|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-349 |
3.85e-157 |
|
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: 444.92 E-value: 3.85e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 1 MKTLEVKTSSATYPVFIGDGIKRNIVDLITSTgHSYTKLLIVTDTAVDAIYGDEMVRLLQQK-WPVNKVVVPSGEQSKSF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLAEL-LKGRRVLVVTDENVAPLYGERLRAALEAAgFEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 80 AEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFH 158
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 159 QPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSELMS-IRSLTDLSKSELAHMLYQGIQVKASIVQEDEKEQG 237
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEEnADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 238 VRAFLNLGHTLGHAIEAEYGYgAITHGDAIAIGMQFALYVSEKELGLSLN-RLELKEWMKELGFPVQVtQEISTKTFVDR 316
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRL-PALDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|...
gi 751617995 317 MIGDKKARGGSVQFVLLKQVGDVTLQSFTKDEL 349
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEEL 350
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-349 |
1.36e-154 |
|
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: 438.03 E-value: 1.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 12 TYPVFIGDGIKRNIVDLITStgHSYTKLLIVTDTAVDAIYGDEMVRLLQQK-WPVNKVVVPSGEQSKSFAEFEHIHTKAI 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLEL--KKGSKVVIVTDENVAKLYGELLLKSLEAAgFKVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 91 QFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSM 169
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 170 LETLSQIERRSGFAEVIKHALISSEDFLSELMSIR-SLTDLSKSELAHMLYQGIQVKASIVQEDEKEQGVRAFLNLGHTL 248
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLdKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 249 GHAIEAEYGYgAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMKELGFPVQVTqEISTKTFVDRMIGDKKARGGS 327
Cdd:cd08195 239 GHAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLErIRALLKKLGLPTSIK-DLDPEELLEAMKRDKKNRGGK 316
|
330 340
....*....|....*....|..
gi 751617995 328 VQFVLLKQVGDVTLQSFTKDEL 349
Cdd:cd08195 317 IRFVLLKGIGKAVIVDDVSEEE 338
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-351 |
3.27e-138 |
|
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: 396.62 E-value: 3.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 13 YPVFIGDGIKRNIVDLITStghsYTKLLIVTDTAVDAIYGDEMVRLLQQ-KWPVNKVVVPSGEQSKSFAEFEHIHTKAIQ 91
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAE----PSKLVIITDETVADLYGDKLLEALQAlGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 92 FQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSML 170
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 171 ETLSQIERRSGFAEVIKHALISSEDFLSELMSIRSLTDLSKSE--LAHMLYQGIQVKASIVQEDEKEQGVRAFLNLGHTL 248
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELehLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 249 GHAIEAEYGYGAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMKELGFPVQVTQEISTKTFVDRMIGDKKARGGS 327
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIErLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330 340
....*....|....*....|....*
gi 751617995 328 VQFVLLKQVGDVTLQS-FTKDELHY 351
Cdd:TIGR01357 317 IRFVLLEEIGKAALAReVPDEMVLE 341
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
68-324 |
3.50e-128 |
|
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: 367.98 E-value: 3.50e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 68 VVVPSGEQSKSFAEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGIN 146
Cdd:pfam01761 2 IVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 147 HPLGKNLIGAFHQPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSEL-MSIRSLTDLSKSELAHMLYQGIQVK 225
Cdd:pfam01761 82 HPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLeENAEALLNLDPDALEEAIARSCEVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 226 ASIVQEDEKEQGVRAFLNLGHTLGHAIEAEYGYGAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMKELGFPVQV 304
Cdd:pfam01761 162 ADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVErIRALLKKYGLPTSL 241
|
250 260
....*....|....*....|
gi 751617995 305 tQEISTKTFVDRMIGDKKAR 324
Cdd:pfam01761 242 -PDLDVEQLLAAMARDKKVR 260
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-346 |
1.31e-100 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 304.00 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 1 MKTLEVKTSSATYPVFIGDGIKRNiVDLITSTGHSyTKLLIVTDTAVDAIYGDEMVRLLQQKWP---VNKVVVPSGEQSK 77
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDH-GELLQRHVHG-KRVLVVTNETVAPLYLEKVVEALTAKGPeltVESVILPDGEKYK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 78 SFAEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGA 156
