|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-357 |
0e+00 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 575.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 1 MEKVTVTLGERSYPINIAPSLYNEPGA-FWPLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGElLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 80 IMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 160 PASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKEtSG 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERE-SG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 240 LRALLNLGHTFGHAIEAHMGYgVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKGPsQMKPDDYLPH 319
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLP-ALDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 757601119 320 MMRDKKVMGGKLHLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-357 |
1.31e-176 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 493.88 E-value: 1.31e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 12 SYPINIAPSLYNEPGAFWPLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLFIMNDVFTALLEK 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 92 HHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLK 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 172 TLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKETsGLRALLNLGHTFG 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREK-GLRAILNFGHTFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 252 HAIEAHMGYGvWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKgPSQMKPDDYLPHMMRDKKVMGGKL 331
Cdd:cd08195 240 HAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTS-IKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 757601119 332 HLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:cd08195 318 RFVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-349 |
1.62e-163 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 464.24 E-value: 1.62e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 1 MEKVTVTLGERSYPINIAPSLYNEPGAFWPLATGQRAMIVTNETLAPIYLEKVKHALESSG--VKVDSIILPDGEQYKSL 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGpeLTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 79 FIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFY 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 159 QPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKEtS 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKE-S 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 239 GLRALLNLGHTFGHAIEAHMGYGVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKGPSQMKPDDYLP 318
Cdd:PLN02834 306 GLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKS 385
|
330 340 350
....*....|....*....|....*....|..
gi 757601119 319 HMMRDKKVMGGKLHLI-LPTTIGHSEMRADID 349
Cdd:PLN02834 386 LMAVDKKVADGLLRLIlLKGELGNCVFTGDFD 417
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-326 |
4.04e-161 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 451.18 E-value: 4.04e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 66 SIILPDGEQYKSLFIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAV 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 146 NHPLGKNMIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCEL 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 226 KAQVVAADEKEtSGLRALLNLGHTFGHAIEAHMGYGVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPV 305
Cdd:pfam01761 161 KADVVAQDEKE-SGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPT 239
|
250 260
....*....|....*....|.
gi 757601119 306 KGPsQMKPDDYLPHMMRDKKV 326
Cdd:pfam01761 240 SLP-DLDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-357 |
3.58e-159 |
|
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273575 Cd Length: 344 Bit Score: 449.78 E-value: 3.58e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 13 YPINIAPSLYNEPGAFwpLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLFIMNDVFTALLEKH 92
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEE--LAEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 93 HNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLKT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 173 LPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDN-QAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTFG 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQElEHLEELIKRSIEVKASIVAEDEKE-SGLRAILNFGHTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 252 HAIEAHMGYGVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKGPSQMKPDDYLPHMMRDKKVMGGKL 331
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKI 317
|
330 340
....*....|....*....|....*.
gi 757601119 332 HLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:TIGR01357 318 RFVLLEEIGKAALAREVPDEMVLELL 343
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-357 |
0e+00 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 575.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 1 MEKVTVTLGERSYPINIAPSLYNEPGA-FWPLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGElLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 80 IMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 160 PASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKEtSG 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERE-SG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 240 LRALLNLGHTFGHAIEAHMGYgVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKGPsQMKPDDYLPH 319
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLP-ALDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 757601119 320 MMRDKKVMGGKLHLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-357 |
1.31e-176 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 493.88 E-value: 1.31e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 12 SYPINIAPSLYNEPGAFWPLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLFIMNDVFTALLEK 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 92 HHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLK 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 172 TLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKETsGLRALLNLGHTFG 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREK-GLRAILNFGHTFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 252 HAIEAHMGYGvWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKgPSQMKPDDYLPHMMRDKKVMGGKL 331
Cdd:cd08195 240 HAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTS-IKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 757601119 332 HLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:cd08195 318 RFVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-349 |
1.62e-163 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 464.24 E-value: 1.62e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 1 MEKVTVTLGERSYPINIAPSLYNEPGAFWPLATGQRAMIVTNETLAPIYLEKVKHALESSG--VKVDSIILPDGEQYKSL 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGpeLTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 79 FIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFY 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 159 QPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKEtS 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKE-S 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 239 GLRALLNLGHTFGHAIEAHMGYGVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKGPSQMKPDDYLP 318
Cdd:PLN02834 306 GLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKS 385
|
330 340 350
....*....|....*....|....*....|..
