|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-356 |
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: 548.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 1 MERLTVTLGERSYPITIAAGLFNDPASFL-PLKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLA 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLaELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 80 VMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 160 PVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETGL 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 240 RALLNLGHTFGHAIEAEMGYgNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPqEMSAQAYLPHM 319
Cdd:COG0337 241 RALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLP-ALDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 489009704 320 MRDKKVLAGEMRLVLPLAIGSSELRGGVPHDVVLGAI 356
Cdd:COG0337 319 KRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-356 |
1.42e-167 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 471.16 E-value: 1.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 12 SYPITIAAGLFNDPASFLPLKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLAVMDTVFTALLQK 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 92 PHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDLNCLK 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 172 TLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGH 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 252 AIEAEMGYGnWLHGEavaagmvmaaRTSERLGQFRAQDTQRIIDLLKRAGLPVRgPQEMSAQAYLPHMMRDKKVLAGEMR 331
Cdd:cd08195 241 AIESASGYK-LLHGEavaigmvaaaRLSVKLGLLSEEDLERIRALLKKLGLPTS-IKDLDPEELLEAMKRDKKNRGGKIR 318
|
330 340
....*....|....*....|....*
gi 489009704 332 LVLPLAIGSSELRGGVPHDVVLGAI 356
Cdd:cd08195 319 FVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-356 |
4.60e-161 |
|
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: 454.78 E-value: 4.60e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 13 YPITIAAGLFNDPASFLplKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLAVMDTVFTALLQKP 92
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEEL--AEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 93 HGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDLNCLKT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 173 LPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDT-AMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGH 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELeHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 252 AIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPQEMSAQAYLPHMMRDKKVLAGEMR 331
Cdd:TIGR01357 239 AIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKIR 318
|
330 340
....*....|....*....|....*
gi 489009704 332 LVLPLAIGSSELRGGVPHDVVLGAI 356
Cdd:TIGR01357 319 FVLLEEIGKAALAREVPDEMVLELL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-334 |
5.51e-154 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 439.97 E-value: 5.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 1 MERLTVTLGERSYPITIAAGLFNDPASFLPLKSGDQAMLVTNETLAPLYLDTVRSALEQSG--VNVDSVILPDGEQYKSL 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGpeLTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 79 AVMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFW 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 159 QPVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETG 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 239 LRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPQEMSAQAYLPH 318
Cdd:PLN02834 307 LRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSL 386
|
330
....*....|....*.
gi 489009704 319 MMRDKKVLAGEMRLVL 334
Cdd:PLN02834 387 MAVDKKVADGLLRLIL 402
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-326 |
2.69e-152 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 429.23 E-value: 2.69e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 66 SVILPDGEQYKSLAVMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAV 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 146 NHPLGKNMIGAFWQPVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCEL 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 226 KAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVR 305
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|.
gi 489009704 306 GPQEmSAQAYLPHMMRDKKVL 326
Cdd:pfam01761 241 LPDL-DVEQLLAAMARDKKVR 260
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-356 |
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: 548.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 1 MERLTVTLGERSYPITIAAGLFNDPASFL-PLKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLA 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLaELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 80 VMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 160 PVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETGL 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 240 RALLNLGHTFGHAIEAEMGYgNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPqEMSAQAYLPHM 319
Cdd:COG0337 241 RALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLP-ALDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 489009704 320 MRDKKVLAGEMRLVLPLAIGSSELRGGVPHDVVLGAI 356
Cdd:COG0337 319 KRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-356 |
1.42e-167 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 471.16 E-value: 1.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 12 SYPITIAAGLFNDPASFLPLKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLAVMDTVFTALLQK 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 92 PHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDLNCLK 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 172 TLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGH 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 252 AIEAEMGYGnWLHGEavaagmvmaaRTSERLGQFRAQDTQRIIDLLKRAGLPVRgPQEMSAQAYLPHMMRDKKVLAGEMR 331
Cdd:cd08195 241 AIESASGYK-LLHGEavaigmvaaaRLSVKLGLLSEEDLERIRALLKKLGLPTS-IKDLDPEELLEAMKRDKKNRGGKIR 318
|
330 340
....*....|....*....|....*
gi 489009704 332 LVLPLAIGSSELRGGVPHDVVLGAI 356
Cdd:cd08195 319 FVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-356 |
4.60e-161 |
|
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: 454.78 E-value: 4.60e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 13 YPITIAAGLFNDPASFLplKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLAVMDTVFTALLQKP 92
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEEL--AEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 93 HGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDLNCLKT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 173 LPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDT-AMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGH 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELeHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 252 AIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPQEMSAQAYLPHMMRDKKVLAGEMR 331
Cdd:TIGR01357 239 AIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGKIR 318
|
330 340
....*....|....*....|....*
gi 489009704 332 LVLPLAIGSSELRGGVPHDVVLGAI 356
Cdd:TIGR01357 319 FVLLEEIGKAALAREVPDEMVLELL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-334 |
5.51e-154 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 439.97 E-value: 5.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 1 MERLTVTLGERSYPITIAAGLFNDPASFLPLKSGDQAMLVTNETLAPLYLDTVRSALEQSG--VNVDSVILPDGEQYKSL 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGpeLTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 79 AVMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFW 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 159 QPVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETG 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 239 LRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPQEMSAQAYLPH 318
Cdd:PLN02834 307 LRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSL 386
|
330
....*....|....*.
