|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-355 |
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: 571.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 1 MQQIRVDLGERSYPIFIGQGLLAQ-SDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPAA-QVFAHILPDGEQYKTLA 78
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 79 QLESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQ 158
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 159 PQLVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGV 238
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 239 RALLNLGHTFGHAIEAEMGYgNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPEsMDFESFIKHM 318
Cdd:COG0337 241 RALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 647613975 319 RRDKKVLAGQIRLVLPTDMGQAGIFAQVPESLLEQVI 355
Cdd:COG0337 319 KRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-355 |
0e+00 |
|
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: 506.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 12 SYPIFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPA-AQVFAHILPDGEQYKTLAQLESVFTALLEH 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAgFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 91 NCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDTLCLK 170
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 171 TLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRALLNLGHTFGH 250
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 251 AIEAEMGYGnWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPEsMDFESFIKHMRRDKKVLAGQIR 330
Cdd:cd08195 241 AIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGKIR 318
|
330 340
....*....|....*....|....*
gi 647613975 331 LVLPTDMGQAGIFAQVPESLLEQVI 355
Cdd:cd08195 319 FVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
4-333 |
6.09e-170 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 480.42 E-value: 6.09e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 4 IRVDLGERSYPIFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLL---PAAQVFAHILPDGEQYKTLAQL 80
Cdd:PLN02834 70 VKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 81 ESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQ 160
Cdd:PLN02834 150 MKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 161 LVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRA 240
Cdd:PLN02834 230 CVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 241 LLNLGHTFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPESMDFESFIKHMRR 320
Cdd:PLN02834 310 TLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAV 389
|
330
....*....|...
gi 647613975 321 DKKVLAGQIRLVL 333
Cdd:PLN02834 390 DKKVADGLLRLIL 402
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
67-325 |
5.20e-161 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 450.80 E-value: 5.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 67 ILPDGEQYKTLAQLESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNH 146
Cdd:pfam01761 3 VIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGINH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 147 PLGKNMIGAFYQPQLVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKA 226
Cdd:pfam01761 83 PLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEVKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 227 EVVAEDETEQGVRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAP 306
Cdd:pfam01761 163 DVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTSLP 242
|
250
....*....|....*....
gi 647613975 307 EsMDFESFIKHMRRDKKVL 325
Cdd:pfam01761 243 D-LDVEQLLAAMARDKKVR 260
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-356 |
2.21e-152 |
|
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: 432.44 E-value: 2.21e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 13 YPIFIGQGLLAQ-SDCLTasvSGKKVLIVSNDTVAPLY----LQSLQRLllpAAQVFAHILPDGEQYKTLAQLESVFTAL 87
Cdd:TIGR01357 1 YPVHVGEGLLDQlVEELA---EPSKLVIITDETVADLYgdklLEALQAL---GYNVLKLTVPDGEESKSLETVQRLYDQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 88 LEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDTL 167
Cdd:TIGR01357 75 LEAGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 168 CLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVES-LKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRALLNLGH 246
Cdd:TIGR01357 155 FLKTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 247 TFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPESMDFESFIKHMRRDKKVLA 326
Cdd:TIGR01357 235 TIGHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSG 314
|
330 340 350
....*....|....*....|....*....|
gi 647613975 327 GQIRLVLPTDMGQAGIFAQVPESLLEQVIC 356
Cdd:TIGR01357 315 GKIRFVLLEEIGKAALAREVPDEMVLELLD 344
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-355 |
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: 571.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 1 MQQIRVDLGERSYPIFIGQGLLAQ-SDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPAA-QVFAHILPDGEQYKTLA 78
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 79 QLESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQ 158
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 159 PQLVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGV 238
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 239 RALLNLGHTFGHAIEAEMGYgNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPEsMDFESFIKHM 318
Cdd:COG0337 241 RALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 647613975 319 RRDKKVLAGQIRLVLPTDMGQAGIFAQVPESLLEQVI 355
Cdd:COG0337 319 KRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-355 |
0e+00 |
|
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: 506.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 12 SYPIFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPA-AQVFAHILPDGEQYKTLAQLESVFTALLEH 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAgFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 91 NCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDTLCLK 170
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 171 TLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRALLNLGHTFGH 250
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 251 AIEAEMGYGnWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPEsMDFESFIKHMRRDKKVLAGQIR 330
Cdd:cd08195 241 AIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGKIR 318
|
330 340
....*....|....*....|....*
gi 647613975 331 LVLPTDMGQAGIFAQVPESLLEQVI 355
Cdd:cd08195 319 FVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
4-333 |
6.09e-170 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 480.42 E-value: 6.09e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 4 IRVDLGERSYPIFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLL---PAAQVFAHILPDGEQYKTLAQL 80
Cdd:PLN02834 70 VKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 81 ESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQ 160
Cdd:PLN02834 150 MKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 161 LVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRA 240
Cdd:PLN02834 230 CVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 241 LLNLGHTFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPESMDFESFIKHMRR 320
Cdd:PLN02834 310 TLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAV 389
|
330
....*....|...
