|
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: 551.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 1 MEKITVTLGERSYPITIASGLFHQ-PETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLT 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 80 VMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 160 PASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKEtSG 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERE-SG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 240 LRALLNLGHTYGHAIEAHMGYgVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDeMQPEDYLPH 319
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 490370239 320 MMRDKKVSAGKLHLVLPKGIGQSELRADISREQVYKAI 357
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-357 |
7.75e-167 |
|
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: 469.23 E-value: 7.75e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 12 SYPITIASGLFHQPETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLTVMNDVFTALLEK 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 92 NHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLA 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 172 TLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKETsGLRALLNLGHTYG 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREK-GLRAILNFGHTFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 252 HAIEAHMGYGvWLHGEavaagmvmaaktA------------QDLGQFTQAETQRVIQLLKKANLPVNgPDEMQPEDYLPH 319
Cdd:cd08195 240 HAIESASGYK-LLHGE------------AvaigmvaaarlsVKLGLLSEEDLERIRALLKKLGLPTS-IKDLDPEELLEA 305
|
330 340 350
....*....|....*....|....*....|....*...
gi 490370239 320 MMRDKKVSAGKLHLVLPKGIGQSELRADISREQVYKAI 357
Cdd:cd08195 306 MKRDKKNRGGKIRFVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-357 |
2.03e-158 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 451.53 E-value: 2.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 1 MEKITVTLGERSYPITIASGLFHQPETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQG--VLVDSVILPDGEQYKSL 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGpeLTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 79 TVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFY 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 159 QPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKEtS 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKE-S 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 239 GLRALLNLGHTYGHAIEAHMGYGVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDEMQPEDYLP 318
Cdd:PLN02834 306 GLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKS 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490370239 319 HMMRDKKVSAGKLHLVLPKG-IGQSELRADISREQVYKAI 357
Cdd:PLN02834 386 LMAVDKKVADGLLRLILLKGeLGNCVFTGDFDREALEETL 425
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-326 |
2.44e-152 |
|
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: 429.23 E-value: 2.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 66 SVILPDGEQYKSLTVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAV 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 146 NHPLGKNMIGAFYQPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCEL 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 226 KAQVVAADEKEtSGLRALLNLGHTYGHAIEAHMGYGVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPV 305
Cdd:pfam01761 161 KADVVAQDEKE-SGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPT 239
|
250 260
....*....|....*....|.
gi 490370239 306 NGPDEmQPEDYLPHMMRDKKV 326
Cdd:pfam01761 240 SLPDL-DVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-357 |
1.62e-149 |
|
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: 425.51 E-value: 1.62e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 13 YPITIASGLFHQPETFLplKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLTVMNDVFTALLEKN 92
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEEL--AEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 93 HNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLAT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 173 LPPRELSSGLAEVIKYGIILDKDFFIWLENNIDK-LIALEPKAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTYG 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVAEDEKE-SGLRAILNFGHTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 252 HAIEAHMGYGVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDEMQPEDYLPHMMRDKKVSAGKL 331
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKI 317
|
330 340
....*....|....*....|....*.
gi 490370239 332 HLVLPKGIGQSELRADISREQVYKAI 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: 551.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 1 MEKITVTLGERSYPITIASGLFHQ-PETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLT 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 80 VMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 160 PASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKEtSG 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERE-SG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 240 LRALLNLGHTYGHAIEAHMGYgVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDeMQPEDYLPH 319
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 490370239 320 MMRDKKVSAGKLHLVLPKGIGQSELRADISREQVYKAI 357
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-357 |
7.75e-167 |
|
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: 469.23 E-value: 7.75e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 12 SYPITIASGLFHQPETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLTVMNDVFTALLEK 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 92 NHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLA 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 172 TLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKETsGLRALLNLGHTYG 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREK-GLRAILNFGHTFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 252 HAIEAHMGYGvWLHGEavaagmvmaaktA------------QDLGQFTQAETQRVIQLLKKANLPVNgPDEMQPEDYLPH 319
Cdd:cd08195 240 HAIESASGYK-LLHGE------------AvaigmvaaarlsVKLGLLSEEDLERIRALLKKLGLPTS-IKDLDPEELLEA 305
|
330 340 350
....*....|....*....|....*....|....*...
