDFIIDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 116 IQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGLEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEK 195
Cdd:cd00331 85 YQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKTFEVDLNTTER 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226707950 196 LGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLVGEALMTSSSIHTFFED 248
Cdd:cd00331 165 LAPLIPKDVIL-VSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALRE 216
|
|
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
5-248 |
4.89e-92 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 271.48 E-value: 4.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 5 LDKIVNQKKKEVAAL-----YETYTPVKEKRKTRSLVKALEQFT----VIAEVKRASPSKGDINLHVDVRKQVKTYEECG 75
Cdd:pfam00218 1 LEKIVADKRAEVAARkarppLADLQAAARAPPTRSFYDALRESRgrpaLIAEVKKASPSKGLIREDFDPAEIARVYEAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 76 AGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGLEA 155
Cdd:pfam00218 81 ASAISVLTDPKYFQGSIEYLRAVRQAVSLPVLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELYAYARSLGMEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 156 IVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLwISESGIHSKEDIIRVKRAGAKGVLVGEA 235
Cdd:pfam00218 161 LVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLL-VAESGIYTPADVRELKEHGANAFLVGES 239
|
250
....*....|...
gi 226707950 236 LMTSSSIHTFFED 248
Cdd:pfam00218 240 LMRQEDVRAAIRE 252
|
|
| PRK09427 |
PRK09427 |
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
1-237 |
5.78e-64 |
|
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;
Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 206.20 E-value: 5.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 1 MGTILDKIVNQKKKEVAALyETYTP---VKEK--RKTRSLVKALEQFTV--IAEVKRASPSKGDINLHVDVRKQVKTYEE 73
Cdd:PRK09427 3 MPTVLAKIVADKAIWVAAR-KQQQPlasFQNEiqPSDRSFYDALKGPKTafILECKKASPSKGLIRDDFDPAEIARVYKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 74 cGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGL 153
Cdd:PRK09427 82 -YASAISVLTDEKYFQGSFDFLPIVRAIVTQPILCKDFIIDPYQIYLARYYGADAILLMLSVLDDEQYRQLAAVAHSLNM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 154 EAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLwISESGIHSKEDIIRVKRaGAKGVLVG 233
Cdd:PRK09427 161 GVLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPADVIV-ISESGIYTHAQVRELSP-FANGFLIG 238
|
....
gi 226707950 234 EALM 237
Cdd:PRK09427 239 SSLM 242
|
|
| PLN02460 |
PLN02460 |
indole-3-glycerol-phosphate synthase |
4-240 |
7.41e-59 |
|
indole-3-glycerol-phosphate synthase
Pssm-ID: 215254 Cd Length: 338 Bit Score: 189.60 E-value: 7.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 4 ILDKIVNQKKKEVAALYETyTPVKEKRK-------TRSLVKALE-------QFTVIAEVKRASPSKGDINLHVDVRKQVK 69
Cdd:PLN02460 68 ILEEIVWYKDVEVAQMKER-KPLYLLKKalqnappARDFVGALRaahkrtgQPGLIAEVKKASPSRGVLRENFDPVEIAQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 70 TYEECGAGAVSVLTDGQFFKGSFYDLQTAREES-SIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYV 148
Cdd:PLN02460 147 AYEKGGAACLSVLTDEKYFQGSFENLEAIRNAGvKCPLLCKEFIVDAWQIYYARSKGADAILLIAAVLPDLDIKYMLKIC 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 149 LEKGLEAIVEVHDEQELEIAIQLNP-HVIGINNRNLKTFEVDLSQTEKL-----GKRLNEEKLLWISESGIHSKEDIIRV 222
Cdd:PLN02460 227 KSLGMAALIEVHDEREMDRVLGIEGvELIGINNRSLETFEVDISNTKKLlegerGEQIREKGIIVVGESGLFTPDDVAYV 306
|
250
....*....|....*...
gi 226707950 223 KRAGAKGVLVGEALMTSS 240
Cdd:PLN02460 307 QNAGVKAVLVGESLVKQD 324
|
|
| PRK13957 |
PRK13957 |
indole-3-glycerol-phosphate synthase; Provisional |
1-247 |
2.35e-49 |
|
indole-3-glycerol-phosphate synthase; Provisional
Pssm-ID: 140013 Cd Length: 247 Bit Score: 162.74 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 1 MGTILDKIVNQKKKEVAALYETYT------PVKEKRKTRSlvkaleqFTVIAEVKRASPSKGDINLHVDVRKQVKTYEEC 74
Cdd:PRK13957 1 MHRVLREIIETKQNEIEKISRWDPlpdrglPLRDSLKSRS-------FSIIAECKRKSPSAGELRADYHPVQIAKTYETL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 75 GAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGLE 154
Cdd:PRK13957 74 GASAISVLTDQSYFGGSLEDLKSVSSELKIPVLRKDFILDEIQIREARAFGASAILLIVRILTPSQIKSFLKHASSLGMD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 155 AIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLnEEKLLWISESGIHSKEDIIRVkRAGAKGVLVGE 234
Cdd:PRK13957 154 VLVEVHTEDEAKLALDCGAEIIGINTRDLDTFQIHQNLVEEVAAFL-PPNIVKVGESGIESRSDLDKF-RKLVDAALIGT 231
|
250
....*....|....