gi 647613975 321 DKKVLAGQIRLVL 333
Cdd:PLN02834 390 DKKVADGLLRLIL 402
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
67-325 |
5.20e-161 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 450.80 E-value: 5.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 67 ILPDGEQYKTLAQLESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNH 146
Cdd:pfam01761 3 VIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGINH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 147 PLGKNMIGAFYQPQLVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKA 226
Cdd:pfam01761 83 PLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEVKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 227 EVVAEDETEQGVRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAP 306
Cdd:pfam01761 163 DVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTSLP 242
|
250
....*....|....*....
gi 647613975 307 EsMDFESFIKHMRRDKKVL 325
Cdd:pfam01761 243 D-LDVEQLLAAMARDKKVR 260
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-356 |
2.21e-152 |
|
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: 432.44 E-value: 2.21e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 13 YPIFIGQGLLAQ-SDCLTasvSGKKVLIVSNDTVAPLY----LQSLQRLllpAAQVFAHILPDGEQYKTLAQLESVFTAL 87
Cdd:TIGR01357 1 YPVHVGEGLLDQlVEELA---EPSKLVIITDETVADLYgdklLEALQAL---GYNVLKLTVPDGEESKSLETVQRLYDQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 88 LEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDTL 167
Cdd:TIGR01357 75 LEAGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 168 CLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVES-LKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRALLNLGH 246
Cdd:TIGR01357 155 FLKTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 247 TFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPESMDFESFIKHMRRDKKVLA 326
Cdd:TIGR01357 235 TIGHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSG 314
|
330 340 350
....*....|....*....|....*....|
gi 647613975 327 GQIRLVLPTDMGQAGIFAQVPESLLEQVIC 356
Cdd:TIGR01357 315 GKIRFVLLEEIGKAALAREVPDEMVLELLD 344
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
12-338 |
1.52e-95 |
|
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: 287.38 E-value: 1.52e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 12 SYPIFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPAAQVFAHILPDGEQYKTLAQLESVFTALLEHN 91
Cdd:cd08169 1 EYPVFFGEGVFESVNSYIPRDAFDQCLIIVDSGVPDLIVNYLAEYFGYYLEVHVFIIQGGEAYKTFQTVVEELERAAALH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 92 CGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDTLCLKT 171
Cdd:cd08169 81 LNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 172 LPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRALLNLGHTFGHA 251
Cdd:cd08169 161 LPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTFGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 252 IEAEMGYGnWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPESMDFESFIKHMRRDKKVLAGQIRL 331
Cdd:cd08169 241 LELASGYK-IPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDSLYEYLESDKKSLYGNLGM 319
|
....*..
