|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-338 |
0e+00 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 716.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 1 MFRHVHGKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGG 80
Cdd:PLN02834 94 LQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVALGGG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 81 VIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEV 160
Cdd:PLN02834 174 VIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 161 IKYGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYGEWLHG 240
Cdd:PLN02834 254 VKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTFGHAIETGPGYGEWLHG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 241 EAVAAGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPESMTVSMFKSIMAVDKKVADGLLRLILLKGPLGNCVFT 320
Cdd:PLN02834 334 EAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADGLLRLILLKGELGNCVFT 413
|
330
....*....|....*...
gi 30698194 321 GDYDREALDATLRAFSKS 338
Cdd:PLN02834 414 GDFDREALEETLRAFCKS 431
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
3-332 |
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: 511.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 3 RHVHGKRVLVVTNDRVAPLYLDKTIDALTRGNpnVTVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVI 82
Cdd:COG0337 31 ELLKGRRVLVVTDENVAPLYGERLRAALEAAG--FEVHLLVLPDGEASKTLETLERILDALLEAGLDRDDLVVALGGGVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 83 GDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIK 162
Cdd:COG0337 109 GDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVLIDLDFLKTLPERELRAGLAEVIK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 163 YGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYgEWLHGEA 242
Cdd:COG0337 189 YGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGLRALLNFGHTFGHAIEAATGY-RLLHGEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 243 VAAGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPEsMTVSMFKSIMAVDKKVADGLLRLILLKGpLGNCVFTGD 322
Cdd:COG0337 268 VAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAAMKRDKKVRGGKLRFVLLRG-IGKAVIVDD 345
|
330
....*....|
gi 30698194 323 YDREALDATL 332
Cdd:COG0337 346 VDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
7-332 |
1.97e-165 |
|
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: 464.61 E-value: 1.97e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 7 GKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVesVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMC 86
Cdd:cd08195 23 GSKVVIVTDENVAKLYGELLLKSLEAAGFKVEV--IVIPAGEKSKSLETVERIYDFLLEAGLDRDSLLIALGGGVVGDLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 87 GYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLI 166
Cdd:cd08195 101 GFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLKTLPEREFRSGLAEVIKYGLI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 167 RDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYgEWLHGEAVAAG 246
Cdd:cd08195 181 ADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGHAIESASGY-KLLHGEAVAIG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 247 TVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPEsMTVSMFKSIMAVDKKVADGLLRLILLKGPlGNCVFTGDYDRE 326
Cdd:cd08195 260 MVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGKIRFVLLKGI-GKAVIVDDVSEE 337
|
....*.
gi 30698194 327 ALDATL 332
Cdd:cd08195 338 EIREAL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
41-300 |
1.73e-155 |
|
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: 436.16 E-value: 1.73e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 41 SVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGI 120
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 121 NHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSCEN 200
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 201 KADVVSQDEKESGLRATLNLGHTFGHAIETGFGYGEWLHGEAVAAGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTT 280
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|
gi 30698194 281 PPEsMTVSMFKSIMAVDKKV 300
Cdd:pfam01761 241 LPD-LDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
6-332 |
7.58e-136 |
|
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: 389.68 E-value: 7.58e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 6 HGKRVLVVTNDRVAPLYLDKTIDALTrgNPNVTVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDM 85
Cdd:TIGR01357 19 EPSKLVIITDETVADLYGDKLLEALQ--ALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAGLDRSSTIIALGGGVVGDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 86 CGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGL 165
Cdd:TIGR01357 97 AGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 166 IRDAEFFEWQEKNIEALLARDP-AALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYGEWLHGEAVA 244
Cdd:TIGR01357 177 IADAELFDELESNDKLRLNLQElEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGHAIEAEAGYGKIPHGEAVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 245 AGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPESMTVSMFKSIMAVDKKVADGLLRLILLKGpLGNCVFTGDYD 324
Cdd:TIGR01357 257 IGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKIRFVLLEE-IGKAALAREVP 335
|
....*...
