|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09427 |
PRK09427 |
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
1-453 |
0e+00 |
|
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;
Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 935.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 1 MMQTVLAKIVADKAIWVETRKEQQPLASFQNEVQPSTRHFYDALQGARTSFILECKKASPSKGVIRDDFDPARIAAIYKH 80
Cdd:PRK09427 2 MMPTVLAKIVADKAIWVAARKQQQPLASFQNEIQPSDRSFYDALKGPKTAFILECKKASPSKGLIRDDFDPAEIARVYKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 81 YASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLEMG 160
Cdd:PRK09427 82 YASAISVLTDEKYFQGSFDFLPIVRAIVTQPILCKDFIIDPYQIYLARYYGADAILLMLSVLDDEQYRQLAAVAHSLNMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 161 VLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSAL 240
Cdd:PRK09427 162 VLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPADVIVISESGIYTHAQVRELSPFANGFLIGSSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 241 MAHDDLNAAVRRVLLGENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAPLQYVGVFRNHDIADV 320
Cdd:PRK09427 242 MAEDDLELAVRKLILGENKVCGLTRPQDAKAAYDAGAVYGGLIFVEKSPRYVSLEQAQEIIAAAPLRYVGVFRNADIEDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 321 VDKAKVLSLAAVQLHGNEDQQYIDTLRGALPANIAIWKALSVGETLPARELQHVDKYVLDNGQGGSGQRFDWSLLNGQSL 400
Cdd:PRK09427 322 VDIAKQLSLAAVQLHGDEDQAYIDALREALPKTCQIWKAISVGDTLPARDLQHVDRYLLDNGQGGTGQTFDWSLLPGQSL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446906631 401 GNVLLAGGLGADNCVEAAQTGCAGLDFNSAVESQPGIKDARLLASVFQTLRAY 453
Cdd:PRK09427 402 DNVLLAGGLNPDNCQQAAQLGCAGLDFNSGVESAPGIKDAQKLASVFQTLRAY 454
|
|
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
6-252 |
5.36e-136 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 390.89 E-value: 5.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 6 LAKIVADKAIWVETRKEQQPLASFQNEV-QPSTRHFYDALQGA--RTSFILECKKASPSKGVIRDDFDPARIAAIYKHY- 81
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPLADLQAAArAPPTRSFYDALRESrgRPALIAEVKKASPSKGLIREDFDPAEIARVYEAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 82 ASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLEMGV 161
Cdd:pfam00218 81 ASAISVLTDPKYFQGSIEYLRAVRQAVSLPVLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELYAYARSLGMEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 162 LTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELS-HFANGFLIGSAL 240
Cdd:pfam00218 161 LVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKeHGANAFLVGESL 240
|
250
....*....|..
gi 446906631 241 MAHDDLNAAVRR 252
Cdd:pfam00218 241 MRQEDVRAAIRE 252
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
3-254 |
8.38e-133 |
|
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: 383.22 E-value: 8.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 3 QTVLAKIVADKAIWVETRKEQQPLASFQNEV--QPSTRHFYDALQGA-RTSFILECKKASPSKGVIRDDFDPARIAAIYK 79
Cdd:COG0134 1 PTILDKIVAHKREEVAARKARVPLAELEARAaaAPPPRDFAAALRAAgGPAVIAEIKKASPSKGLIREDFDPAEIARAYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 80 HY-ASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLE 158
Cdd:COG0134 81 AGgAAAISVLTDEKFFQGSLEDLRAVRAAVDLPVLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLKELLALAHSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 159 MGVLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVREL-SHFANGFLIG 237
Cdd:COG0134 161 MDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLaAAGADAFLVG 240
|
250
....*....|....*..