gi 647613975 332 VLPTDMG 338
Cdd:cd08169 320 ILLSGVG 326
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-355 |
1.24e-91 |
|
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: 278.31 E-value: 1.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 12 SYPIFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPA-AQVFAHILPDGEQYKTLAQLESVFTALLEH 90
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAgIPVELLVVPAGESNKTLSTLTELAERLIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 91 NCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDTLCLK 170
Cdd:cd08197 81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 171 TLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAEDETEQGVRALLNLGHTFGH 250
Cdd:cd08197 161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTVGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 251 AIEAEMGyGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPESMDFESFIKHMRRDKK-----VL 325
Cdd:cd08197 241 AIELLSG-GELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPDGISVEAILEVIRYDNKrgyikAD 319
|
330 340 350
....*....|....*....|....*....|....*
gi 647613975 326 AGQIRLVLPTDMGQ----AGIF-AQVPESLLEQVI 355
Cdd:cd08197 320 ADTIRMVLLEKLGKpanpDGDYlTPVPEEIVKEAL 354
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
12-352 |
8.08e-69 |
|
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: 219.32 E-value: 8.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 12 SYPIFIGQGLLAQSDCLTA---SVSGKKVLIVSNDTVAPLYLQSLQRLLlPAAQVFAHI--LPDGEQYKTLAQLESVFTA 86
Cdd:cd08199 1 SYDVVLVDDLFDPENPTLAdayGRPGRRRLVVVDENVDRLYGARIRAYF-AAHGIEATIlvLPGGEANKTMETVLRIVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 87 LLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDT 166
Cdd:cd08199 80 LDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 167 LCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYA---IRRCCEIKAEVVAEDETEQGVRALLN 243
Cdd:cd08199 160 SFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVETRFFQDEVAdeiIRRAIQGMLEELAPNLWEHDLERLVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 244 LGHTFGHAIEAEMGYGnWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPE-SMDF-----ESFIKH 317
Cdd:cd08199 240 FGHTFSPILEMAAAPE-LLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHPLcTPDLlwralEDIVKH 318
|
330 340 350
....*....|....*....|....*....|....*
gi 647613975 318 mrRDkkvlaGQIRLVLPTDMGQAGIFAQVPESLLE 352
Cdd:cd08199 319 --RD-----GLQRLPLPKGIGECVFVNDVTEEELE 346
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
2-355 |
4.16e-59 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 195.50 E-value: 4.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 2 QQIRVDLgerSYPIFIGQGLLAQSDCLTASV-------SGKKVLIVSNDTVA----------PLYLQSLQRLLLPAAQVf 64
Cdd:PRK06203 6 QSFAVTF---EYPVYFTRDLFSPENPLLAEVlaadgegKPKKVLVVIDSGVLrahpdlleqiTAYFAAHADVLELVAEP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 65 aHILPDGEQYKT-LAQLESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTA 143
Cdd:PRK06203 82 -LVVPGGEAAKNdPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 144 VNHPLGKNMIGAFYQPQLVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCE 223
Cdd:PRK06203 161 INAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 224 IKAEVVAE--DETEQGVRALLNLGHTFGHAIEAEMGYgNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDL 301
Cdd:PRK06203 241 LHLEHIAGggDPFEFGSSRPLDFGHWSAHKLEQLTNY-ALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGF 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647613975 302 PVTAPE-SMD----------FESFIKHmrrdkkvLAGQIRLVLPTDMGQAGIFAQVPESLLEQVI 355
Cdd:PRK06203 320 PLYHPAlATRdskgrellkgLEEFREH-------LGGRLTITLLTGIGRGIEVHEIDLDLLRQAI 377
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
33-307 |
1.61e-57 |
|
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: 190.86 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 33 SGKKVLIVSNDTVA---PLYLQSLQR--------LLLPAAqvfAHILPDGEQYK-TLAQLESVFTALLEHNCGRDVVLVA 100
Cdd:cd08198 29 RRHRVLFVIDSGVAaahPALVKQIERyfqahpdrLELVAP---PLIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 101 LGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLIDTLCLKTLPVREFAAG 180
Cdd:cd08198 106 IGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 181 MAEVIKYGIIWDADFFLWLENNVESLKSQQPEALAYAIRRCCEIKAEVVAE--DETEQGVRALLNLGHTFGHAIEAEMGY 258
Cdd:cd08198 186 IAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAELHLDHIAAsgDPFETGSARPLDFGHWSAHKLEQLSGY 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 647613975 259 GnWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPVTAPE 307
Cdd:cd08198 266 A-LRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLPLWHPL 313
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
13-339 |
1.64e-57 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 195.47 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 13 YPIFIGQGLLAQsdclTASVSGKKVLivsndTVAPLYLQSLQR-------LLLPAA-QVFAHILPDGEQYKTLAQLESVF 84
Cdd:PRK14021 189 YDVRIGEGAMNH----LPQVLGPKPV-----KVALIHTQPVQRhsdrartLLRQGGyEVSDIVIPDAEAGKTIEVANGIW 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 85 TALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQLVLI 164
Cdd:PRK14021 260 QRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 165 DTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWLENNVESLK---------SQQPEALAYAIRRCCEIKAEVVAEDETE 235
Cdd:PRK14021 340 DTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRafdgstflgSPLEDVVAELIERTVKVKAYHVSSDLKE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 236 QGVRALLNLGHTFGHAIEaEMGYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPvTAPESMDFESFI 315
Cdd:PRK14021 420 AGLREFLNYGHTLGHAIE-KLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLASLGLP-TSWNGGSFDDVL 497
|
330 340
....*....|....*....|....
