|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-347 |
2.71e-156 |
|
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: 442.22 E-value: 2.71e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 1 MQ-IKVNLKENAYKVYI---------DELENLEFDTKVFILSNPKISGLHLKKLLNKIKA--KEIFIATIKDGEEYKNLN 68
Cdd:COG0337 1 MQtLTVNLGERSYDIRIgrglldelgELLAELLKGRRVLVVTDENVAPLYGERLRAALEAagFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 69 TVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQ 148
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 149 PKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKsfLNARcENEIFSKIIAKSIELKAKVVEQDEKE 228
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADA--LLAR-DPEALEEAIARSCEIKAEVVAADERE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 229 NHLRMLLNYGHTFAHVIENLTQYSvYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHYKIDNINAFYE 308
Cdd:COG0337 238 SGLRALLNFGHTFGHAIEAATGYR-LLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLA 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 2199892730 309 AFFMDKKNSNQKLNFILPDSLGKGLIKDNIDLKIIIKTL 347
Cdd:COG0337 317 AMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-347 |
2.62e-150 |
|
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: 426.86 E-value: 2.62e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 12 YKVYID--------ELENLEFDTKVFILSNPKISGLHLKKLLNKIKA--KEIFIATIKDGEEYKNLNTVEEILNQMFNSK 81
Cdd:cd08195 2 YPILIGsglldklgELLELKKGSKVVIVTDENVAKLYGELLLKSLEAagFKVEVIVIPAGEKSKSLETVERIYDFLLEAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 82 LDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPKAVYCESEFLKT 161
Cdd:cd08195 82 LDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLKT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 162 LGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKSFlnaRCENEIFSKIIAKSIELKAKVVEQDEKENHLRMLLNYGHTF 241
Cdd:cd08195 162 LPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKIL---ARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 242 AHVIENLTQYSvYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHYKIDNINAFYEAFFMDKKNSNQKL 321
Cdd:cd08195 239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 2199892730 322 NFILPDSLGKGLIKDNIDLKIIIKTL 347
Cdd:cd08195 318 RFVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
12-347 |
4.56e-141 |
|
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: 403.55 E-value: 4.56e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 12 YKVYIDE------LENLEFDTKVFILSNPKISGLHLKKLLNKIKAK--EIFIATIKDGEEYKNLNTVEEILNQMFNSKLD 83
Cdd:TIGR01357 1 YPVHVGEglldqlVEELAEPSKLVIITDETVADLYGDKLLEALQALgyNVLKLTVPDGEESKSLETVQRLYDQLLEAGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 84 RKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPKAVYCESEFLKTLG 163
Cdd:TIGR01357 81 RSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 164 EKELSAGIAEFIKMAVIFDKNLLDFIESIDEKSFLnaRCENEIFSKIIAKSIELKAKVVEQDEKENHLRMLLNYGHTFAH 243
Cdd:TIGR01357 161 DRELRSGMAEVIKHGLIADAELFDELESNDKLRLN--LQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 244 VIENLTQYSVYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHY-KIDNINAFYEAFFMDKKNSNQKLN 322
Cdd:TIGR01357 239 AIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLpKDLDVDELLNAMLNDKKNSGGKIR 318
|
330 340
....*....|....*....|....*
gi 2199892730 323 FILPDSLGKGLIKDNIDLKIIIKTL 347
Cdd:TIGR01357 319 FVLLEEIGKAALAREVPDEMVLELL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
55-316 |
1.78e-135 |
|
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: 386.08 E-value: 1.78e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 55 IATIKDGEEYKNLNTVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGI 134
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 135 NNSFGKNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKSFlnaRCENEIFSKIIAKS 214
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALL---NLDPDALEEAIARS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 215 IELKAKVVEQDEKENHLRMLLNYGHTFAHVIENLTQYSVYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNL 294
Cdd:pfam01761 158 CEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGL 237
|
250 260
....*....|....*....|..