gi 446906631 238 SALMAHDDLNAAVRRVL 254
Cdd:COG0134 241 EALMRAPDPGAALRELL 257
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
40-253 |
3.45e-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: 319.02 E-value: 3.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 40 FYDALQGA-RTSFILECKKASPSKGVIRDDFDPARIAAIYKHY-ASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDF 117
Cdd:cd00331 1 FKAALKRPgGLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAgAAAISVLTEPKYFQGSLEDLRAVREAVSLPVLRKDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 118 IIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLEMGVLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLN 197
Cdd:cd00331 81 IIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKTFEVDLN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446906631 198 RTRELAPKLGHNVTVISESGINTYAQVREL-SHFANGFLIGSALMAHDDLNAAVRRV 253
Cdd:cd00331 161 TTERLAPLIPKDVILVSESGISTPEDVKRLaEAGADAVLIGESLMRAPDPGAALREL 217
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09427 |
PRK09427 |
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
1-453 |
0e+00 |
|
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;
Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 935.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 1 MMQTVLAKIVADKAIWVETRKEQQPLASFQNEVQPSTRHFYDALQGARTSFILECKKASPSKGVIRDDFDPARIAAIYKH 80
Cdd:PRK09427 2 MMPTVLAKIVADKAIWVAARKQQQPLASFQNEIQPSDRSFYDALKGPKTAFILECKKASPSKGLIRDDFDPAEIARVYKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 81 YASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLEMG 160
Cdd:PRK09427 82 YASAISVLTDEKYFQGSFDFLPIVRAIVTQPILCKDFIIDPYQIYLARYYGADAILLMLSVLDDEQYRQLAAVAHSLNMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 161 VLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSAL 240
Cdd:PRK09427 162 VLTEVSNEEELERAIALGAKVIGINNRNLRDLSIDLNRTRELAPLIPADVIVISESGIYTHAQVRELSPFANGFLIGSSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 241 MAHDDLNAAVRRVLLGENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAPLQYVGVFRNHDIADV 320
Cdd:PRK09427 242 MAEDDLELAVRKLILGENKVCGLTRPQDAKAAYDAGAVYGGLIFVEKSPRYVSLEQAQEIIAAAPLRYVGVFRNADIEDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 321 VDKAKVLSLAAVQLHGNEDQQYIDTLRGALPANIAIWKALSVGETLPARELQHVDKYVLDNGQGGSGQRFDWSLLNGQSL 400
Cdd:PRK09427 322 VDIAKQLSLAAVQLHGDEDQAYIDALREALPKTCQIWKAISVGDTLPARDLQHVDRYLLDNGQGGTGQTFDWSLLPGQSL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446906631 401 GNVLLAGGLGADNCVEAAQTGCAGLDFNSAVESQPGIKDARLLASVFQTLRAY 453
Cdd:PRK09427 402 DNVLLAGGLNPDNCQQAAQLGCAGLDFNSGVESAPGIKDAQKLASVFQTLRAY 454
|
|
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
6-252 |
5.36e-136 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 390.89 E-value: 5.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 6 LAKIVADKAIWVETRKEQQPLASFQNEV-QPSTRHFYDALQGA--RTSFILECKKASPSKGVIRDDFDPARIAAIYKHY- 81
Cdd:pfam00218 1 LEKIVADKRAEVAARKARPPLADLQAAArAPPTRSFYDALRESrgRPALIAEVKKASPSKGLIREDFDPAEIARVYEAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 82 ASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLEMGV 161
Cdd:pfam00218 81 ASAISVLTDPKYFQGSIEYLRAVRQAVSLPVLRKDFIIDEYQIDEARLAGADAILLIVAVLDDELLEELYAYARSLGMEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 162 LTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELS-HFANGFLIGSAL 240
Cdd:pfam00218 161 LVEVHNEEELERALALGAKIIGVNNRNLKTFEVDLNTTRRLAPLIPADVLLVAESGIYTPADVRELKeHGANAFLVGESL 240
|
250
....*....|..