gi 647613975 316 KHMRRDKKVLAGQIRLVLPTDMGQ 339
Cdd:PRK14021 498 ALMHRDKKARGNELRFVVLDEIGH 521
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
67-334 |
1.81e-47 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 167.39 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 67 ILPDGEQYKTLAQLESVFTALLEHNCGRDVVLVALGGGVIGDMVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNH 146
Cdd:PRK13951 210 LFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAIDF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 147 PLGKNMIGAFYQPQLVLIDTLCLKTLPVREFAAGMAEVIKYGIIWDADFFLWleNNVESLKSQQPEALAYAIRRCCEIKA 226
Cdd:PRK13951 290 AGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVELF--DEPEKIEKRNLRVLSEMVKISVEEKA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 227 EVVAEDETEQGVRALLNLGHTFGHAIEAEMGYGnwlHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFdLPVTAP 306
Cdd:PRK13951 368 RIVMEDPYDMGLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQI-VPIPVP 443
|
250 260
....*....|....*....|....*...
gi 647613975 307 eSMDFESFIKHMRRDKKVLAGQiRLVLP 334
Cdd:PRK13951 444 -SVDVEKARNLILNDKKILKGS-RVRLP 469
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
34-318 |
1.56e-24 |
|
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: 100.90 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 34 GKKVLIVSNDTVAPLYLQ----SLQRLLLPAAQVFAHILPDGEQYKTLAQLEsvftalleHNCGRDVVlVALGGGVIGDM 109
Cdd:cd07766 22 FDRALVVSDEGVVKGVGEkvadSLKKGLAVAIFDFVGENPTFEEVKNAVERA--------RAAEADAV-IAVGGGSTLDT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 110 VGFAAACYQRGVDFIQIPTTLLSqvDSSVGGKTAVNHPLGKN-MIGAFYQPQLVLIDTLCLKTLPVREFAAGMAEVIKYG 188
Cdd:cd07766 93 AKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 189 IIwdadfflwLENNVESlksqqpealayairrCCEIKAEVVaedeteqgVRALLNLGHTFGHAIEAEMGYgnwLHGEAVA 268
Cdd:cd07766 171 VE--------LEKVVEA---------------ATLAGMGLF--------ESPGLGLAHAIGHALTAFEGI---PHGEAVA 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 647613975 269 AGTVLAAQTAKAMELIDESILRRITELLQVFDLPVT----APESMDFESFIKHM 318
Cdd:cd07766 217 VGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHladlGVSKEDIPKLAEKA 270
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-316 |
1.19e-11 |
|
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: 64.88 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 15 IFIGQGLLAQ-SDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLlpAAQVFAHILPDGEQYKTLAQLESVFTALLEHNcg 93
Cdd:cd08173 5 VVVGHGAINKiGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLL--ESSGVEVVIVDIATIEEAAEVEKVKKLIKESK-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 94 rDVVLVALGGGVIGDMVGFAAacYQRGVDFIQIPTTL-----------LSQVDSSVGGKTavnHPlgknmigafyqPQLV 162
Cdd:cd08173 81 -ADFIIGVGGGKVIDVAKYAA--YKLNLPFISIPTSAshdgiaspfasIKGGDKPYSIKA---KA-----------PIAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 163 LIDTLCLKTLPVREFAAGMAEVI-KYGIIWDADFFLWLENnvESLkSQQPEALAY-----AIRRCCEIKAEvvAEDETEQ 236
Cdd:cd08173 144 IADTEIISKAPKRLLAAGCGDLIsNITAVKDWRLAHRLKG--EYY-SEYAASLALmsaklIIENADLIKPG--LEEGVRT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 237 GVRALLNLG----------------HTFGHAIEAeMGYGNWLHGEAVAAGTVLAA--QTAKamelidesiLRRITELLQV 298
Cdd:cd08173 219 VVKALISSGvamsiagssrpasgseHLFSHALDK-LAPGPALHGEQCGVGTIMMAylHGGD---------WKEIREALKK 288
|
330
....*....|....*....