gi 490370239 320 MMRDKKVSAGKLHLVLPKGIGQSELRADISREQVYKAI 357
Cdd:cd08195 306 MKRDKKNRGGKIRFVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-357 |
2.03e-158 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 451.53 E-value: 2.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 1 MEKITVTLGERSYPITIASGLFHQPETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQG--VLVDSVILPDGEQYKSL 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGpeLTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 79 TVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFY 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 159 QPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKEtS 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKE-S 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 239 GLRALLNLGHTYGHAIEAHMGYGVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDEMQPEDYLP 318
Cdd:PLN02834 306 GLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKS 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490370239 319 HMMRDKKVSAGKLHLVLPKG-IGQSELRADISREQVYKAI 357
Cdd:PLN02834 386 LMAVDKKVADGLLRLILLKGeLGNCVFTGDFDREALEETL 425
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-326 |
2.44e-152 |
|
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: 429.23 E-value: 2.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 66 SVILPDGEQYKSLTVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAV 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 146 NHPLGKNMIGAFYQPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCEL 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 226 KAQVVAADEKEtSGLRALLNLGHTYGHAIEAHMGYGVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPV 305
Cdd:pfam01761 161 KADVVAQDEKE-SGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPT 239
|
250 260
....*....|....*....|.
gi 490370239 306 NGPDEmQPEDYLPHMMRDKKV 326
Cdd:pfam01761 240 SLPDL-DVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-357 |
1.62e-149 |
|
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: 425.51 E-value: 1.62e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 13 YPITIASGLFHQPETFLplKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLTVMNDVFTALLEKN 92
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEEL--AEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 93 HNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLAT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 173 LPPRELSSGLAEVIKYGIILDKDFFIWLENNIDK-LIALEPKAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTYG 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVAEDEKE-SGLRAILNFGHTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 252 HAIEAHMGYGVWLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDEMQPEDYLPHMMRDKKVSAGKL 331
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKI 317
|
330 340
....*....|....*....|....*.
gi 490370239 332 HLVLPKGIGQSELRADISREQVYKAI 357
Cdd:TIGR01357 318 RFVLLEEIGKAALAREVPDEMVLELL 343
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-340 |
1.33e-84 |
|
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: 260.59 E-value: 1.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 12 SYPITIASGLFHQPETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLTVMNDVFTALLEK 91
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAERLIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 92 NHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLA 171
Cdd:cd08197 81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 172 TLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTYG 251
Cdd:cd08197 161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYE-KKEGLILEYGHTVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 252 HAIEAHMGYGVwLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDEMQPEDYLPHMMRDKK-----V 326
Cdd:cd08197 240 HAIELLSGGEL-SHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPDGISVEAILEVIRYDNKrgyikA 318
|
330
....*....|....
gi 490370239 327 SAGKLHLVLPKGIG 340
Cdd:cd08197 319 DADTIRMVLLEKLG 332
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
12-340 |
5.03e-83 |
|
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: 255.41 E-value: 5.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 12 SYPITIASGLFHQPETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLeQQGVLVDSVILPDGEQYKSLTVMNDVFTALLEK 91
Cdd:cd08169 1 EYPVFFGEGVFESVNSYIPRDAFDQCLIIVDSGVPDLIVNYLAEYF-GYYLEVHVFIIQGGEAYKTFQTVVEELERAAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 92 NHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLA 171
Cdd:cd08169 80 HLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 172 TLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTYG 251
Cdd:cd08169 160 TLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDE-QGKRRGLNYGHTFG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 252 HAIEAHMGYGVwLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNGPDEMQPEDYLPHMMRDKKVSAGKL 331
Cdd:cd08169 239 HALELASGYKI-PHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDSLYEYLESDKKSLYGNL 317
|
....*....