gi 2199892730 295 PTHYKIDNINAFYEAFFMDKKN 316
Cdd:pfam01761 238 PTSLPDLDVEQLLAAMARDKKV 259
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
3-351 |
9.88e-91 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 278.19 E-value: 9.88e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 3 IKVNLKENAYKVYI-----DELENLEFD---TKVFILSNPKISGLHLKKLLNKIKAKEIFIAT----IKDGEEYKNLNTV 70
Cdd:PLN02834 70 VKVDLGDRSYPIYIgsgllDHGELLQRHvhgKRVLVVTNETVAPLYLEKVVEALTAKGPELTVesviLPDGEKYKDMETL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 71 EEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPK 150
Cdd:PLN02834 150 MKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 151 AVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKsfLNARcENEIFSKIIAKSIELKAKVVEQDEKENH 230
Cdd:PLN02834 230 CVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEK--LLAR-DPGALAYAIKRSCENKAEVVSLDEKESG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 231 LRMLLNYGHTFAHVIENLTQYSVYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHY--KIDnINAFYE 308
Cdd:PLN02834 307 LRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPpeKMT-VEMFKS 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2199892730 309 AFFMDKKNSNQKLNFI-LPDSLGKGLIKDNIDLKIIIKTLKEFS 351
Cdd:PLN02834 386 LMAVDKKVADGLLRLIlLKGELGNCVFTGDFDREALEETLRAFC 429
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-347 |
2.71e-156 |
|
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: 442.22 E-value: 2.71e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 1 MQ-IKVNLKENAYKVYI---------DELENLEFDTKVFILSNPKISGLHLKKLLNKIKA--KEIFIATIKDGEEYKNLN 68
Cdd:COG0337 1 MQtLTVNLGERSYDIRIgrglldelgELLAELLKGRRVLVVTDENVAPLYGERLRAALEAagFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 69 TVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQ 148
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 149 PKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKsfLNARcENEIFSKIIAKSIELKAKVVEQDEKE 228
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADA--LLAR-DPEALEEAIARSCEIKAEVVAADERE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 229 NHLRMLLNYGHTFAHVIENLTQYSvYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHYKIDNINAFYE 308
Cdd:COG0337 238 SGLRALLNFGHTFGHAIEAATGYR-LLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLA 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 2199892730 309 AFFMDKKNSNQKLNFILPDSLGKGLIKDNIDLKIIIKTL 347
Cdd:COG0337 317 AMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-347 |
2.62e-150 |
|
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: 426.86 E-value: 2.62e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 12 YKVYID--------ELENLEFDTKVFILSNPKISGLHLKKLLNKIKA--KEIFIATIKDGEEYKNLNTVEEILNQMFNSK 81
Cdd:cd08195 2 YPILIGsglldklgELLELKKGSKVVIVTDENVAKLYGELLLKSLEAagFKVEVIVIPAGEKSKSLETVERIYDFLLEAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 82 LDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPKAVYCESEFLKT 161
Cdd:cd08195 82 LDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLKT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 162 LGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKSFlnaRCENEIFSKIIAKSIELKAKVVEQDEKENHLRMLLNYGHTF 241
Cdd:cd08195 162 LPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKIL---ARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 242 AHVIENLTQYSvYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHYKIDNINAFYEAFFMDKKNSNQKL 321
Cdd:cd08195 239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 2199892730 322 NFILPDSLGKGLIKDNIDLKIIIKTL 347
Cdd:cd08195 318 RFVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
12-347 |
4.56e-141 |
|
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: 403.55 E-value: 4.56e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 12 YKVYIDE------LENLEFDTKVFILSNPKISGLHLKKLLNKIKAK--EIFIATIKDGEEYKNLNTVEEILNQMFNSKLD 83
Cdd:TIGR01357 1 YPVHVGEglldqlVEELAEPSKLVIITDETVADLYGDKLLEALQALgyNVLKLTVPDGEESKSLETVQRLYDQLLEAGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 84 RKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPKAVYCESEFLKTLG 163
Cdd:TIGR01357 81 RSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 164 EKELSAGIAEFIKMAVIFDKNLLDFIESIDEKSFLnaRCENEIFSKIIAKSIELKAKVVEQDEKENHLRMLLNYGHTFAH 243
Cdd:TIGR01357 161 DRELRSGMAEVIKHGLIADAELFDELESNDKLRLN--LQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 244 VIENLTQYSVYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHY-KIDNINAFYEAFFMDKKNSNQKLN 322
Cdd:TIGR01357 239 AIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLpKDLDVDELLNAMLNDKKNSGGKIR 318
|
330 340
....*....|....*....|....*
gi 2199892730 323 FILPDSLGKGLIKDNIDLKIIIKTL 347
Cdd:TIGR01357 319 FVLLEEIGKAALAREVPDEMVLELL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
55-316 |
1.78e-135 |
|
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: 386.08 E-value: 1.78e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 55 IATIKDGEEYKNLNTVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGI 134
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 135 NNSFGKNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKSFlnaRCENEIFSKIIAKS 214
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALL---NLDPDALEEAIARS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 215 IELKAKVVEQDEKENHLRMLLNYGHTFAHVIENLTQYSVYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNL 294
Cdd:pfam01761 158 CEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGL 237
|
250 260
....*....|....*....|..