gi 30698194 325 REALDATL 332
Cdd:TIGR01357 336 DEMVLELL 343
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-338 |
0e+00 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 716.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 1 MFRHVHGKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGG 80
Cdd:PLN02834 94 LQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVALGGG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 81 VIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEV 160
Cdd:PLN02834 174 VIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 161 IKYGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYGEWLHG 240
Cdd:PLN02834 254 VKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTFGHAIETGPGYGEWLHG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 241 EAVAAGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPESMTVSMFKSIMAVDKKVADGLLRLILLKGPLGNCVFT 320
Cdd:PLN02834 334 EAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADGLLRLILLKGELGNCVFT 413
|
330
....*....|....*...
gi 30698194 321 GDYDREALDATLRAFSKS 338
Cdd:PLN02834 414 GDFDREALEETLRAFCKS 431
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
3-332 |
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: 511.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 3 RHVHGKRVLVVTNDRVAPLYLDKTIDALTRGNpnVTVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVI 82
Cdd:COG0337 31 ELLKGRRVLVVTDENVAPLYGERLRAALEAAG--FEVHLLVLPDGEASKTLETLERILDALLEAGLDRDDLVVALGGGVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 83 GDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIK 162
Cdd:COG0337 109 GDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVLIDLDFLKTLPERELRAGLAEVIK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 163 YGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYgEWLHGEA 242
Cdd:COG0337 189 YGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGLRALLNFGHTFGHAIEAATGY-RLLHGEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 243 VAAGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPEsMTVSMFKSIMAVDKKVADGLLRLILLKGpLGNCVFTGD 322
Cdd:COG0337 268 VAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAAMKRDKKVRGGKLRFVLLRG-IGKAVIVDD 345
|
330
....*....|
gi 30698194 323 YDREALDATL 332
Cdd:COG0337 346 VDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
7-332 |
1.97e-165 |
|
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: 464.61 E-value: 1.97e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 7 GKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVesVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMC 86
Cdd:cd08195 23 GSKVVIVTDENVAKLYGELLLKSLEAAGFKVEV--IVIPAGEKSKSLETVERIYDFLLEAGLDRDSLLIALGGGVVGDLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 87 GYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLI 166
Cdd:cd08195 101 GFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLKTLPEREFRSGLAEVIKYGLI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 167 RDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYgEWLHGEAVAAG 246
Cdd:cd08195 181 ADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGHAIESASGY-KLLHGEAVAIG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 247 TVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPEsMTVSMFKSIMAVDKKVADGLLRLILLKGPlGNCVFTGDYDRE 326
Cdd:cd08195 260 MVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGKIRFVLLKGI-GKAVIVDDVSEE 337
|
....*.
gi 30698194 327 ALDATL 332
Cdd:cd08195 338 EIREAL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
41-300 |
1.73e-155 |
|
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: 436.16 E-value: 1.73e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 41 SVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGI 120
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 121 NHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSCEN 200
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 201 KADVVSQDEKESGLRATLNLGHTFGHAIETGFGYGEWLHGEAVAAGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTT 280
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|
gi 30698194 281 PPEsMTVSMFKSIMAVDKKV 300
Cdd:pfam01761 241 LPD-LDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
6-332 |
7.58e-136 |
|
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: 389.68 E-value: 7.58e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 6 HGKRVLVVTNDRVAPLYLDKTIDALTrgNPNVTVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDM 85
Cdd:TIGR01357 19 EPSKLVIITDETVADLYGDKLLEALQ--ALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAGLDRSSTIIALGGGVVGDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 86 CGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGL 165
Cdd:TIGR01357 97 AGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 166 IRDAEFFEWQEKNIEALLARDP-AALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYGEWLHGEAVA 244
Cdd:TIGR01357 177 IADAELFDELESNDKLRLNLQElEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGHAIEAEAGYGKIPHGEAVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 245 AGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPESMTVSMFKSIMAVDKKVADGLLRLILLKGpLGNCVFTGDYD 324
Cdd:TIGR01357 257 IGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKIRFVLLEE-IGKAALAREVP 335
|
....*...