gi 490370239 332 HLVLPKGIG 340
Cdd:cd08169 318 GMILLSGVG 326
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
12-357 |
2.01e-65 |
|
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: 210.85 E-value: 2.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 12 SYPITIASGLFHQPETFL---PLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEQYKSLTVMNDVFTAL 88
Cdd:cd08199 1 SYDVVLVDDLFDPENPTLadaYGRPGRRRLVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTMETVLRIVDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 89 LEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLD 168
Cdd:cd08199 81 DDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 169 CLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIA--LEPKAMAY-CIRRCCELKAQVVAADEKETSgLRALLN 245
Cdd:cd08199 161 FLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVEtrFFQDEVADeIIRRAIQGMLEELAPNLWEHD-LERLVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 246 LGHTYGHAIEAHMGYGVwLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPVNgpDEMQPEDYLPHMMRD-K 324
Cdd:cd08199 240 FGHTFSPILEMAAAPEL-LHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVW--HPLCTPDLLWRALEDiV 316
|
330 340 350
....*....|....*....|....*....|...
gi 490370239 325 KVSAGKLHLVLPKGIGQSELRADISREQVYKAI 357
Cdd:cd08199 317 KHRDGLQRLPLPKGIGECVFVNDVTEEELERAL 349
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
51-341 |
4.09e-56 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 192.00 E-value: 4.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 51 DKVTNTLEQQGVLVDSVILPDGEQYKSLTVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTT 130
Cdd:PRK14021 225 DRARTLLRQGGYEVSDIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 131 LLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIAL 210
Cdd:PRK14021 305 LLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAF 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 211 EPKA---------MAYCIRRCCELKAQVVAADEKEtSGLRALLNLGHTYGHAIEaHMGYGVWLHGEAVAAGMVMAAKTAQ 281
Cdd:PRK14021 385 DGSTflgspledvVAELIERTVKVKAYHVSSDLKE-AGLREFLNYGHTLGHAIE-KLEHFRWRHGNAVAVGMVYAAELAH 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 282 DLGQFTQAETQRVIQLLKKANLPVNGPDEMQpEDYLPHMMRDKKVSAGKLHLVLPKGIGQ 341
Cdd:PRK14021 463 LLGYIDQDLVDYHRSLLASLGLPTSWNGGSF-DDVLALMHRDKKARGNELRFVVLDEIGH 521
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
63-357 |
1.48e-54 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 183.94 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 63 LVDSVILPDGEQYK-SLTVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGG 141
Cdd:PRK06203 78 VAEPLVVPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 142 KTAVNHPLGKNMIGAFYQPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRR 221
Cdd:PRK06203 158 KNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 222 CCELKAQVVAA--DEKETSGLRAlLNLGHTYGHAIEAHMGYGVwLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLK 299
Cdd:PRK06203 238 CAELHLEHIAGggDPFEFGSSRP-LDFGHWSAHKLEQLTNYAL-RHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLR 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 300 KANLPVNGPdEMQPEDYLP------------HMmrdkkvsAGKLHLVLPKGIGQSELRADISREQVYKAI 357
Cdd:PRK06203 316 ALGFPLYHP-ALATRDSKGrellkgleefreHL-------GGRLTITLLTGIGRGIEVHEIDLDLLRQAI 377
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
67-358 |
1.08e-52 |
|
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: 178.53 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 67 VILPDGEQYK-SLTVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAV 145
Cdd:cd08198 70 LIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 146 NHPLGKNMIGAFYQPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWLENNIDKLIALEPKAMAYCIRRCCEL 225
Cdd:cd08198 150 NFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 226 KAQVVAA--DEKETSGLRAlLNLGHTYGHAIEAHMGYGVwLHGEAVAAGMVMAAKTAQDLGQFTQAETQRVIQLLKKANL 303
Cdd:cd08198 230 HLDHIAAsgDPFETGSARP-LDFGHWSAHKLEQLSGYAL-RHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGL 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490370239 304 PVNGPD-EMQPEDYLPHMMRDKKVS-AGKLHLVLPKGIGQSELRADISREQVYKAIT 358
Cdd:cd08198 308 PLWHPLlERDGVLELLDGLEEFREHlGGRLTITLLRGIGVGVEVHEIDLDLMEEAID 364
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
67-343 |
4.67e-40 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 147.74 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 67 VILPDGEQYKSLTVMNDVFTALLEKNHNRDTTLLALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVN 146
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAID 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 147 HPLGKNMIGAFYQPASVVIDLDCLATLPPRELSSGLAEVIKYGIILDKDFFIWleNNIDKLIALEPKAMAYCIRRCCELK 226
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVELF--DEPEKIEKRNLRVLSEMVKISVEEK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 227 AQVVAADEKETsGLRALLNLGHTYGHAIEAHMGYGvwlHGEAVAAGMVMAAKTAQDLGqFTQAETQRVIQLLKKANLPVN 306
Cdd:PRK13951 367 ARIVMEDPYDM-GLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGIEKETMYLYRKG-IVPKETMRWIVEKVKQIVPIP 441
|
250 260 270
....*....|....*....|....*....|....*...