gi 757601119 319 HMMRDKKVMGGKLHLI-LPTTIGHSEMRADID 349
Cdd:PLN02834 386 LMAVDKKVADGLLRLIlLKGELGNCVFTGDFD 417
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-326 |
4.04e-161 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 451.18 E-value: 4.04e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 66 SIILPDGEQYKSLFIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAV 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 146 NHPLGKNMIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCEL 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 226 KAQVVAADEKEtSGLRALLNLGHTFGHAIEAHMGYGVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPV 305
Cdd:pfam01761 161 KADVVAQDEKE-SGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPT 239
|
250 260
....*....|....*....|.
gi 757601119 306 KGPsQMKPDDYLPHMMRDKKV 326
Cdd:pfam01761 240 SLP-DLDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-357 |
3.58e-159 |
|
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273575 Cd Length: 344 Bit Score: 449.78 E-value: 3.58e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 13 YPINIAPSLYNEPGAFwpLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLFIMNDVFTALLEKH 92
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEE--LAEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 93 HNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLKT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 173 LPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDN-QAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTFG 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQElEHLEELIKRSIEVKASIVAEDEKE-SGLRAILNFGHTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 252 HAIEAHMGYGVWLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKGPSQMKPDDYLPHMMRDKKVMGGKL 331
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKI 317
|
330 340
....*....|....*....|....*.
gi 757601119 332 HLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:TIGR01357 318 RFVLLEEIGKAALAREVPDEMVLELL 343
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-341 |
9.99e-89 |
|
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose; 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. They are important antibacterial agents. DOIS is a homolog of the dehydroquinate synthase which catalyzes the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate (DHQ) in the shikimate pathway.
Pssm-ID: 341476 Cd Length: 355 Bit Score: 270.99 E-value: 9.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 12 SYPINIAPSLYNEPGAFWPLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLFIMNDVFTALLEK 91
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAERLIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 92 HHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLK 171
Cdd:cd08197 81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 172 TLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTFG 251
Cdd:cd08197 161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYE-KKEGLILEYGHTVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 252 HAIEAHMGYGVwLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVKGPSQMKPDDYLPHMMRDKK-----V 326
Cdd:cd08197 240 HAIELLSGGEL-SHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPDGISVEAILEVIRYDNKrgyikA 318
|
330
....*....|....*
gi 757601119 327 MGGKLHLILPTTIGH 341
Cdd:cd08197 319 DADTIRMVLLEKLGK 333
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
35-340 |
4.99e-85 |
|
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.
Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 260.80 E-value: 4.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 35 QRAMIVTNETLAPIYLEKVKHALeSSGVKVDSIILPDGEQYKSLFIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFA 114
Cdd:cd08169 24 DQCLIIVDSGVPDLIVNYLAEYF-GYYLEVHVFIIQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDVVGFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 115 AASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDG 194
Cdd:cd08169 103 AATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIADN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 195 DFFTWLENNIDALVALDNQAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTFGHAIEAHMGYGVwLHGEAVAAGIV 274
Cdd:cd08169 183 DFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDE-QGKRRGLNYGHTFGHALELASGYKI-PHGEAVAVGMA 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757601119 275 MAARTAELIGQFTPEQTQRVIALLERASLPVKGPSQMKPDDYLPHMMRDKKVMGGKLHLILPTTIG 340
Cdd:cd08169 261 YAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDSLYEYLESDKKSLYGNLGMILLSGVG 326
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
12-357 |
2.43e-68 |
|
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.