gi 446906631 241 MAHDDLNAAVRR 252
Cdd:pfam00218 241 MRQEDVRAAIRE 252
|
|
| TrpC |
COG0134 |
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
3-254 |
8.38e-133 |
|
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: 383.22 E-value: 8.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 3 QTVLAKIVADKAIWVETRKEQQPLASFQNEV--QPSTRHFYDALQGA-RTSFILECKKASPSKGVIRDDFDPARIAAIYK 79
Cdd:COG0134 1 PTILDKIVAHKREEVAARKARVPLAELEARAaaAPPPRDFAAALRAAgGPAVIAEIKKASPSKGLIREDFDPAEIARAYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 80 HY-ASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLE 158
Cdd:COG0134 81 AGgAAAISVLTDEKFFQGSLEDLRAVRAAVDLPVLRKDFIIDPYQIYEARAAGADAILLIAAALDDEQLKELLALAHSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 159 MGVLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVREL-SHFANGFLIG 237
Cdd:COG0134 161 MDVLVEVHDEEELERALALGARLIGINNRNLKTFEVDLETTERLAPLIPADVLVVSESGIRTPEDVARLaAAGADAFLVG 240
|
250
....*....|....*..
gi 446906631 238 SALMAHDDLNAAVRRVL 254
Cdd:COG0134 241 EALMRAPDPGAALRELL 257
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
2-257 |
2.97e-110 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 325.96 E-value: 2.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 2 MQTVLAKIVADKAIWVETRKEQQPLASFQNEV--QPSTRHFYDALQGARTSFILECKKASPSKGVIRDDFDPARIAAIY- 78
Cdd:PRK00278 1 MMDILDKIVAYKREEVAARKAQVPLAELKARAaaAPPPRDFAAALRAGKPAVIAEVKKASPSKGVIREDFDPVEIAKAYe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 79 KHYASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLE 158
Cdd:PRK00278 81 AGGAACLSVLTDERFFQGSLEYLRAARAAVSLPVLRKDFIIDPYQIYEARAAGADAILLIVAALDDEQLKELLDYAHSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 159 MGVLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVREL-SHFANGFLIG 237
Cdd:PRK00278 161 LDVLVEVHDEEELERALKLGAPLIGINNRNLKTFEVDLETTERLAPLIPSDRLVVSESGIFTPEDLKRLaKAGADAVLVG 240
|
250 260
....*....|....*....|
gi 446906631 238 SALMAHDDLNAAVRRVLLGE 257
Cdd:PRK00278 241 ESLMRADDPGAALRELLGAK 260
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
40-253 |
3.45e-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: 319.02 E-value: 3.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 40 FYDALQGA-RTSFILECKKASPSKGVIRDDFDPARIAAIYKHY-ASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDF 117
Cdd:cd00331 1 FKAALKRPgGLGVIAEVKRASPSKGLIREDFDPVEIAKAYEKAgAAAISVLTEPKYFQGSLEDLRAVREAVSLPVLRKDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 118 IIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLEMGVLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLN 197
Cdd:cd00331 81 IIDPYQIYEARAAGADAVLLIVAALDDEQLKELYELARELGMEVLVEVHDEEELERALALGAKIIGINNRDLKTFEVDLN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446906631 198 RTRELAPKLGHNVTVISESGINTYAQVREL-SHFANGFLIGSALMAHDDLNAAVRRV 253
Cdd:cd00331 161 TTERLAPLIPKDVILVSESGISTPEDVKRLaEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| PRAI |
pfam00697 |
N-(5'phosphoribosyl)anthranilate (PRA) isomerase; |
258-448 |
2.31e-82 |
|
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
Pssm-ID: 395566 Cd Length: 193 Bit Score: 251.88 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 258 NKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAPLQYVGVFRNHDIADVVDKAKVLSLAAVQLHGN 337
Cdd:pfam00697 1 AKICGLTRLSDVKAAVKAGADYLGLIFSESSKRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQLHGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 338 EDQQYIDTLRGALPANIAIWKALSVGETLPARELQHVDKYVLDNGQGGSGQRFDWSLLNGQSL--GNVLLAGGLGADNCV 415
Cdd:pfam00697 81 EDQEYENLLPTGVPVIKAIWVPDSVDTVDIARRADHVDLPLLDSGAGGTGELFDWSLVSKWLKsgLKVILAGGLNPDNVV 160
|
170 180 190
....*....|....*....|....*....|....