gi 490370239 307 GPDeMQPEDYLPHMMRDKKVSAG-KLHLVLPKGIGQSE 343
Cdd:PRK13951 442 VPS-VDVEKARNLILNDKKILKGsRVRLPYVKEIGKIE 478
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
34-305 |
1.14e-21 |
|
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: 93.20 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 34 GQQVMIVTNVTLAPLYLDKVTNTLeqqGVLVDSVILPDGEQYKSL-TVMNDVFTALLEKNhnrdTTLLALGGGVIGDLTG 112
Cdd:cd07766 22 FDRALVVSDEGVVKGVGEKVADSL---KKGLAVAIFDFVGENPTFeEVKNAVERARAAEA----DAVIAVGGGSTLDTAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 113 FAAASYQRGVRFIQVPTTLLSqvDSSVGGKTAVNHPLGKN-MIGAFYQPASVVIDLDCLATLPPRELSSGLAEVIKYGII 191
Cdd:cd07766 95 AVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 192 LDKdfFIWlennidklialepkamaycirRCCELKAQVVAadeketsglRALLNLGHTYGHAIEAHMGYgvwLHGEAVAA 271
Cdd:cd07766 173 LEK--VVE---------------------AATLAGMGLFE---------SPGLGLAHAIGHALTAFEGI---PHGEAVAV 217
|
250 260 270
....*....|....*....|....*....|....
gi 490370239 272 GMVMAAKTAQDLGQFTQAETQRVIQLLKKANLPV 305
Cdd:cd07766 218 GLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPT 251
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
32-267 |
8.57e-11 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 61.55 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 32 KKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEqyKSLTVMNDVFTALLEKNHnrdTTLLALGGGVIGDLT 111
Cdd:pfam13685 17 LGFRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGN--ADMETAEKLVGALRERDA---DAVVGVGGGTVIDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 112 GFAAasYQRGVRFIQVPTTLlsqvdsSVGGKTAVNHPL----GKNMIGAfYQPASVVIDLDCLATLPPRELSSGLAEVI- 186
Cdd:pfam13685 92 KYAA--FKLGKPFISVPTAA------SNDGFASPGASLtvdgKKRSIPA-AAPFGVIADTDVIAAAPRRLLASGVGDLLa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 187 KYGIILDKdffiWLENN--IDKLIALEPKAMaycirrcCELKAQVVAADEKETSGLRALLNLG---------------HT 249
Cdd:pfam13685 163 KITAVADW----ELAHAeeVAAPLALLSAAM-------VMNFADRPLRDPGDIEALAELLSALamggagssrpasgseHL 231
|
250
....*....|....*....
gi 490370239 250 YGHAIE-AHMGYGvwLHGE 267
Cdd:pfam13685 232 ISHALDmIAPKQA--LHGE 248
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
15-267 |
5.15e-09 |
|
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: 57.14 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 15 ITIASGLFHQ-PETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVILPDGEqykslTVMNDVFT--ALLEK 91
Cdd:cd08175 4 IVIGEGALKKlPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEG-----DLIADEAAvgKVLLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 92 NHNRDTTLLALGGGVIGDLTGFaaASYQRGVRFIQVPTTllsqvdSSVGGKTAVNHPLgknMIGAFYQ------PASVVI 165
Cdd:cd08175 79 LEKDTDLIIAVGSGTINDLTKY--AAYKLGIPYISVPTA------PSMDGYTSSGAPI---IVDGVKKtfpahaPKAIFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 166 DLDCLATLPPRELSSGLAEVI-KYGIILDkdffiWLennIDKLIALEP------KAMAYCIRRCCELKAQVVAADEKETS 238
Cdd:cd08175 148 DLDVLANAPQRMIAAGFGDLLgKYTALAD-----WK---LSHLLGGEYycpevaDLVQEALEKCLDNAEGIAARDPEAIE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490370239 239 GL-RALLNLG----------------HTYGHAIE-AHMGYGV--WLHGE 267
Cdd:cd08175 220 ALmEALILSGlamqlvgnsrpasgaeHHLSHYWEmEFLRLGKppVLHGE 268
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
31-193 |
1.22e-06 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 49.89 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 31 LKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVlVDSVILPDGEqyksltvMNDVFTALLEKNHNRDTTLLALGGGVIGDL 110
Cdd:PRK00843 31 LKLTGRALIVTGPTTKKIAGDRVEENLEDAGD-VEVVIVDEAT-------MEEVEKVEEKAKDVNAGFLIGVGGGKVIDV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 111 TGFAaaSYQRGVRFIQVPTT-----LLSQVDSSVGGKTavNHPLGKNMigafyqPASVVIDLDCLATLPPRELSSGLAEV 185
Cdd:PRK00843 103 AKLA--AYRLGIPFISVPTAashdgIASPRASIKGGGK--PVSVKAKP------PLAVIADTEIIAKAPYRLLAAGCGDI 172
|
....*....