Pssm-ID: 341478 Cd Length: 349 Bit Score: 218.55 E-value: 2.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 12 SYPINIAPSLY---NEPGAFWPLATGQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLFIMNDVFTAL 88
Cdd:cd08199 1 SYDVVLVDDLFdpeNPTLADAYGRPGRRRLVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTMETVLRIVDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 89 LEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLD 168
Cdd:cd08199 81 DDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 169 CLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVA---LDNQAMAYCIRRCCELKAQVVAADEKETSgLRALLN 245
Cdd:cd08199 161 FLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVEtrfFQDEVADEIIRRAIQGMLEELAPNLWEHD-LERLVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 246 LGHTFGHAIEAHMGYGVwLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLPVkgpsqmkpddylPHMMRDKK 325
Cdd:cd08199 240 FGHTFSPILEMAAAPEL-LHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPV------------WHPLCTPD 306
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 757601119 326 VM-----------GGKLHLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:cd08199 307 LLwraledivkhrDGLQRLPLPKGIGECVFVNDVTEEELERAL 349
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
51-353 |
3.84e-63 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 210.49 E-value: 3.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 51 EKVKHALESSGVKVDSIILPDGEQYKSLFIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTT 130
Cdd:PRK14021 225 DRARTLLRQGGYEVSDIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 131 LLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVAL 210
Cdd:PRK14021 305 LLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAF 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 211 DNQA---------MAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTFGHAIEaHMGYGVWLHGEAVAAGIVMAARTAE 281
Cdd:PRK14021 385 DGSTflgspledvVAELIERTVKVKAYHVSSDLKE-AGLREFLNYGHTLGHAIE-KLEHFRWRHGNAVAVGMVYAAELAH 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757601119 282 LIGQFTPEQTQRVIALLERASLPVKGpSQMKPDDYLPHMMRDKKVMGGKLHLILPTTIGHSEMRADIDAQTV 353
Cdd:PRK14021 463 LLGYIDQDLVDYHRSLLASLGLPTSW-NGGSFDDVLALMHRDKKARGNELRFVVLDEIGHPVHLDNPPAEAV 533
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
65-357 |
1.72e-61 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 202.05 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 65 DSIILPDGEQYKSLFIMNDVFTALLEKHH-NRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKT 143
Cdd:PRK06203 80 EPLVVPGGEAAKNDPALVEALHAAINRHGiDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 144 AVNHPLGKNMIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCC 223
Cdd:PRK06203 160 GINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 224 ELKAQVVAA--DEKETSGLRAlLNLGHTFGHAIEAHMGYGVwLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERA 301
Cdd:PRK06203 240 ELHLEHIAGggDPFEFGSSRP-LDFGHWSAHKLEQLTNYAL-RHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRAL 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 302 SLPVKGPSQMKPDDYLPHMMRD----KKVMGGKLHLILPTTIGHSEMRADIDAQTVIAAI 357
Cdd:PRK06203 318 GFPLYHPALATRDSKGRELLKGleefREHLGGRLTITLLTGIGRGIEVHEIDLDLLRQAI 377
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
67-349 |
1.61e-60 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; This family contains dehydroquinate synthase-like proteins. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. The activity of DHQS requires NAD as cofactor. Proteins of this family share sequence similarity and functional motifs with that of dehydroquinate synthase, but the specific function has not been characterized.