gi 489009704 319 MMRDKKVLAGEMRLVL 334
Cdd:PLN02834 387 MAVDKKVADGLLRLIL 402
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-326 |
2.69e-152 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 429.23 E-value: 2.69e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 66 SVILPDGEQYKSLAVMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAV 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 146 NHPLGKNMIGAFWQPVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCEL 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 226 KAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVR 305
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|.
gi 489009704 306 GPQEmSAQAYLPHMMRDKKVL 326
Cdd:pfam01761 241 LPDL-DVEQLLAAMARDKKVR 260
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-356 |
2.36e-87 |
|
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: 267.53 E-value: 2.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 12 SYPITIAAGLFNDPASFLPLKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLAVMDTVFTALLQK 91
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAERLIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 92 PHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDLNCLK 171
Cdd:cd08197 81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 172 TLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGH 251
Cdd:cd08197 161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTVGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 252 AIEAEMGyGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPQEMSAQAYLPHMMRDKK-----VL 326
Cdd:cd08197 241 AIELLSG-GELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPDGISVEAILEVIRYDNKrgyikAD 319
|
330 340 350
....*....|....*....|....*....|....*
gi 489009704 327 AGEMRLVLPLAIGSSELRGG-----VPHDVVLGAI 356
Cdd:cd08197 320 ADTIRMVLLEKLGKPANPDGdyltpVPEEIVKEAL 354
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
12-339 |
3.98e-81 |
|
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: 250.79 E-value: 3.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 12 SYPITIAAGLFNDPASFLPLKSGDQAMLVTNETLAPLYldtVRSALEQSG--VNVDSVILPDGEQYKSLAVMDTVFTALL 89
Cdd:cd08169 1 EYPVFFGEGVFESVNSYIPRDAFDQCLIIVDSGVPDLI---VNYLAEYFGyyLEVHVFIIQGGEAYKTFQTVVEELERAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 90 QKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDLNC 169
Cdd:cd08169 78 ALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 170 LKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTF 249
Cdd:cd08169 158 LKTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 250 GHAIEAEMGYGnWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGPQEMSAQAYLPHMMRDKKVLAGE 329
Cdd:cd08169 238 GHALELASGYK-IPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDSLYEYLESDKKSLYGN 316
|
330
....*....|
gi 489009704 330 MRLVLPLAIG 339
Cdd:cd08169 317 LGMILLSGVG 326
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
12-341 |
6.32e-66 |
|
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: 212.39 E-value: 6.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 12 SYPITIAAGLFnDPASFLPLKSGDQA----MLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLAVMDTVFTA 87
Cdd:cd08199 1 SYDVVLVDDLF-DPENPTLADAYGRPgrrrLVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTMETVLRIVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 88 LLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDL 167
Cdd:cd08199 80 LDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 168 NCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLA---LDDTAMAYCIRRCCELKAEVVAADERETGLRALLN 244
Cdd:cd08199 160 SFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVEtrfFQDEVADEIIRRAIQGMLEELAPNLWEHDLERLVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 245 LGHTFGHAIEAEMGYGnWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVR----GPQEM--SAQAYLPH 318
Cdd:cd08199 240 FGHTFSPILEMAAAPE-LLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWhplcTPDLLwrALEDIVKH 318
|
330 340
....*....|....*....|...