gi 226707950 235 ALMTSSSI-HTFFE 247
Cdd:PRK13957 232 YFMEKKDIrKAWLS 245
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
3-241 |
9.24e-47 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 165.20 E-value: 9.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 3 TILDKIV-----NQKKKEV--------AALYETYTPVKEKRktrsLVKALEQFTVIAEVKRASPSKGDINLHVDVRKQVK 69
Cdd:PRK13802 2 SVLDELVagaleDQRTRELtvsleevkKAAAAAPAPIDATR----WLKRADGIPVIAEIKRASPSKGHLSDIPDPAALAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 70 TYEECGAGAVSVLTDGQFFKGSFYDLQTAREESSIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVL 149
Cdd:PRK13802 78 EYEQGGASAISVLTEGRRFLGSLDDFDKVRAAVHIPVLRKDFIVTDYQIWEARAHGADLVLLIVAALDDAQLKHLLDLAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 150 EKGLEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEkLLWISESGIHSKEDIIRVKRAGAKG 229
Cdd:PRK13802 158 ELGMTVLVETHTREEIERAIAAGAKVIGINARNLKDLKVDVNKYNELAADLPDD-VIKVAESGVFGAVEVEDYARAGADA 236
|
250
....*....|..
gi 226707950 230 VLVGEALMTSSS 241
Cdd:PRK13802 237 VLVGEGVATADD 248
|
|
| Indglycph_syn_Halo_TrpC |
NF041303 |
indole-3-glycerol phosphate synthase; |
33-237 |
8.16e-43 |
|
indole-3-glycerol phosphate synthase;
Pssm-ID: 469200 Cd Length: 250 Bit Score: 145.89 E-value: 8.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 33 RSLVKALE------QFTVIAEVKRASPSKgDINLHVDVRKQVKTYEECGAGAVSVLTDGQFFKGSFYDLQTAREESSIPL 106
Cdd:NF041303 32 RSLPDAFAaaeadgRVPVIAEVKPTSPTT-DGTRDDDPVELAEAMVAGGAAALSVLTEPEHFGGSPETLRRVREAVDVPV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 107 LCKDFIIDKIQIDrAYEAgaDIILLIvAALTKEKLKELYSYVLEKGLEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTF 186
Cdd:NF041303 111 LRKDFLLREAQLD-AVEA--DVVLLI-ARFVGDDLEGLVAAARERGFQPLVEVHTRAELERALDAGADIIGVNNRDLAKL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 226707950 187 EVDLSQTEKLGKRLNEEKLLWISESGIHSKEDIIRVKRAGAKGVLVGEALM 237
Cdd:NF041303 187 EVDLGTFESVAPHVPDDDVTLIAESGISTPADVRRMREAGADALLVGSAIM 237
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
63-233 |
5.36e-08 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 51.82 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 63 DVRKQVKTYEECGAGAVSVLTDGQFFKGSFYDLQT----AREESSIPLLCKDFIID-----KIQIDRAYEAGADIILLIV 133
Cdd:cd04722 13 DPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEvlkeVAAETDLPLGVQLAINDaaaavDIAAAAARAAGADGVEIHG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226707950 134 AA-----LTKEKLKELYSYVLEKGLEAIVEVHDEQELEIAIQLNPHVIGINNRNLKTF--EVDLSQTEKLGKRLNEEKLL 206
Cdd:cd04722 93 AVgylarEDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGgrDAVPIADLLLILAKRGSKVP 172
|
170 180
....*....|....*....|....*..
gi 226707950 207 WISESGIHSKEDIIRVKRAGAKGVLVG 233
Cdd:cd04722 173 VIAGGGINDPEDAAEALALGADGVIVG 199
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
188-236 |
2.78e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 37.84 E-value: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226707950 188 VDLSQTEKLGKRLNEEkllWISESGIHSKEDIIRVKRAGAKGVLVGEAL 236
Cdd:pfam00977 177 PDLELTRELAEAVNIP---VIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
188-236 |
4.08e-03 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 37.56 E-value: 4.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226707950 188 VDLSQTEKLGKRLNEEKllwISESGIHSKEDIIRVKRAGAKGVLVGEAL 236
Cdd:TIGR00007 176 PNFELTKELVKAVNVPV---IASGGVSSIDDLIALKKLGVYGVIVGKAL 221
|
|
|