Pssm-ID: 341477 Cd Length: 366 Bit Score: 198.56 E-value: 1.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 67 IILPDGEQYK-SLFIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAV 145
Cdd:cd08198 70 LIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 146 NHPLGKNMIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFTWLENNIDALVALDNQAMAYCIRRCCEL 225
Cdd:cd08198 150 NFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 226 KAQVVAA--DEKETSGLRAlLNLGHTFGHAIEAHMGYGVwLHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASL 303
Cdd:cd08198 230 HLDHIAAsgDPFETGSARP-LDFGHWSAHKLEQLSGYAL-RHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGL 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 757601119 304 PVKGPS-QMKPDDYLPHMMRD-KKVMGGKLHLILPTTIG---------HSEMRADID 349
Cdd:cd08198 308 PLWHPLlERDGVLELLDGLEEfREHLGGRLTITLLRGIGvgvevheidLDLMEEAID 364
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
67-330 |
1.22e-42 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 154.68 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 67 IILPDGEQYKSLFIMNDVFTALLEKHHNRDTTLIALGGGVIGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVN 146
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAID 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 147 HPLGKNMIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGIILDGDFFtwLENNIDALVALDNQAMAYCIRRCCELK 226
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVE--LFDEPEKIEKRNLRVLSEMVKISVEEK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 227 AQVVAADEKETsGLRALLNLGHTFGHAIEAHMGYGvwlHGEAVAAGIVMAARTAELIGqFTPEQTQRVIALLERASLPVK 306
Cdd:PRK13951 367 ARIVMEDPYDM-GLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGIEKETMYLYRKG-IVPKETMRWIVEKVKQIVPIP 441
|
250 260
....*....|....*....|....
gi 757601119 307 GPSQMKPDDYLpHMMRDKKVMGGK 330
Cdd:PRK13951 442 VPSVDVEKARN-LILNDKKILKGS 464
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
34-306 |
1.00e-23 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 98.59 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 34 GQRAMIVTNETLAPIYLEKVKHALeSSGVKVDSIILPDGEqyKSLfimnDVFTALLEKHHN-RDTTLIALGGGVIGDLTG 112
Cdd:cd07766 22 FDRALVVSDEGVVKGVGEKVADSL-KKGLAVAIFDFVGEN--PTF----EEVKNAVERARAaEADAVIAVGGGSTLDTAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 113 FAAASYQRGVRFIQIPTTLLSqvDSSVGGKTAVNHPLGKN-MIGAFYQPASVVIDLDCLKTLPKRELASGLAEVIKYGII 191
Cdd:cd07766 95 AVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 192 ldgdfftwLENNIDAlvaldnqamaycirrCCELKAQVVAadeketsglRALLNLGHTFGHAIEAHMGYgvwLHGEAVAA 271
Cdd:cd07766 173 --------LEKVVEA---------------ATLAGMGLFE---------SPGLGLAHAIGHALTAFEGI---PHGEAVAV 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 757601119 272 GIVMAARTAEligQFTPEQTQ---RVIALLERASLPVK 306
Cdd:cd07766 218 GLPYVLKVAN---DMNPEPEAaieAVFKFLEDLGLPTH 252
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
34-270 |
2.94e-14 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 71.56 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 34 GQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEqykslfimNDVFTA--LLEKHHNRDTT-LIALGGGVIGDL 110
Cdd:pfam13685 19 FRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGN--------ADMETAekLVGALRERDADaVVGVGGGTVIDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 111 TGFAAasYQRGVRFIQIPTTLlsqvdsSVGGKTAVNHPL----GKNMIGAfYQPASVVIDLDCLKTLPKRELASGLAEVI 186
Cdd:pfam13685 91 AKYAA--FKLGKPFISVPTAA------SNDGFASPGASLtvdgKKRSIPA-AAPFGVIADTDVIAAAPRRLLASGVGDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 187 -KYGIILDGdfftWLENNIDALVALDNQAMAYcirrcCELKAQVVAADEKETSGLRALLNLG---------------HTF 250
Cdd:pfam13685 162 aKITAVADW----ELAHAEEVAAPLALLSAAM-----VMNFADRPLRDPGDIEALAELLSALamggagssrpasgseHLI 232
|
250 260
....*....|....*....|.