gi 30698194 325 REALDATL 332
Cdd:TIGR01357 336 DEMVLELL 343
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
6-323 |
3.43e-90 |
|
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: 273.69 E-value: 3.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 6 HGKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVesVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDM 85
Cdd:cd08197 22 KADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVEL--LVVPAGESNKTLSTLTELAERLIAAGITRRSVIIALGGGVVGNI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 86 CGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGL 165
Cdd:cd08197 100 AGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLKTLPPRQIRSGLCEAIKNAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 166 IRDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETgFGYGEWLHGEAVAA 245
Cdd:cd08197 180 IQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTVGHAIEL-LSGGELSHGEAVAI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 246 GTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPESMTVSMFKSIMAVDKK-----VADGLLRLILLKGpLGNCVFT 320
Cdd:cd08197 259 GMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPDGISVEAILEVIRYDNKrgyikADADTIRMVLLEK-LGKPANP 337
|
....
gi 30698194 321 -GDY 323
Cdd:cd08197 338 dGDY 341
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
9-317 |
6.66e-87 |
|
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: 264.65 E-value: 6.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 9 RVLVVTNDRVAPLYLDKTIDALTRGNPnvtVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGY 88
Cdd:cd08169 25 QCLIIVDSGVPDLIVNYLAEYFGYYLE---VHVFIIQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDVVGF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 89 AAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLIRD 168
Cdd:cd08169 102 AAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIAD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 169 AEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYgEWLHGEAVAAGTV 248
Cdd:cd08169 182 NDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTFGHALELASGY-KIPHGEAVAVGMA 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30698194 249 MAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPESMTVSMFKSIMAVDKKVADGLLRLILLKGpLGNC 317
Cdd:cd08169 261 YAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDSLYEYLESDKKSLYGNLGMILLSG-VGDG 328
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
7-332 |
2.30e-80 |
|
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: 248.60 E-value: 2.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 7 GKRVLVVTNDRVAPLYLDKtIDALTRGNpNVTVESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMC 86
Cdd:cd08199 26 GRRRLVVVDENVDRLYGAR-IRAYFAAH-GIEATILVLPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLLDVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 87 GYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLI 166
Cdd:cd08199 104 GFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 167 RDAEFFEWQEKNIEALLA----RDPAALAfAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYgEWLHGEA 242
Cdd:cd08199 184 KDAELFELLEEHGAALVEtrffQDEVADE-IIRRAIQGMLEELAPNLWEHDLERLVDFGHTFSPILEMAAAP-ELLHGEA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 243 VaagtvmAVDM------SYRLGWIDESIVKRVNKILVRAKLPTTPPESMTVSMFKSIMAVDKKvADGLLRLILLKGpLGN 316
Cdd:cd08199 262 V------AIDMalsavlAYRRGLLSEEELDRILRLMRRLGLPVWHPLCTPDLLWRALEDIVKH-RDGLQRLPLPKG-IGE 333
|
330
....*....|....*.
gi 30698194 317 CVFTGDYDREALDATL 332
Cdd:cd08199 334 CVFVNDVTEEELERAL 349
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
8-283 |
1.05e-62 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 204.36 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 8 KRVLVVTNDRVAPLY--LDKTIDALTRGNPNV---TVESVILPDGEKYK-DMDTLMKVFDKAIESRLDRRCTFVALGGGV 81
Cdd:PRK06203 43 KKVLVVIDSGVLRAHpdLLEQITAYFAAHADVlelVAEPLVVPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 82 IGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVI 161
Cdd:PRK06203 123 VLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 162 KYGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSCENKADVVSQ--DEKESGLRATLNLGHTFGHAIETGFGYgEWLH 239
Cdd:PRK06203 203 KVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAELHLEHIAGggDPFEFGSSRPLDFGHWSAHKLEQLTNY-ALRH 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 30698194 240 GEAVAAGtvMAVDM--SYRLGWIDESIVKRVNKILVRAKLPTTPPE 283
Cdd:PRK06203 282 GEAVAIG--IALDSlySYLLGLLSEAEAQRILALLRALGFPLYHPA 325
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
40-283 |
4.31e-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: 196.64 E-value: 4.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 40 ESVILPDGEKYK-DMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKT 118
Cdd:cd08198 68 PPLIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 119 GINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLIRDAEFFEWQEKNIEALLARDPAALAFAIKRSC 198
Cdd:cd08198 148 GINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 199 ENKAD--VVSQDEKESGLRATLNLGHTFGHAIETGFGYgEWLHGEAVAAGtvMAVDMSY--RLGWIDESIVKRVNKILVR 274
Cdd:cd08198 228 ELHLDhiAASGDPFETGSARPLDFGHWSAHKLEQLSGY-ALRHGEAVAIG--IALDSLYarLLGLLSREDFDRILALLQN 304
|
....*....