gi 490370239 186 I-KYGIILD 193
Cdd:PRK00843 173 IsNYTAVKD 181
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
15-186 |
6.14e-05 |
|
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: 44.43 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 15 ITIASGLFHQPETFL--PLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQG--VLVDSVILPDGEQYKSLTVMNDVFTALLe 90
Cdd:cd08174 4 LKIEEGALEHLGKYLadRNQGFGKVAIVTGEGIDELLGEDILESLEEAGeiVTVEENTDNSAEELAEKAFSLPKVDAIV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 91 knhnrdttllALGGGVIGDLTGFAAasYQRGVRFIQVPTTLLSqvD---SSV------GGKTAVnhplGKNMigafyqPA 161
Cdd:cd08174 83 ----------GIGGGKVLDVAKYAA--FLSKLPFISVPTSLSN--DgiaSPVavlkvdGKRKSL----GAKM------PY 138
|
170 180
....*....|....*....|....*
gi 490370239 162 SVVIDLDCLATLPPRELSSGLAEVI 186
Cdd:cd08174 139 GVIVDLDVIKSAPRRLILAGIGDLI 163
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
15-204 |
1.21e-04 |
|
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: 43.32 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 15 ITIASGLFHQPETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQqgvlvdsviLPDGEQYKSLTVMNDVftalLEKNHN 94
Cdd:cd08549 4 TIVGDGAINKIEEILKKLNLKRVLIITGKNTKAKYCRFFYDQLKT---------VCDIVYYDNIDNLEDE----LKKYTF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 95 RDTtLLALGGGVIGDLTGFAaaSYQRGVRFIQVPTTllsqvdSSVGGKTAVNHPLGKNmiGAFYQ-----PASVVIDLDC 169
Cdd:cd08549 71 YDC-VIGIGGGRSIDTGKYL--AYKLKIPFISVPTS------ASNDGIASPIVSLRIP--GVKKTfmadaPIAIIADTEI 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 490370239 170 LATLPPRELSSGLAEVI-KYGIILDKDFFIWLENNI 204
Cdd:cd08549 140 IKKSPRRLLSAGIGDLVsNITAVLDWKLAHKEKGEK 175
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
25-193 |
5.64e-04 |
|
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: 41.38 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 25 PETFLPLKKGQQVMIVTNVTLAPLYLDKVTNTLEQQGVLVDSVilpdgeQYKSLTVMNDVFTALLEKNHNRDTTLLALGG 104
Cdd:cd08173 16 GEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIV------DIATIEEAAEVEKVKKLIKESKADFIIGVGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370239 105 GVIGDLTgfAAASYQRGVRFIQVPTTL-----------LSQVDSSVGGKTavnHPlgknmigafyqPASVVIDLDCLATL 173
Cdd:cd08173 90 GKVIDVA--KYAAYKLNLPFISIPTSAshdgiaspfasIKGGDKPYSIKA---KA-----------PIAIIADTEIISKA 153
|
170 180
....*....|....*....|.
gi 490370239 174 PPRELSSGLAEVI-KYGIILD 193
Cdd:cd08173 154 PKRLLAAGCGDLIsNITAVKD 174
|
|
| |