gi 2199892730 295 PTHYKIDNINAFYEAFFMDKKN 316
Cdd:pfam01761 238 PTSLPDLDVEQLLAAMARDKKV 259
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
23-332 |
1.75e-94 |
|
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: 284.30 E-value: 1.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 23 EFDtKVFILSNPKISGLHLKKLLNKIKAK-EIFIATIKDGEEYKNLNTVEEILNQMFNSKLDRKSILISFGGGVISDIGG 101
Cdd:cd08169 22 AFD-QCLIIVDSGVPDLIVNYLAEYFGYYlEVHVFIIQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDVVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 102 FVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIF 181
Cdd:cd08169 101 FAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 182 DKNLLDFIESIDEKSFLNARcenEIFSKIIAKSIELKAKVVEQDEKENHLRMLLNYGHTFAHVIENLTQYSVyLHGEAVA 261
Cdd:cd08169 181 DNDFFEFLEDKANSATVYSP---EQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTFGHALELASGYKI-PHGEAVA 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2199892730 262 IGMNMANRLALNLELLSEKECHRIERILKKFNLPTHY-KIDNINAFYEAFFMDKKNSNQKLNFILPDSLGKG 332
Cdd:cd08169 257 VGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHpLALDPDSLYEYLESDKKSLYGNLGMILLSGVGDG 328
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
3-351 |
9.88e-91 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 278.19 E-value: 9.88e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 3 IKVNLKENAYKVYI-----DELENLEFD---TKVFILSNPKISGLHLKKLLNKIKAKEIFIAT----IKDGEEYKNLNTV 70
Cdd:PLN02834 70 VKVDLGDRSYPIYIgsgllDHGELLQRHvhgKRVLVVTNETVAPLYLEKVVEALTAKGPELTVesviLPDGEKYKDMETL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 71 EEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPK 150
Cdd:PLN02834 150 MKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 151 AVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKsfLNARcENEIFSKIIAKSIELKAKVVEQDEKENH 230
Cdd:PLN02834 230 CVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEK--LLAR-DPGALAYAIKRSCENKAEVVSLDEKESG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 231 LRMLLNYGHTFAHVIENLTQYSVYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHY--KIDnINAFYE 308
Cdd:PLN02834 307 LRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPpeKMT-VEMFKS 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2199892730 309 AFFMDKKNSNQKLNFI-LPDSLGKGLIKDNIDLKIIIKTLKEFS 351
Cdd:PLN02834 386 LMAVDKKVADGLLRLIlLKGELGNCVFTGDFDREALEETLRAFC 429
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
18-348 |
2.34e-81 |
|
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: 251.73 E-value: 2.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 18 ELENLEFDtKVFILSNPKISGLHLKKLLNKIKAKEIFIATI--KDGEEYKNLNTVEEILNQMFNSKLDRKSILISFGGGV 95
Cdd:cd08197 17 ILEELKAD-RHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLvvPAGESNKTLSTLTELAERLIAAGITRRSVIIALGGGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 96 ISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFGKNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFI 175
Cdd:cd08197 96 VGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLKTLPPRQIRSGLCEAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 176 KMAVIFDKNLLDFIESIdeksfLNARCENEI--FSKIIAKSIELKAKVVEQDEKENHLRMLLNYGHTFAHVIENLTQYSv 253
Cdd:cd08197 176 KNALIQDPEFLDYLEDY-----LNSDLDYDPefLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTVGHAIELLSGGE- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 254 YLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTH----YKIDNInafYEAFFMDKK-----NSNQKLNFI 324
Cdd:cd08197 250 LSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIipdgISVEAI---LEVIRYDNKrgyikADADTIRMV 326
|
330 340
....*....|....*....|....*....