gi 446906631 416 EAAQT-GCAGLDFNSAVESQpGIKDARLLASVFQ 448
Cdd:pfam00697 161 EAIKTpGVIGVDVSSGVETN-GIKDLNKIRKFVQ 193
|
|
| TrpF |
COG0135 |
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ... |
258-452 |
1.67e-73 |
|
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: 229.64 E-value: 1.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 258 NKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAP--LQYVGVFRNHDIADVVDKAKVLSLAAVQLH 335
Cdd:COG0135 4 VKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPpfVKKVGVFVNADPEEILEIVEAVGLDAVQLH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 336 GNEDQQYIDTLRgaLPANIAIWKALSVGETLPAREL----QHVDKYVLD----NGQGGSGQRFDWSLLNGQSLG-NVLLA 406
Cdd:COG0135 84 GDESPEYCAALR--ERLGLPVIKAIRVGDGADLEEAaayaPVADALLLDakvpGLYGGTGKTFDWSLLAGLALPkPVILA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446906631 407 GGLGADNCVEA-AQTGCAGLDFNSAVESQPGIKDARLLASVFQTLRA 452
Cdd:COG0135 162 GGLTPENVAEAiRLVRPYGVDVSSGVESAPGVKDPDKIRAFVEAVRA 208
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
258-448 |
6.66e-69 |
|
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: 217.83 E-value: 6.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 258 NKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAP--LQYVGVFRNHDIADVVDKAKVLSLAAVQLH 335
Cdd:cd00405 1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPpfVKRVGVFVNEDLEEILEIAEELGLDVVQLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 336 GNEDQQYIDTLRGALpaNIAIWKALSVGETLP----ARELQHVDKYVLDN----GQGGSGQRFDWSLLNGQSLG-NVLLA 406
Cdd:cd00405 81 GDESPEYCAQLRARL--GLPVIKAIRVKDEEDlekaAAYAGEVDAILLDSksggGGGGTGKTFDWSLLRGLASRkPVILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446906631 407 GGLGADNCVEA-AQTGCAGLDFNSAVESQPGIKDARLLASVFQ 448
Cdd:cd00405 159 GGLTPDNVAEAiRLVRPYGVDVSSGVETSPGIKDPEKIRAFIE 201
|
|
| PLN02460 |
PLN02460 |
indole-3-glycerol-phosphate synthase |
3-250 |
4.83e-63 |
|
indole-3-glycerol-phosphate synthase
Pssm-ID: 215254 Cd Length: 338 Bit Score: 207.32 E-value: 4.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 3 QTVLAKIVADKAIWVETRKEQQPLASFQNEVQ--PSTRHFYDALQGA--RTSF---ILECKKASPSKGVIRDDFDPARIA 75
Cdd:PLN02460 66 RNILEEIVWYKDVEVAQMKERKPLYLLKKALQnaPPARDFVGALRAAhkRTGQpglIAEVKKASPSRGVLRENFDPVEIA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 76 AIY-KHYASAISVLTDEKYFQGSFDFLPIVSQIAPQ-PILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAV 153
Cdd:PLN02460 146 QAYeKGGAACLSVLTDEKYFQGSFENLEAIRNAGVKcPLLCKEFIVDAWQIYYARSKGADAILLIAAVLPDLDIKYMLKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 154 AHSLEMGVLTEVSNEEELERAIAL-GAKVVGINNRDLRDLSIDLNRTREL-APKLGH-----NVTVISESGINT---YAQ 223
Cdd:PLN02460 226 CKSLGMAALIEVHDEREMDRVLGIeGVELIGINNRSLETFEVDISNTKKLlEGERGEqirekGIIVVGESGLFTpddVAY 305
|
250 260
....*....|....*....|....*..