gi 647613975 299 FDLPVTAPE-SMDFESFIK 316
Cdd:cd08173 289 IGAPTTAKElGLDKEIIIE 307
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
15-307 |
1.07e-09 |
|
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: 59.02 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 15 IFIGQGLLAQSDCLTASVsGKKVLIVSNDTVAPLYLQSLQRLLLPAAQVFAHILPDGEQykTLAQLESVFTALLEHNCGr 94
Cdd:COG0371 9 YVQGEGALDELGEYLADL-GKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGEC--SEEEIERLAEEAKEQGAD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 95 dvVLVALGGGVIGDMVGFAAacYQRGVDFIQIPTTLlsqvdSSVGGKTAVN---HPLGKnMIGAFYQPQ---LVLIDTLC 168
Cdd:COG0371 85 --VIIGVGGGKALDTAKAVA--YRLGLPVVSVPTIA-----STDAPASPLSviyTEDGA-FDGYSFLAKnpdLVLVDTDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 169 LKTLPVREFAAGMAEVI-KYgiiWDADFflWLENNvESLKSQQPEALAYAIRRCC---------EIKAEVVAEDETEQGV 238
Cdd:COG0371 155 IAKAPVRLLAAGIGDALaKW---YEARD--WSLAH-RDLAGEYYTEAAVALARLCaetlleygeAAIKAVEAGVVTPALE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 239 RALL-----------------NLG--HTFGHAIEAEMGYGNWLHGEAVAAGTVLAAqtakAMELIDESIlRRITELLQVF 299
Cdd:COG0371 229 RVVEanlllsglamgigssrpGSGaaHAIHNGLTALPETHHALHGEKVAFGTLVQL----VLEGRPEEI-EELLDFLRSV 303
|
....*...
gi 647613975 300 DLPVTAPE 307
Cdd:COG0371 304 GLPTTLAD 311
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
15-312 |
9.47e-09 |
|
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: 56.03 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 15 IFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPAAQVfahilpdgEQYKTLAQLESVftalLEHNCGR 94
Cdd:cd08549 4 TIVGDGAINKIEEILKKLNLKRVLIITGKNTKAKYCRFFYDQLKTVCDI--------VYYDNIDNLEDE----LKKYTFY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 95 DVVlVALGGGVIGDMVGFAAacYQRGVDFIQIPTTllsqvdSSVGGKTAVNHPLGKNmiGAFYQ-----PQLVLIDTLCL 169
Cdd:cd08549 72 DCV-IGIGGGRSIDTGKYLA--YKLKIPFISVPTS------ASNDGIASPIVSLRIP--GVKKTfmadaPIAIIADTEII 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 170 KTLPVREFAAGMAEVI-KYGIIWDADFFLWLENNVESLKSQQpeaLAYAIRRCCEIKAEVVAEDetEQGVR----ALLNL 244
Cdd:cd08549 141 KKSPRRLLSAGIGDLVsNITAVLDWKLAHKEKGEKYSEFAAI---LSKTSAKELVSYVLKASDL--EEYHRvlvkALVGS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 245 G----------------HTFGHAIEAEM---GYGNWLHGEAVAAGTVLAAQTAKAMELIDESILRRITELLQVFDLPvTA 305
Cdd:cd08549 216 GiamaiagssrpasgseHLFSHALDKLKeeyLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAP-TT 294
|
....*..
gi 647613975 306 PESMDFE 312
Cdd:cd08549 295 AKQLGID 301
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
15-275 |
2.98e-08 |
|
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: 54.82 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 15 IFIGQGLLAQ-SDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPAAQVFAHILPDGEQ-----YKTLAQLesvftalL 88
Cdd:cd08175 4 IVIGEGALKKlPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEGdliadEAAVGKV-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 89 EHNCGRDVVLVALGGGVIGDMVGFAAacYQRGVDFIQIPTTllsqvdSSVGGKTAVNHPLgknMIGAFYQ------PQLV 162
Cdd:cd08175 77 LELEKDTDLIIAVGSGTINDLTKYAA--YKLGIPYISVPTA------PSMDGYTSSGAPI---IVDGVKKtfpahaPKAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 163 LIDTLCLKTLPVREFAAGMAEVI-KY--GIIWD-ADFFlwlenNVESLkSQQPEAL-AYAIRRCCEIKAEVVA--EDETE 235