gi 30698194 275 AKLPTTPPE 283
Cdd:cd08198 305 LGLPLWHPL 313
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
39-333 |
4.26e-58 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 196.24 E-value: 4.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 39 VESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKT 118
Cdd:PRK14021 238 VSDIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKT 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 119 GINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLIRDAEFFEWQEKNIEALLARDPAA--------- 189
Cdd:PRK14021 318 GINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAFDGSTflgspledv 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 190 LAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETgFGYGEWLHGEAVAAGTVMAVDMSYRLGWIDESIVKRVN 269
Cdd:PRK14021 398 VAELIERTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEK-LEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHR 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30698194 270 KILVRAKLPTtppeSMTVSMFKSIMAV---DKKVADGLLRLILLKGpLGNCVFTGDYDREALDATLR 333
Cdd:PRK14021 477 SLLASLGLPT----SWNGGSFDDVLALmhrDKKARGNELRFVVLDE-IGHPVHLDNPPAEAVEEAFR 538
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
11-313 |
4.32e-46 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 163.15 E-value: 4.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 11 LVVTNDRVAPLYldktidalTRGNPNvtvESVILPDGEKYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAA 90
Cdd:PRK13951 189 LVFTTERVEKIY--------GRYLPE---NRLLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 91 ASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYGLI--RD 168
Cdd:PRK13951 258 STFKRGVGLSFYPTTLLAQVDASVGGKNAIDFAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILsgRG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 169 AEFFEwqekNIEALLARDPAALAFAIKRSCENKADVVSQDEKESGLRATLNLGHTFGHAIETGFGYGewlHGEAVAAGTV 248
Cdd:PRK13951 338 VELFD----EPEKIEKRNLRVLSEMVKISVEEKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGIE 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 249 MAVDMSYRLGWIDES----IVKRVnKILVRAKLPTTPPESMtvsmfKSIMAVDKKVADG-LLRLILLKGP 313
Cdd:PRK13951 411 KETMYLYRKGIVPKEtmrwIVEKV-KQIVPIPVPSVDVEKA-----RNLILNDKKILKGsRVRLPYVKEI 474
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
6-280 |
2.17e-27 |
|
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: 108.22 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 6 HGKRVLVVTNDRVAPLYLDKTIDALTRGnpnVTVESVILPDGEKykDMDTLMKVFDKAIESRLDrrcTFVALGGGVIGDM 85
Cdd:cd07766 21 GFDRALVVSDEGVVKGVGEKVADSLKKG---LAVAIFDFVGENP--TFEEVKNAVERARAAEAD---AVIAVGGGSTLDT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 86 CGYAAASYLRGVNFIQIPTTVMAqvDSSVGGKTGINHRLGKNL-IGAFYQPQCVLVDTDTLNTLPDREMASGLAEVIKYG 164
Cdd:cd07766 93 AKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNKqVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 165 LIRdaeffewqEKNIEAllardpaalafaikrSCENKADVVSqdekesglRATLNLGHTFGHAIETGFGYgewLHGEAVA 244
Cdd:cd07766 171 VEL--------EKVVEA---------------ATLAGMGLFE--------SPGLGLAHAIGHALTAFEGI---PHGEAVA 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 30698194 245 AGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTT 280
Cdd:cd07766 217 VGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTH 252