gi 757601119 251 GHAIE-AHMGYGvwLHGEAVA 270
Cdd:pfam13685 233 SHALDmIAPKQA--LHGEQVG 251
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
34-324 |
6.07e-11 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 62.91 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 34 GQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQ----YKSLFimndvftALLEKHHNRDTTLIALGGGVIGD 109
Cdd:cd08175 24 GKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEGDliadEAAVG-------KVLLELEKDTDLIIAVGSGTIND 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 110 LTGFAaaSYQRGVRFIQIPTTllsqvdSSVGGKTAVNHPLgknMIGAFYQ------PASVVIDLDCLKTLPKRELASGLA 183
Cdd:cd08175 97 LTKYA--AYKLGIPYISVPTA------PSMDGYTSSGAPI---IVDGVKKtfpahaPKAIFADLDVLANAPQRMIAAGFG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 184 EVI-KYGIILDgdfftWLENNI-------DALVALdnqaMAYCIRRCCELKAQVVAADEKETSGL-RALLNLG------- 247
Cdd:cd08175 166 DLLgKYTALAD-----WKLSHLlggeyycPEVADL----VQEALEKCLDNAEGIAARDPEAIEALmEALILSGlamqlvg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 248 ---------HTFGHAIE-AHMGYGV--WLHGEAVAAG-IVMAartAELIGQFTPeQTQRVIALLERASLPVKgPSQMK-P 313
Cdd:cd08175 237 nsrpasgaeHHLSHYWEmEFLRLGKppVLHGEKVGVGtLLIA---ALYILEQLP-PPEELRELLRKAGAPTT-PEDLGiD 311
|
330
....*....|....*..
gi 757601119 314 DDYLP------HMMRDK 324
Cdd:cd08175 312 RDLLRdslrlaKEIRDR 328
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
30-305 |
1.80e-09 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 58.30 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 30 PLATGQRAMIVTNETLAPIYLEKVKHALESSG--VKVDSIILPDGEQYKSLFIMNDVFTALlekhhnrdttlIALGGGVI 107
Cdd:cd08174 21 RNQGFGKVAIVTGEGIDELLGEDILESLEEAGeiVTVEENTDNSAEELAEKAFSLPKVDAI-----------VGIGGGKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 108 GDLTGFAAasYQRGVRFIQIPTTLLSqvD---SSV------GGKTAVnhplGKNMigafyqPASVVIDLDCLKTLPKREL 178
Cdd:cd08174 90 LDVAKYAA--FLSKLPFISVPTSLSN--DgiaSPVavlkvdGKRKSL----GAKM------PYGVIVDLDVIKSAPRRLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 179 ASGLAEVI-KYGIILDgdfftW-LENN-----IDALVALDNQAMAYCIRRCCElkaqvvaADEKETSGLRALLN---LG- 247
Cdd:cd08174 156 LAGIGDLIsNITALYD-----WkLAEEkggepVDDFAYLLSRTAADSLLNTPG-------KDIKDDEFLKELAEslvLSg 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757601119 248 ----------------HTFGHAIEAHMGyGVWLHGEAVAAGIVMAARtaeLIGQftpeQTQRVIALLERASLPV 305
Cdd:cd08174 224 iameiagssrpasgseHLISHALDKLFP-GPALHGIQVGLGTYFMSF---LQGQ----RYEEIRDVLKRTGFPL 289
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
31-276 |
9.71e-09 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 56.06 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 31 LATGQRAMIVTNETLAPIYLEKVKHALESSGvKVDSIILPDGeqykslfIMNDVFTALLEKHHNRDTTLIALGGGVIGDL 110
Cdd:PRK00843 31 LKLTGRALIVTGPTTKKIAGDRVEENLEDAG-DVEVVIVDEA-------TMEEVEKVEEKAKDVNAGFLIGVGGGKVIDV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 111 TGFAaaSYQRGVRFIQIPTT-----LLSQVDSSVGGKTavNHPLGKNMigafyqPASVVIDLDCLKTLPKRELASGLAEV 185