gi 446906631 224 VRELSHFAngFLIGSALMAHDDLNAAV 250
Cdd:PLN02460 306 VQNAGVKA--VLVGESLVKQDDPGKGI 330
|
|
| PRK01222 |
PRK01222 |
phosphoribosylanthranilate isomerase; |
259-453 |
3.99e-49 |
|
phosphoribosylanthranilate isomerase;
Pssm-ID: 234923 Cd Length: 210 Bit Score: 166.52 E-value: 3.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 259 KVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAP--LQYVGVFRNHDIADVVDKAKVLSLAAVQLHG 336
Cdd:PRK01222 6 KICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPpfVKVVGVFVNASDEEIDEIVETVPLDLLQLHG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 337 NEDQQYIDTLRGALpaNIAIWKALSVGETLPARELQH----VDKYVLD---NGQGGSGQRFDWSLLNGQSLGNVLLAGGL 409
Cdd:PRK01222 86 DETPEFCRQLKRRY--GLPVIKALRVRSAGDLEAAAAyygdADGLLLDayvGLPGGTGKTFDWSLLPAGLAKPWILAGGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446906631 410 GADNCVEA-AQTGCAGLDFNSAVESQPGIKDARLLASVFQTLRAY 453
Cdd:PRK01222 164 NPDNVAEAiRQVRPYGVDVSSGVESAPGIKDPEKIRAFIEAVKSA 208
|
|
| PRK13957 |
PRK13957 |
indole-3-glycerol-phosphate synthase; Provisional |
2-249 |
2.04e-48 |
|
indole-3-glycerol-phosphate synthase; Provisional
Pssm-ID: 140013 Cd Length: 247 Bit Score: 166.21 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 2 MQTVLAKIVADKAIWVETRKEQQPLASFQNEVQpstrhfyDALQGARTSFILECKKASPSKGVIRDDFDPARIAAIYKHY 81
Cdd:PRK13957 1 MHRVLREIIETKQNEIEKISRWDPLPDRGLPLR-------DSLKSRSFSIIAECKRKSPSAGELRADYHPVQIAKTYETL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 82 -ASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDEQYRQLAAVAHSLEMG 160
Cdd:PRK13957 74 gASAISVLTDQSYFGGSLEDLKSVSSELKIPVLRKDFILDEIQIREARAFGASAILLIVRILTPSQIKSFLKHASSLGMD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 161 VLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSAL 240
Cdd:PRK13957 154 VLVEVHTEDEAKLALDCGAEIIGINTRDLDTFQIHQNLVEEVAAFLPPNIVKVGESGIESRSDLDKFRKLVDAALIGTYF 233
|
....*....
gi 446906631 241 MAHDDLNAA 249
Cdd:PRK13957 234 MEKKDIRKA 242
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
52-254 |
1.05e-45 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 168.67 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 52 ILECKKASPSKGVIRDDFDPARIAAIY-KHYASAISVLTDEKYFQGSFDFLPIVSQIAPQPILCKDFIIDPYQIYLARYY 130
Cdd:PRK13802 53 IAEIKRASPSKGHLSDIPDPAALAREYeQGGASAISVLTEGRRFLGSLDDFDKVRAAVHIPVLRKDFIVTDYQIWEARAH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 131 QADACLLMLSVLDDEQYRQLAAVAHSLEMGVLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNV 210
Cdd:PRK13802 133 GADLVLLIVAALDDAQLKHLLDLAHELGMTVLVETHTREEIERAIAAGAKVIGINARNLKDLKVDVNKYNELAADLPDDV 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446906631 211 TVISESGINTYAQVRELSHF-ANGFLIGSALMAHDDLNAAVRRVL 254
Cdd:PRK13802 213 IKVAESGVFGAVEVEDYARAgADAVLVGEGVATADDHELAVERLV 257
|
|
| PLN02363 |
PLN02363 |
phosphoribosylanthranilate isomerase |
259-440 |
6.58e-26 |
|
phosphoribosylanthranilate isomerase
Pssm-ID: 215207 Cd Length: 256 Bit Score: 105.71 E-value: 6.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 259 KVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAP---LQYVGVFRNHDIADVVDKAKVLSLAAVQLH 335