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
7-283 |
1.41e-13 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 70.69 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 7 GKRVLVVTNDRVAPLYLDKTIDALtrgNPNVTVESVILPDGekykDMDTLMKVFDKAIESRLDrrcTFVALGGGVIGDMC 86
Cdd:PRK00843 34 TGRALIVTGPTTKKIAGDRVEENL---EDAGDVEVVIVDEA----TMEEVEKVEEKAKDVNAG---FLIGVGGGKVIDVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 87 GYAaaSYLRGVNFIQIPTTvmAQVDSSVGGKTGINHrLGKNLIGAFYQPQCVLVDTDTLNTLPDREMASGLAEVI-KYGL 165
Cdd:PRK00843 104 KLA--AYRLGIPFISVPTA--ASHDGIASPRASIKG-GGKPVSVKAKPPLAVIADTEIIAKAPYRLLAAGCGDIIsNYTA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 166 IRDaeffeWQ----EKNIE-----ALLARDPAALAF----AIKRSCENKADVVSQDEKESGL--------RATLNLGHTF 224
Cdd:PRK00843 179 VKD-----WRlahrLRGEYyseyaAALSLMTAKMLIenadIIKPGLEESARLVVKALISSGVamsiagssRPASGSEHLF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30698194 225 GHAIETgFGYGEWLHGEAVAAGTVMavdMSYRLG--WidesivKRVNKILVRAKLPTTPPE 283
Cdd:PRK00843 254 SHALDR-LAPGPALHGEQCGVGTII---MMYLHGgdW------RKIRDALKKIGAPTTAKE 304
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
7-283 |
3.02e-13 |
|
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: 69.50 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 7 GKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVESVILpdgekYKDMDTLMKVFDKAIESRLDrrcTFVALGGGVIGDMC 86
Cdd:cd08173 25 GKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIAT-----IEEAAEVEKVKKLIKESKAD---FIIGVGGGKVIDVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 87 GYAAasYLRGVNFIQIPTTvmAQVD------SSVGGKTGINHRLGKnligafyQPQCVLVDTDTLNTLPDREMASGLAEV 160
Cdd:cd08173 97 KYAA--YKLNLPFISIPTS--ASHDgiaspfASIKGGDKPYSIKAK-------APIAIIADTEIISKAPKRLLAAGCGDL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 161 I-KYGLIRDaeffeWQekniealLARD---------PAALAFAIKRSCENKADVVSQDEKESG---LRATLNLG------ 221
Cdd:cd08173 166 IsNITAVKD-----WR-------LAHRlkgeyyseyAASLALMSAKLIIENADLIKPGLEEGVrtvVKALISSGvamsia 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698194 222 ----------HTFGHAIETgFGYGEWLHGEAVAAGTVMavdMSY--RLGWidesivKRVNKILVRAKLPTTPPE 283
Cdd:cd08173 234 gssrpasgseHLFSHALDK-LAPGPALHGEQCGVGTIM---MAYlhGGDW------KEIREALKKIGAPTTAKE 297
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
3-283 |
1.35e-12 |
|
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: 67.59 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 3 RHVHGKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVES--VILPDGEKYKDMDTLmkvfdkaiesrldrrctfVALGGG 80
Cdd:cd08549 19 KKLNLKRVLIITGKNTKAKYCRFFYDQLKTVCDIVYYDNidNLEDELKKYTFYDCV------------------IGIGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 81 VIGDMCGYAaaSYLRGVNFIQIPTTvmAQVD--SSVGGKTGINHRLGKNLIGAfyqPQCVLVDTDTLNTLPDREMASGLA 158
Cdd:cd08549 81 RSIDTGKYL--AYKLKIPFISVPTS--ASNDgiASPIVSLRIPGVKKTFMADA---PIAIIADTEIIKKSPRRLLSAGIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 159 EVI-KYGLIRDAEFFEWQEKNIEALLArdpAALAFAIKRSCENKADVVSQDEK----------ESGLrATLNLG------ 221
Cdd:cd08549 154 DLVsNITAVLDWKLAHKEKGEKYSEFA---AILSKTSAKELVSYVLKASDLEEyhrvlvkalvGSGI-AMAIAGssrpas 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30698194 222 ---HTFGHAIETGF---GYGEWLHGEAVAAGTVMAVDMSYRLGWIDESIVKRVNKILVRAKLPTTPPE 283
Cdd:cd08549 230 gseHLFSHALDKLKeeyLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAPTTAKQ 297