gi 489009704 319 mmRDkkvlaGEMRLVLPLAIGSS 341
Cdd:cd08199 319 --RD-----GLQRLPLPKGIGEC 334
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
13-339 |
8.54e-57 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 193.54 E-value: 8.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 13 YPITIAAGLFNDPASFLPLKSGDQAMLVTNETlaPLYLDTVRSALEQSGVNVDSVILPDGEQYKSLAVMDTVFTALLQKP 92
Cdd:PRK14021 189 YDVRIGEGAMNHLPQVLGPKPVKVALIHTQPV--QRHSDRARTLLRQGGYEVSDIVIPDAEAGKTIEVANGIWQRLGNEG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 93 HGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFWQPVSVVVDLNCLKT 172
Cdd:PRK14021 267 FTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLAT 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 173 LPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTA---------MAYCIRRCCELKAEVVAADERETGLRALL 243
Cdd:PRK14021 347 LPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAFDGSTflgspledvVAELIERTVKVKAYHVSSDLKEAGLREFL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 244 NLGHTFGHAIEaEMGYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLPVRGpQEMSAQAYLPHMMRDK 323
Cdd:PRK14021 427 NYGHTLGHAIE-KLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLASLGLPTSW-NGGSFDDVLALMHRDK 504
|
330
....*....|....*.
gi 489009704 324 KVLAGEMRLVLPLAIG 339
Cdd:PRK14021 505 KARGNELRFVVLDEIG 520
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
65-308 |
8.74e-52 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 176.63 E-value: 8.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 65 DSVILPDGEQYK-SLAVMDTVFTALLQkpHG--RDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGG 141
Cdd:PRK06203 80 EPLVVPGGEAAKnDPALVEALHAAINR--HGidRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 142 KTAVNHPLGKNMIGAFWQPVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRR 221
Cdd:PRK06203 158 KNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 222 CCELKAEVVAA--DERETGLRALLNLGHTFGHAIEAEMGYgNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKR 299
Cdd:PRK06203 238 CAELHLEHIAGggDPFEFGSSRPLDFGHWSAHKLEQLTNY-ALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRA 316
|
....*....
gi 489009704 300 AGLPVRGPQ 308
Cdd:PRK06203 317 LGFPLYHPA 325
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
67-357 |
1.92e-50 |
|
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: 172.37 E-value: 1.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 67 VILPDGEQYK-SLAVMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAV 145
Cdd:cd08198 70 LIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 146 NHPLGKNMIGAFWQPVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFSWLENNIDALLALDDTAMAYCIRRCCEL 225
Cdd:cd08198 150 NFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 226 KAEVVAA--DERETGLRALLNLGHTFGHAIEAEMGYGnWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKRAGLP 303
Cdd:cd08198 230 HLDHIAAsgDPFETGSARPLDFGHWSAHKLEQLSGYA-LRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLP 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489009704 304 VRGPQ-EMSAQAYLPHMMRD-KKVLAGEMRLVLPLAIGSSELRGGVPHDVVLGAIA 357
Cdd:cd08198 309 LWHPLlERDGVLELLDGLEEfREHLGGRLTITLLRGIGVGVEVHEIDLDLMEEAID 364
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
67-335 |
2.02e-40 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 148.51 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 67 VILPDGEQYKSLAVMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVN 146
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAID 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 147 HPLGKNMIGAFWQPVSVVVDLNCLKTLPKRELASGLAEVIKYGVILDGEFFswLENNIDALLALDDTAMAYCIRRCCELK 226
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVE--LFDEPEKIEKRNLRVLSEMVKISVEEK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 227 AEVVAADERETGLRALLNLGHTFGHAIEAEMGYGnwlHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKR-AGLPVR 305
Cdd:PRK13951 367 ARIVMEDPYDMGLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQiVPIPVP 443
|
250 260 270
....*....|....*....|....*....|
gi 489009704 306 GPQEMSAQAYLphmMRDKKVLAGEmRLVLP 335
Cdd:PRK13951 444 SVDVEKARNLI---LNDKKILKGS-RVRLP 469
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
34-304 |
4.32e-25 |
|
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: 102.44 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 34 GDQAMLVTNETLAPLYLDTVRSALEqSGVNVDSVILPDGEqykslAVMDTVFTALLQKPHGRDTTLVALGGGVIGDLTGF 113
Cdd:cd07766 22 FDRALVVSDEGVVKGVGEKVADSLK-KGLAVAIFDFVGEN-----PTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 114 AAASYQRGVRFIQVPTTLLSqvDSSVGGKTAVNHPLGKN-MIGAFWQPVSVVVDLNCLKTLPKRELASGLAEVIKYGVIl 192
Cdd:cd07766 96 VAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 193 dgeffswLENNIDAllalddtamaycirrCCELKAEVVAaderetglRALLNLGHTFGHAIEAEMGYgnwLHGEAVAAGM 272
Cdd:cd07766 173 -------LEKVVEA---------------ATLAGMGLFE--------SPGLGLAHAIGHALTAFEGI---PHGEAVAVGL 219
|
250 260 270
....*....|....*....|....*....|..