Cdd:PRK00843 103 AKLA--AYRLGIPFISVPTAashdgIASPRASIKGGGK--PVSVKAKP------PLAVIADTEIIAKAPYRLLAAGCGDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 186 I-KYGIILDGDFFTWLENN-----------IDALVALDNQAMaycIRRCCELKAQVVAadeketsglRALLNLG------ 247
Cdd:PRK00843 173 IsNYTAVKDWRLAHRLRGEyyseyaaalslMTAKMLIENADI---IKPGLEESARLVV---------KALISSGvamsia 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 757601119 248 ----------HTFGHAIEAhMGYGVWLHGEAVAAG-IVMA 276
Cdd:PRK00843 241 gssrpasgseHLFSHALDR-LAPGPALHGEQCGVGtIIMM 279
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
34-278 |
3.13e-08 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 54.48 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 34 GQRAMIVTNETLAPIYLEKVKHALESSGVKVDSIILPDGEQYKSLfimnDVFTALleKHHNRDTTLIALGGGVIGDLTgf 113
Cdd:cd08173 25 GKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEV----EKVKKL--IKESKADFIIGVGGGKVIDVA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 114 AAASYQRGVRFIQIPTTL-----------LSQVDSSVGGKTavnHPlgknmigafyqPASVVIDLDCLKTLPKRELASGL 182
Cdd:cd08173 97 KYAAYKLNLPFISIPTSAshdgiaspfasIKGGDKPYSIKA---KA-----------PIAIIADTEIISKAPKRLLAAGC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 183 AEVI-KYGIILDGDFFTWLEN-----------NIDALVALDNqamAYCIRRCCELKAQVVaadeketsgLRALLNLG--- 247
Cdd:cd08173 163 GDLIsNITAVKDWRLAHRLKGeyyseyaaslaLMSAKLIIEN---ADLIKPGLEEGVRTV---------VKALISSGvam 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 757601119 248 -------------HTFGHAIEAhMGYGVWLHGEAVAAGIVMAAR 278
Cdd:cd08173 231 siagssrpasgseHLFSHALDK-LAPGPALHGEQCGVGTIMMAY 273
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
99-304 |
1.30e-07 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 52.57 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 99 LIALGGGVIGDLTGFAaaSYQRGVRFIQIPTTllsqvdSSVGGKTAVNHPLGKNmiGAFYQ-----PASVVIDLDCLKTL 173
Cdd:cd08549 74 VIGIGGGRSIDTGKYL--AYKLKIPFISVPTS------ASNDGIASPIVSLRIP--GVKKTfmadaPIAIIADTEIIKKS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 174 PKRELASGLAEVI-KYGIILDGDFFTWLENNI--DALVALDNQAMAYCIRrccelKAQVVAADEKETSGL-RALLNLG-- 247
Cdd:cd08549 144 PRRLLSAGIGDLVsNITAVLDWKLAHKEKGEKysEFAAILSKTSAKELVS-----YVLKASDLEEYHRVLvKALVGSGia 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757601119 248 --------------HTFGHAIEAHMGYGVW---LHGEAVAAGIVMAARTAELIGQFTPEQTQRVIALLERASLP 304
Cdd:cd08549 219 maiagssrpasgseHLFSHALDKLKEEYLNinvLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAP 292
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
19-105 |
9.26e-03 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 37.55 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757601119 19 PSLYNEPGAFWPLAT----GQRAMIVTNETLAPI-YLEKVKHALESSGVKVD--SIILPD---GEQYKSLFIMNDVftal 88
Cdd:cd08178 4 PKIYFEPGCLPYLLLelpgVKRAFIVTDRVLYKLgYVDKVLDVLEARGVETEvfSDVEPDptlSTVRKGLEAMNAF---- 79
|
90
....*....|....*..
gi 757601119 89 lekhhnRDTTLIALGGG 105
Cdd:cd08178 80 ------KPDVIIALGGG 90
|
|
| |