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
7-244 |
2.05e-12 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 66.17 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 7 GKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVESVILPDGekykDMDTLMKVFDKAIESRLDrrcTFVALGGGVIGDMC 86
Cdd:pfam13685 19 FRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGNA----DMETAEKLVGALRERDAD---AVVGVGGGTVIDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 87 GYAAasYLRGVNFIQIPTTvmAQVDSSVGGKTGINHRLGKNLIGAfYQPQCVLVDTDTLNTLPDREMASGLAEVI-KYGL 165
Cdd:pfam13685 92 KYAA--FKLGKPFISVPTA--ASNDGFASPGASLTVDGKKRSIPA-AAPFGVIADTDVIAAAPRRLLASGVGDLLaKITA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 166 IRDaeffeWQEKNIEALlaRDPAALAFAikRSCENKADVVSQDEKESGLRATLNLG----------------HTFGHAIE 229
Cdd:pfam13685 167 VAD-----WELAHAEEV--AAPLALLSA--AMVMNFADRPLRDPGDIEALAELLSAlamggagssrpasgseHLISHALD 237
|
250
....*....|....*
gi 30698194 230 TGFGyGEWLHGEAVA 244
Cdd:pfam13685 238 MIAP-KQALHGEQVG 251
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
6-283 |
4.06e-11 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 63.26 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 6 HGKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVESVilpDGEKykDMDTLMKVFDKAIESRLDrrcTFVALGGGVIGDM 85
Cdd:COG0371 26 LGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVF---GGEC--SEEEIERLAEEAKEQGAD---VIIGVGGGKALDT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 86 CGYAAasYLRGVNFIQIPTTvmAQVDS-----SVggktgINHRLGKnLIGAFYQPQC---VLVDTDTLNTLPDREMASGL 157
Cdd:COG0371 98 AKAVA--YRLGLPVVSVPTI--ASTDApasplSV-----IYTEDGA-FDGYSFLAKNpdlVLVDTDIIAKAPVRLLAAGI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 158 AEVIkyglirdAEFFE---WQEKNiEALLARDPAALAFAIKRSCEN---------KADVVSQDEKE------------SG 213
Cdd:COG0371 168 GDAL-------AKWYEardWSLAH-RDLAGEYYTEAAVALARLCAEtlleygeaaIKAVEAGVVTPalervveanlllSG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30698194 214 L-------RATLNLGHTFGHAIETGFGYGEWLHGEAVAAGTVMavdMSYRLGWIDEsiVKRVNKILVRAKLPTTPPE 283
Cdd:COG0371 240 LamgigssRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLV---QLVLEGRPEE--IEELLDFLRSVGLPTTLAD 311
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
1-281 |
7.52e-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: 56.36 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 1 MFRHVHGKRVLVVTNDRVAPLYLDKTIDALTRGNpnVTVESVILPD-GEKYKDMDTLMKVFDkaiesRLDRRCTF-VALG 78
Cdd:cd08175 18 LKELFGGKKVLVVADENTYAAAGEEVEAALEEAG--VTVCLLIFPGeGDLIADEAAVGKVLL-----ELEKDTDLiIAVG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 79 GGVIGDMCGYaaASYLRGVNFIQIPTTvmAQVD---SSV------GGKTGINHRLgknligafyqPQCVLVDTDTLNTLP 149
Cdd:cd08175 91 SGTINDLTKY--AAYKLGIPYISVPTA--PSMDgytSSGapiivdGVKKTFPAHA----------PKAIFADLDVLANAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 150 DREMASGLAEVI-KY----------------------GLIRDAEffewQE--KNIEALLARDPAA---LAFAIkrscenk 201
Cdd:cd08175 157 QRMIAAGFGDLLgKYtaladwklshllggeyycpevaDLVQEAL----EKclDNAEGIAARDPEAieaLMEAL------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 202 advvsqdeKESGLrATLNLG---------HTFGHAIET---GFGYGEWLHGEAVAAGTVMAVDMsyrlgWIDESI--VKR 267
Cdd:cd08175 226 --------ILSGL-AMQLVGnsrpasgaeHHLSHYWEMeflRLGKPPVLHGEKVGVGTLLIAAL-----YILEQLppPEE 291
|
330
....*....|....