gi 489009704 273 VMAARTSERLGQFRAQDTQRIIDLLKRAGLPV 304
Cdd:cd07766 220 PYVLKVANDMNPEPEAAIEAVFKFLEDLGLPT 251
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
31-266 |
6.20e-09 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 56.83 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 31 LKSGDQAMLVTNETLAPLYLDTVRSALEQSGvNVDSVILPDgeqykslAVMDTVFTALLQKPHGRDTTLVALGGGVIGDL 110
Cdd:PRK00843 31 LKLTGRALIVTGPTTKKIAGDRVEENLEDAG-DVEVVIVDE-------ATMEEVEKVEEKAKDVNAGFLIGVGGGKVIDV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 111 TGFAaaSYQRGVRFIQVPTT-----LLSQVDSSVGGKTavNHPLGKNMigafwqPVSVVVDLNCLKTLPKRELASGLAEV 185
Cdd:PRK00843 103 AKLA--AYRLGIPFISVPTAashdgIASPRASIKGGGK--PVSVKAKP------PLAVIADTEIIAKAPYRLLAAGCGDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 186 I-KYGVILD--------GEFFSwlE-----NNIDALLALDDTAMaycIRRCCELKAEVVAaderetglRALLNLG----- 246
Cdd:PRK00843 173 IsNYTAVKDwrlahrlrGEYYS--EyaaalSLMTAKMLIENADI---IKPGLEESARLVV--------KALISSGvamsi 239
|
250 260 270
....*....|....*....|....*....|.
gi 489009704 247 -----------HTFGHAIEAeMGYGNWLHGE 266
Cdd:PRK00843 240 agssrpasgseHLFSHALDR-LAPGPALHGE 269
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
15-266 |
1.26e-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: 55.98 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 15 ITIAAGLFNDPASFL-PLKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILPDGEQYksLAVMDTVFTALLQKPH 93
Cdd:cd08175 4 IVIGEGALKKLPEYLkELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEGDL--IADEAAVGKVLLELEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 94 GRDTtLVALGGGVIGDLTGFaaASYQRGVRFIQVPTTllsqvdSSVGGKTAVNHPLgknMIGAFWQ------PVSVVVDL 167
Cdd:cd08175 82 DTDL-IIAVGSGTINDLTKY--AAYKLGIPYISVPTA------PSMDGYTSSGAPI---IVDGVKKtfpahaPKAIFADL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 168 NCLKTLPKRELASGLAEVI-KY--------GVILDGEFFswlennidallalDDTA---MAYCIRRCCELKAEVVAADER 235
Cdd:cd08175 150 DVLANAPQRMIAAGFGDLLgKYtaladwklSHLLGGEYY-------------CPEVadlVQEALEKCLDNAEGIAARDPE 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489009704 236 ETGL--RALLNLG----------------HTFGHAIE---AEMGYGNWLHGE 266
Cdd:cd08175 217 AIEAlmEALILSGlamqlvgnsrpasgaeHHLSHYWEmefLRLGKPPVLHGE 268
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
89-303 |
1.83e-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: 55.26 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 89 LQKPHGRDTtLVALGGGVIGDLTGFAaaSYQRGVRFIQVPTTllsqvdSSVGGKTAVNHPLGKNMIGAFWQ---PVSVVV 165
Cdd:cd08549 65 LKKYTFYDC-VIGIGGGRSIDTGKYL--AYKLKIPFISVPTS------ASNDGIASPIVSLRIPGVKKTFMadaPIAIIA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 166 DLNCLKTLPKRELASGLAEVI-KYGVILDGEFFSWLENNI--DALLALDDTAMAYCIRrccelkaEVVAADERETGLR-- 240
Cdd:cd08549 136 DTEIIKKSPRRLLSAGIGDLVsNITAVLDWKLAHKEKGEKysEFAAILSKTSAKELVS-------YVLKASDLEEYHRvl 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 241 --ALLNLG----------------HTFGHAIEAEM---GYGNWLHGEAVAAGMVMAARTSERLGQFRAQDTQRIIDLLKR 299
Cdd:cd08549 209 vkALVGSGiamaiagssrpasgseHLFSHALDKLKeeyLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKK 288
|
....