gi 2199892730 325 LPDSLGKGLIKDN-----IDLKIIIKTLK 348
Cdd:cd08197 327 LLEKLGKPANPDGdyltpVPEEIVKEALE 355
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
52-332 |
8.69e-74 |
|
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: 232.03 E-value: 8.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 52 EIFIATIKDGEEYKNLNTVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGK 131
Cdd:cd08199 55 EATILVLPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 132 TGINnsFG--KNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESIDEKSFLNARCENEIFSK 209
Cdd:cd08199 135 TGVN--FGghKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVETRFFQDEVADE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 210 IIAKSIELKAKVVEQDEKENHLRMLLNYGHTFAHVIENLTQYSVyLHGEAVAIGMNMANRLALNLELLSEKECHRIERIL 289
Cdd:cd08199 213 IIRRAIQGMLEELAPNLWEHDLERLVDFGHTFSPILEMAAAPEL-LHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLM 291
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2199892730 290 KKFNLPTHYKIDNINAFYEAFFMDKKNSNQKLNFILPDSLGKG 332
Cdd:cd08199 292 RRLGLPVWHPLCTPDLLWRALEDIVKHRDGLQRLPLPKGIGEC 334
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
61-349 |
8.75e-52 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; This family contains dehydroquinate synthase-like proteins. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. The activity of DHQS requires NAD as cofactor. Proteins of this family share sequence similarity and functional motifs with that of dehydroquinate synthase, but the specific function has not been characterized.
Pssm-ID: 341477 Cd Length: 366 Bit Score: 175.45 E-value: 8.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 61 GEEYKN-LNTVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGInNSFG 139
Cdd:cd08198 75 GEAVKNdPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGI-NFFG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 140 -KNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIEsidEKSFLNARCENEIFSKIIAKSIELk 218
Cdd:cd08198 154 kKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLE---RNAAALRQRDPDAMEKLIRRCAEL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 219 akvveqdekenHLRML--------------LNYGHTFAHVIENLTQYSVyLHGEAVAIGMNMANRLALNLELLSEKECHR 284
Cdd:cd08198 230 -----------HLDHIaasgdpfetgsarpLDFGHWSAHKLEQLSGYAL-RHGEAVAIGIALDSLYARLLGLLSREDFDR 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2199892730 285 IERILKKFNLPT------HYKIDNINAFYEAFfmdKKNSNQKLNFILPDSLGKGLIKDNIDLKIIIKTLKE 349
Cdd:cd08198 298 ILALLQNLGLPLwhplleRDGVLELLDGLEEF---REHLGGRLTITLLRGIGVGVEVHEIDLDLMEEAIDE 365
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
61-297 |
7.63e-50 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 171.23 E-value: 7.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 61 GEEYKN-LNTVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGInNSFG 139
Cdd:PRK06203 87 GEAAKNdPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGI-NAFG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 140 -KNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIESidEKSFLnARCENEIFSKIIAKSIELk 218
Cdd:PRK06203 166 kKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEA--HAAAL-AARDPEAMEELIYRCAEL- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 219 akvveqdekenHLRML--------------LNYGHTFAHVIENLTQYSVyLHGEAVAIGMNMANRLALNLELLSEKECHR 284
Cdd:PRK06203 242 -----------HLEHIagggdpfefgssrpLDFGHWSAHKLEQLTNYAL-RHGEAVAIGIALDSLYSYLLGLLSEAEAQR 309
|
250
....*....|...