Cdd:cd08175 146 FADLDVLANAPQRMIAAGFGDLLgKYtaLADWKlSHLL-----GGEYY-CPEVADLvQEALEKCLDNAEGIAArdPEAIE 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 647613975 236 QGVRALLNLG----------------HTFGHAIE---AEMGYGNWLHGEAVAAGTVLAA 275
Cdd:cd08175 220 ALMEALILSGlamqlvgnsrpasgaeHHLSHYWEmefLRLGKPPVLHGEKVGVGTLLIA 278
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
15-307 |
4.80e-08 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 54.13 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 15 IFIGQGLLAQ-SDCLTASVSGKKVLIVSNDTVAPLYLQSLQRLLLPAAQVFAHILPDGeqykTLAQLESVFTALLEHNCG 93
Cdd:PRK00843 14 VVVGHGVLDDiGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGDVEVVIVDEA----TMEEVEKVEEKAKDVNAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 94 rdvVLVALGGGVIGDMVGFAAacYQRGVDFIQIPTT-----LLSQVDSSVGGKTavNHPLGKNMigafyqPQLVLIDTLC 168
Cdd:PRK00843 90 ---FLIGVGGGKVIDVAKLAA--YRLGIPFISVPTAashdgIASPRASIKGGGK--PVSVKAKP------PLAVIADTEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 169 LKTLPVREFAAGMAEVI-KYGIIWDadfflW-LENnveSLK----SQQPEALAyairrccEIKAEVVAED------ETEQ 236
Cdd:PRK00843 157 IAKAPYRLLAAGCGDIIsNYTAVKD-----WrLAH---RLRgeyySEYAAALS-------LMTAKMLIENadiikpGLEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 237 GVR----ALLNLG----------------HTFGHAIEAeMGYGNWLHGEAVAAGTVLaaqtakaMELIDESILRRITELL 296
Cdd:PRK00843 222 SARlvvkALISSGvamsiagssrpasgseHLFSHALDR-LAPGPALHGEQCGVGTII-------MMYLHGGDWRKIRDAL 293
|
330
....*....|.
gi 647613975 297 QVFDLPVTAPE 307
Cdd:PRK00843 294 KKIGAPTTAKE 304
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
15-354 |
1.28e-05 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 46.44 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 15 IFIGQGLLAQSDCLTASvSGKKVLIVS-NDTVAPLYLQSLQRLLLPA---AQVFAHILPDgeqyKTLAQLESVFTALLEH 90
Cdd:pfam00465 4 IVFGAGALAELGEELKR-LGARALIVTdPGSLKSGLLDKVLASLEEAgieVVVFDGVEPE----PTLEEVDEAAALAREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 91 NCgrDVVlVALGGG-------VIGDMVG---------FAAACYQRGVDFIQIPTTL-----LSQV----DSSVGGKTAVN 145
Cdd:pfam00465 79 GA--DVI-IAVGGGsvidtakAIALLLTnpgdvwdylGGKPLTKPALPLIAIPTTAgtgseVTPLavitDTETGEKLGIF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 146 HPlgkNMIgafyqPQLVLIDTLCLKTLPVREFAAGMAevikygiiwDAdFFLWLENNVESLKSQQPEALA-YAIRRCCEI 224
Cdd:pfam00465 156 SP---KLL-----PDLAILDPELTLTLPPRLTAATGM---------DA-LAHAVEAYVSKGANPLTDALAlEAIRLIAEN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 225 KAEVVAEDETEQGVRALLN---------------LGHTFGHAIeaemgyGNWLHgeaVAAGTVLAAQTAKAMELIDESIL 289
Cdd:pfam00465 218 LPRAVADGEDLEARENMLLastlaglafsnaglgAAHALAHAL------GGRYG---IPHGLANAILLPYVLRFNAPAAP 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647613975 290 RRITELLQVFDLPVTAPESMDFESFIKHMRRDkkvlagqirLVLPTDMGQAGIfaqvPESLLEQV 354
Cdd:pfam00465 289 EKLAQLARALGEDSDEEAAEEAIEALRELLRE---------LGLPTTLSELGV----TEEDLDAL 340
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
15-129 |
3.28e-05 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 45.22 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613975 15 IFIGQGLLAQSDCLTASVSGKKVLIVSNDTVAPL-YLQSLQRLLLPA---AQVFAHILPDgeqyKTLAQLESVFTALLEH 90
Cdd:cd08194 4 IIIGGGALEELGEEAASLGGKRALIVTDKVMVKLgLVDKVTQLLAEAgiaYAVFDDVVSE----PTDEMVEEGLALYKEG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 647613975 91 NCGrdvVLVALGGG-------VIGDMVGFA---------AACYQRGVDFIQIPTT 129
Cdd:cd08194 80 GCD---FIVALGGGspidtakAIAVLATNGgpirdymgpRKVDKPGLPLIAIPTT 131
|
|
| |