gi 30698194 268 VNKILVRAKLPTTP 281
Cdd:cd08175 292 LRELLRKAGAPTTP 305
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
3-298 |
7.93e-08 |
|
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: 53.29 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 3 RHVHGKRVLVVTNDRVAPLYLDKTIDALTRGNPNVTVESVilpdgekykDMDTLMKVFDKAIesRLDRRCTFVALGGGVI 82
Cdd:cd08174 21 RNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEEN---------TDNSAEELAEKAF--SLPKVDAIVGIGGGKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 83 GDMCGYAAasYLRGVNFIQIPTTV----MAqvdSSV------GGKTGINHRLgknligafyqPQCVLVDTDTLNTLPDRE 152
Cdd:cd08174 90 LDVAKYAA--FLSKLPFISVPTSLsndgIA---SPVavlkvdGKRKSLGAKM----------PYGVIVDLDVIKSAPRRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 153 MASGLAEVI-KYGLIRDaeffeWQ---EKNIE------ALLARDpAALAFaikRSCENKAdvvsqDEKESGLRATLN--- 219
Cdd:cd08174 155 ILAGIGDLIsNITALYD-----WKlaeEKGGEpvddfaYLLSRT-AADSL---LNTPGKD-----IKDDEFLKELAEslv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 220 LG-----------------HTFGHAIETGFGyGEWLHGEAVAAGTVMavdMSYrlgwIDESIVKRVNKILVRAKLPTTPP 282
Cdd:cd08174 221 LSgiameiagssrpasgseHLISHALDKLFP-GPALHGIQVGLGTYF---MSF----LQGQRYEEIRDVLKRTGFPLNPS 292
|
330
....*....|....*..
gi 30698194 283 ES-MTVSMFksIMAVDK 298
Cdd:cd08174 293 DLgLTKEEF--IEAVKL 307
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
6-156 |
7.44e-06 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 47.21 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 6 HGKRVLVVTNDRVAPL-YLDKTIDALTRGNPNVTVESVILPDgekyKDMDTLMKVFDKAIESRLDrrcTFVALGGG---- 80
Cdd:pfam00465 21 LGARALIVTDPGSLKSgLLDKVLASLEEAGIEVVVFDGVEPE----PTLEEVDEAAALAREAGAD---VIIAVGGGsvid 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 81 ---VIGDMCGY--AAASYLRG-------VNFIQIPTTV-----MAQV----DSSVGGKTGINHRlgkNLIgafyqPQCVL 139
Cdd:pfam00465 94 takAIALLLTNpgDVWDYLGGkpltkpaLPLIAIPTTAgtgseVTPLavitDTETGEKLGIFSP---KLL-----PDLAI 165
|
170
....*....|....*..
gi 30698194 140 VDTDTLNTLPDREMASG 156
Cdd:pfam00465 166 LDPELTLTLPPRLTAAT 182
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
3-105 |
2.48e-03 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 39.40 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 3 RHVHGKRVLVVTNDRVAPL-YLDKTIDALTRGNPnVTVESVILPDgekyKDMDTLMKVFDKAIESRLDrrcTFVALGGGV 81
Cdd:cd08180 18 KELKGKRVFIVTDPFMVKSgMVDKVTDELDKSNE-VEIFSDVVPD----PSIEVVAKGLAKILEFKPD---TIIALGGGS 89
|
90 100 110
....*....|....*....|....*....|
gi 30698194 82 IGDMCGYAAASYLRGVN------FIQIPTT 105
Cdd:cd08180 90 AIDAAKAIIYFALKQKGnikkplFIAIPTT 119
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
7-155 |
2.82e-03 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 39.07 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 7 GKRVLVVTNDRVAPL-YLDKTIDALTRGNPNVTV--ESVILPDGEKYKDmdtlmkVFDKAIESRLDrrcTFVALGGG-VI 82
Cdd:cd08190 23 AKKVLVVTDPGLAKLgLVERVLESLEKAGIEVVVydGVRVEPTDESFEE------AIEFAKEGDFD---AFVAVGGGsVI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698194 83 gDMCGYAA--ASYLRG----VN---------------FIQIPTTV--------MAQVD-SSVGGKTGINHRlgknligaF 132
Cdd:cd08190 94 -DTAKAANlyATHPGDfldyVNapigkgkpvpgplkpLIAIPTTAgtgsettgVAIFDlEELKVKTGISSR--------Y 164
|
170 180
....*....|....*....|...
gi 30698194 133 YQPQCVLVDTDTLNTLPDREMAS 155
Cdd:cd08190 165 LRPTLAIVDPLLTLTLPPRVTAS 187
|
|
| |