gi 2199892730 285 IERILKKFNLPTH 297
Cdd:PRK06203 310 ILALLRALGFPLY 322
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
52-337 |
4.59e-49 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 172.74 E-value: 4.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 52 EIFIATIKDGEEYKNLNTVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGK 131
Cdd:PRK14021 237 EVSDIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 132 TGINNSFGKNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDFIE-------SIDEKSFLNARCEn 204
Cdd:PRK14021 317 TGINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEdhaaelrAFDGSTFLGSPLE- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 205 EIFSKIIAKSIELKAKVVEQDEKENHLRMLLNYGHTFAHVIENLTQYSvYLHGEAVAIGMNMANRLALNLELLSEKECHR 284
Cdd:PRK14021 396 DVVAELIERTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEKLEHFR-WRHGNAVAVGMVYAAELAHLLGYIDQDLVDY 474
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2199892730 285 IERILKKFNLPTHYKIDNINAFYEAFFMDKKNSNQKLNFILPDSLGKGLIKDN 337
Cdd:PRK14021 475 HRSLLASLGLPTSWNGGSFDDVLALMHRDKKARGNELRFVVLDEIGHPVHLDN 527
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
60-264 |
1.75e-32 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 126.56 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 60 DGEEYKNLNTVEEILNQMFNSKLDRKSILISFGGGVISDIGGFVSSIYKRGIDFINIPTTLLACIDAAVGGKTGINNSFG 139
Cdd:PRK13951 213 DGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAIDFAGV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 140 KNLIGTFYQPKAVYCESEFLKTLGEKELSAGIAEFIKMAVIFDKNLLDF--IESIDEKSFlnarcenEIFSKIIAKSIEL 217
Cdd:PRK13951 293 KNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVELFdePEKIEKRNL-------RVLSEMVKISVEE 365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2199892730 218 KAKVVEQDEKENHLRMLLNYGHTFAHVIENLTQYSvylHGEAVAIGM 264
Cdd:PRK13951 366 KARIVMEDPYDMGLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGI 409
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
15-303 |
1.24e-21 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 92.81 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 15 YIDELENLEFDtKVFILSN---PKISGLHLKKLLNKIKAKEIFIAtikdGEEYKNLNTVEEILNQMFNSKLDrksILISF 91
Cdd:cd07766 13 KLGEIKRRGFD-RALVVSDegvVKGVGEKVADSLKKGLAVAIFDF----VGENPTFEEVKNAVERARAAEAD---AVIAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 92 GGGVISDIGGFVSSIYKRGIDFINIPTTLLAciDAAVGGKTGINNSFGKNL-IGTFYQPKAVYCESEFLKTLGEKELSAG 170
Cdd:cd07766 85 GGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNKqVGPHYNPDVVFVDTDITKGLPPRQVASG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 171 IAEFIKMAVIFDknlldfiesideksflnarceneifsKIIAKSIELKAKVVEqdekenhlRMLLNYGHTFAHvieNLTQ 250
Cdd:cd07766 163 GVDALAHAVELE--------------------------KVVEAATLAGMGLFE--------SPGLGLAHAIGH---ALTA 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2199892730 251 YSVYLHGEAVAIGMNMANRLALNLELLSEKECHRIERILKKFNLPTHYKIDNI 303
Cdd:cd07766 206 FEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHLADLGV 258
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
55-304 |
1.48e-08 |
|
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: 55.65 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 55 IATIKDGEEYKNLNTVEEILnqmfnSKLDRKSILISFGGGVISDIGGFVSsiYKRGIDFINIPTTllacidAAVGGKTGI 134
Cdd:cd08549 46 LKTVCDIVYYDNIDNLEDEL-----KKYTFYDCVIGIGGGRSIDTGKYLA--YKLKIPFISVPTS------ASNDGIASP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 135 NNSFGKNLIGTFYQ---PKAVYCESEFLKTLGEKELSAGIAEFI-KMAVIFDKNLLDFI--ESIDEKSflnarcenEIFS 208
Cdd:cd08549 113 IVSLRIPGVKKTFMadaPIAIIADTEIIKKSPRRLLSAGIGDLVsNITAVLDWKLAHKEkgEKYSEFA--------AILS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 209 KIIAKSI---ELKAKVVEQDEKE-------NHLRMLL--------NYGHTFAHVIENLTQYSVY---LHGEAVAIGMNMA 267
Cdd:cd08549 185 KTSAKELvsyVLKASDLEEYHRVlvkalvgSGIAMAIagssrpasGSEHLFSHALDKLKEEYLNinvLHGEQVGVGTIIM 264
|
250 260 270
....*....|....*....|....*....|....*..