gi 489009704 300 AGLP 303
Cdd:cd08549 289 VGAP 292
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
31-266 |
5.98e-07 |
|
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: 50.63 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 31 LKSGDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVilpdgeqykSLAVMDTVFTA--LLQKPHGRDTTLV-ALGGGVI 107
Cdd:cd08173 22 LLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIV---------DIATIEEAAEVekVKKLIKESKADFIiGVGGGKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 108 GDLTgfAAASYQRGVRFIQVPTTL-----------LSQVDSSVGGKTavnHPlgknmigafwqPVSVVVDLNCLKTLPKR 176
Cdd:cd08173 93 IDVA--KYAAYKLNLPFISIPTSAshdgiaspfasIKGGDKPYSIKA---KA-----------PIAIIADTEIISKAPKR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 177 ELASGLAEVI-KYGVILD--------GEFFSwlenNIDALLALDDTAMAycIRRCCELKAEvvAADERETGLRALLNLG- 246
Cdd:cd08173 157 LLAAGCGDLIsNITAVKDwrlahrlkGEYYS----EYAASLALMSAKLI--IENADLIKPG--LEEGVRTVVKALISSGv 228
|
250 260 270
....*....|....*....|....*....|....*
gi 489009704 247 ---------------HTFGHAIEAeMGYGNWLHGE 266
Cdd:cd08173 229 amsiagssrpasgseHLFSHALDK-LAPGPALHGE 262
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
15-304 |
6.52e-06 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 47.52 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 15 ITIAAGLFNDPASFL--PLKSGDQAMLVTNETLAPLYLDTVRSALEQSG--VNVDSVILPDGEQYKSLAVMDTVFTALlq 90
Cdd:cd08174 4 LKIEEGALEHLGKYLadRNQGFGKVAIVTGEGIDELLGEDILESLEEAGeiVTVEENTDNSAEELAEKAFSLPKVDAI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 91 kphgrdttlVALGGGVIGDLTGFAAasYQRGVRFIQVPTTLLSqvD---SSV------GGKTAVnhplGKNMigafwqPV 161
Cdd:cd08174 82 ---------VGIGGGKVLDVAKYAA--FLSKLPFISVPTSLSN--DgiaSPVavlkvdGKRKSL----GAKM------PY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 162 SVVVDLNCLKTLPKRELASGLAEVI-KYGVILDGEfFSWLENN--ID---ALLAldDTAmAYCIRRCCElkaevvAADER 235
Cdd:cd08174 139 GVIVDLDVIKSAPRRLILAGIGDLIsNITALYDWK-LAEEKGGepVDdfaYLLS--RTA-ADSLLNTPG------KDIKD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 236 ETGLRALLN---LG-----------------HTFGHAIEaEMGYGNWLHGEavaagmvmaartserlgQ----------F 285
Cdd:cd08174 209 DEFLKELAEslvLSgiameiagssrpasgseHLISHALD-KLFPGPALHGI-----------------QvglgtyfmsfL 270
|
330
....*....|....*....
gi 489009704 286 RAQDTQRIIDLLKRAGLPV 304
Cdd:cd08174 271 QGQRYEEIRDVLKRTGFPL 289
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
34-188 |
2.43e-04 |
|
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: 42.46 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 34 GDQAMLVTNETLAPLYLDTVRSALEQSGVNVDSVILpDGEQykSLAVMDTVftALLQKPHGRDTtLVALGGGVIGDLTGF 113
Cdd:COG0371 27 GKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVF-GGEC--SEEEIERL--AEEAKEQGADV-IIGVGGGKALDTAKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009704 114 AAasYQRGVRFIQVPTTL--------LSQVDSSVGGKTAVNHpLGKNmigafwqPVSVVVDLNCLKTLPKRELASGLAEV 185
Cdd:COG0371 101 VA--YRLGLPVVSVPTIAstdapaspLSVIYTEDGAFDGYSF-LAKN-------PDLVLVDTDIIAKAPVRLLAAGIGDA 170
|
....
gi 489009704 186 I-KY 188
Cdd:COG0371 171 LaKW 174
|
|
| |