Cdd:PLN02363 50 KMCGITSARDAAMAVEAGADFIGMILWPKSKRSISLSVAKEISQVAReggAKPVGVFVDDDANTILRAADSSDLELVQLH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 336 GNEDQQYIDTLRGALPAnIAIWKALSVGETL---PARELQHVDKYVLDNGQGGSGQRFDWS---LLNGQSLGNVLLAGGL 409
Cdd:PLN02363 130 GNGSRAAFSRLVRERKV-IYVLNANEDGKLLnvvPEEDCHLADWILVDSATGGSGKGFNWQnfkLPSVRSRNGWLLAGGL 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 446906631 410 GADNCVEAAqtgCA----GLDFNSAVESQPGI-KDA 440
Cdd:PLN02363 209 TPENVHEAV---SLlkptGVDVSSGICGPDGIrKDP 241
|
|
| PRK13958 |
PRK13958 |
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional |
259-451 |
1.37e-15 |
|
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
Pssm-ID: 184418 Cd Length: 207 Bit Score: 75.15 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 259 KVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAP--LQYVGVFRNHDIADVVDKAKVLSLAAVQLHG 336
Cdd:PRK13958 4 KFCGFTTIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPnhIDKVCVVVNPDLTTIEHILSNTSINTIQLHG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 337 NEDQQYIDTLRGALPaNIAIWKALSVGETLPARELQ---HVDKYVLDNGQ---GGSGQRFDWSLLNGQSLGNVLLAGGLG 410
Cdd:PRK13958 84 TESIDFIQEIKKKYS-SIKIIKALPADENIIQNINKykgFVDLFIIDTPSvsyGGTGQTYDWTILKHIKDIPYLIAGGIN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446906631 411 ADNC--VEAAQTGCAGLDFNSAVESQpGIKDARLLASVFQTLR 451
Cdd:PRK13958 163 SENIqtVEQLKLSHQGYDIASGIETN-GRKDINKMTAIVNIVK 204
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
259-451 |
5.43e-15 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 77.16 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 259 KVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVE-QAQEVMAAAP---LQYVGVFRNHDIADVVDKAKVLSLAAVQL 334
Cdd:PRK13803 6 KICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVGNKfLAPNLEKAIRkagGRPVGVFVNESAKAMLKFSKKNGIDFVQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 335 HGNEDQQYIDTLRGALPANIAIWKALSVGETLPAREL----QHVDKYVLDN---GQGGSGQRFDWSLLNGQSLGNV-LLA 406
Cdd:PRK13803 86 HGAESKAEPAYCQRIYKKSIKKIGSFLIDDAFGFEVLdeyrDHVKYFLFDNktkIYGGSGKSFDWEKFYNYNFKFPfFLS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446906631 407 GGLGADNCVEAAQTGCA---GLDFNSAVESQPGIKDARLLASVFQTLR 451
Cdd:PRK13803 166 GGLSPTNFDRIINLTHPqilGIDVSSGFEDSPGNKKLTLLKSFITNVK 213
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
68-238 |
3.96e-14 |
|
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: 71.08 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 68 DFDPARIAAIYKHY-ASAISVLTDEKYFQGSF----DFLPIVSQIAPQPILCKDFIIDPYQIY-----LARYYQADACLL 137
Cdd:cd04722 11 SGDPVELAKAAAEAgADAIIVGTRSSDPEEAEtddkEVLKEVAAETDLPLGVQLAINDAAAAVdiaaaAARAAGADGVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906631 138 MLSV-----LDDEQYRQLAAVAHSLEMGVLTEVSNEEELERAIALGAKVVGINNRDLRDLSIDLNRT---RELAPKLGHN 209
Cdd:cd04722 91 HGAVgylarEDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIadlLLILAKRGSK 170
|
170 180 190
....*....|....*....|....*....|
gi 446906631 210 VTVISESGINTYAQVRELSHF-ANGFLIGS 238
Cdd:cd04722 171 VPVIAGGGINDPEDAAEALALgADGVIVGS 200
|
|
|