gi 2199892730 268 NRLALNLELLSEKECHRIERILKKFNLPTHYKIDNIN 304
Cdd:cd08549 265 SYLHEKENKKLSGLHERIKMILKKVGAPTTAKQLGID 301
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
4-120 |
1.65e-06 |
|
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: 49.09 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 4 KVNLKENAYKVYIDELENLEFDTKVFILSNPKISGLHLKKLLNKIKAKEIFIATIkDGEEYKNLNTVEEILNQMFNSKLD 83
Cdd:cd08173 4 NVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIV-DIATIEEAAEVEKVKKLIKESKAD 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 2199892730 84 rksILISFGGGVISDIGGFVSsiYKRGIDFINIPTTL 120
Cdd:cd08173 83 ---FIIGVGGGKVIDVAKYAA--YKLNLPFISIPTSA 114
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
17-296 |
2.04e-06 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 49.12 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 17 DELENLEFDTKVFILSNP---KISGLHLKKLLNKIKAKEIFIAtikDGEEYKNLNTVEEILNQMfnskldRKSILISFGG 93
Cdd:PRK00843 26 DVCSDLKLTGRALIVTGPttkKIAGDRVEENLEDAGDVEVVIV---DEATMEEVEKVEEKAKDV------NAGFLIGVGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 94 GVISDIGGFVSsiYKRGIDFINIPTTllACIDAAVGGKTGINNSFGKNLIGTfYQPKAVYCESEFLKTLGEKELSAGIAE 173
Cdd:PRK00843 97 GKVIDVAKLAA--YRLGIPFISVPTA--ASHDGIASPRASIKGGGKPVSVKA-KPPLAVIADTEIIAKAPYRLLAAGCGD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 174 FIK--MAVifdknlldfiesIDEKsfLNARCENEIFSKIIAKSIELKAK-VVEQDEK-----ENHLRM----LLNYG--- 238
Cdd:PRK00843 172 IISnyTAV------------KDWR--LAHRLRGEYYSEYAAALSLMTAKmLIENADIikpglEESARLvvkaLISSGvam 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2199892730 239 -------------HTFAHVIENLTQYSVyLHGEAVAIGMNManrlalnLELLSEKECHRIERILKKFNLPT 296
Cdd:PRK00843 238 siagssrpasgseHLFSHALDRLAPGPA-LHGEQCGVGTII-------MMYLHGGDWRKIRDALKKIGAPT 300
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
26-312 |
1.42e-04 |
|
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: 43.27 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 26 TKVFILSNP---KISGLHLKKLLNKIKAKEIFIATIKDGEEYKNLNTVEEILNQMfnsKLDRkSILISFGGGVISDIGGF 102
Cdd:cd08175 25 KKVLVVADEntyAAAGEEVEAALEEAGVTVCLLIFPGEGDLIADEAAVGKVLLEL---EKDT-DLIIAVGSGTINDLTKY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 103 VSsiYKRGIDFINIPTTllacidAAVGGKTginnSFGKNLI--G---TFY--QPKAVYCESEFLKTlGEKELS-AGIAEF 174
Cdd:cd08175 101 AA--YKLGIPYISVPTA------PSMDGYT----SSGAPIIvdGvkkTFPahAPKAIFADLDVLAN-APQRMIaAGFGDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 175 I-KMAVIFDKNLLDFI--ESIDEKSF-LNARCENEIFSKIiaksielkAKVVEQDEKENHLRM--LLNYG---------- 238
Cdd:cd08175 168 LgKYTALADWKLSHLLggEYYCPEVAdLVQEALEKCLDNA--------EGIAARDPEAIEALMeaLILSGlamqlvgnsr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892730 239 ------HTFAHVIE----NLTQYSVyLHGEAVAIGMNMANRLALNLELLSEKEchrIERILKKFNLPTHYKIDNIN---- 304
Cdd:cd08175 240 pasgaeHHLSHYWEmeflRLGKPPV-LHGEKVGVGTLLIAALYILEQLPPPEE---LRELLRKAGAPTTPEDLGIDrdll 315
|
330
....*....|
gi 2199892730 305 --AFYEAFFM 312
Cdd:cd08175 316 rdSLRLAKEI 325
|
|
| |