Cdd:PLN02834 145 DMETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 157 FHQPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSELMS-IRSLTDLSKSELAHMLYQGIQVKASIVQEDEKE 235
Cdd:PLN02834 225 FYQPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEAnMEKLLARDPGALAYAIKRSCENKAEVVSLDEKE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 236 QGVRAFLNLGHTLGHAIEAEYGYGAITHGDAIAIGMQFALYVSEKeLG---LSL-NRleLKEWMKELGFPVQVTQEISTK 311
Cdd:PLN02834 305 SGLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYR-LGwidMSLvNR--IFALLKRAKLPTNPPEKMTVE 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 751617995 312 TFVDRMIGDKKARGGSVQFVLLKQ-------VGDV-------TLQSFTK 346
Cdd:PLN02834 382 MFKSLMAVDKKVADGLLRLILLKGelgncvfTGDFdrealeeTLRAFCK 430
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-349 |
3.85e-157 |
|
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: 444.92 E-value: 3.85e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 1 MKTLEVKTSSATYPVFIGDGIKRNIVDLITSTgHSYTKLLIVTDTAVDAIYGDEMVRLLQQK-WPVNKVVVPSGEQSKSF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLAEL-LKGRRVLVVTDENVAPLYGERLRAALEAAgFEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 80 AEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFH 158
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 159 QPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSELMS-IRSLTDLSKSELAHMLYQGIQVKASIVQEDEKEQG 237
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEEnADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 238 VRAFLNLGHTLGHAIEAEYGYgAITHGDAIAIGMQFALYVSEKELGLSLN-RLELKEWMKELGFPVQVtQEISTKTFVDR 316
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRL-PALDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|...
gi 751617995 317 MIGDKKARGGSVQFVLLKQVGDVTLQSFTKDEL 349
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEEL 350
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-349 |
1.36e-154 |
|
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: 438.03 E-value: 1.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 12 TYPVFIGDGIKRNIVDLITStgHSYTKLLIVTDTAVDAIYGDEMVRLLQQK-WPVNKVVVPSGEQSKSFAEFEHIHTKAI 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLEL--KKGSKVVIVTDENVAKLYGELLLKSLEAAgFKVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 91 QFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSM 169
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 170 LETLSQIERRSGFAEVIKHALISSEDFLSELMSIR-SLTDLSKSELAHMLYQGIQVKASIVQEDEKEQGVRAFLNLGHTL 248
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLdKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 249 GHAIEAEYGYgAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMKELGFPVQVTqEISTKTFVDRMIGDKKARGGS 327
Cdd:cd08195 239 GHAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLErIRALLKKLGLPTSIK-DLDPEELLEAMKRDKKNRGGK 316
|
330 340
....*....|....*....|..
gi 751617995 328 VQFVLLKQVGDVTLQSFTKDEL 349
Cdd:cd08195 317 IRFVLLKGIGKAVIVDDVSEEE 338
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-351 |
3.27e-138 |
|
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: 396.62 E-value: 3.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 13 YPVFIGDGIKRNIVDLITStghsYTKLLIVTDTAVDAIYGDEMVRLLQQ-KWPVNKVVVPSGEQSKSFAEFEHIHTKAIQ 91
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAE----PSKLVIITDETVADLYGDKLLEALQAlGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 92 FQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSML 170
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 171 ETLSQIERRSGFAEVIKHALISSEDFLSELMSIRSLTDLSKSE--LAHMLYQGIQVKASIVQEDEKEQGVRAFLNLGHTL 248
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELehLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 249 GHAIEAEYGYGAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMKELGFPVQVTQEISTKTFVDRMIGDKKARGGS 327
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIErLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330 340
....*....|....*....|....*
gi 751617995 328 VQFVLLKQVGDVTLQS-FTKDELHY 351
Cdd:TIGR01357 317 IRFVLLEEIGKAALAReVPDEMVLE 341
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
68-324 |
3.50e-128 |
|
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: 367.98 E-value: 3.50e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 68 VVVPSGEQSKSFAEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGIN 146
Cdd:pfam01761 2 IVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 147 HPLGKNLIGAFHQPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSEL-MSIRSLTDLSKSELAHMLYQGIQVK 225
Cdd:pfam01761 82 HPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLeENAEALLNLDPDALEEAIARSCEVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 226 ASIVQEDEKEQGVRAFLNLGHTLGHAIEAEYGYGAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMKELGFPVQV 304
Cdd:pfam01761 162 ADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVErIRALLKKYGLPTSL 241
|
250 260
....*....|....*....|
gi 751617995 305 tQEISTKTFVDRMIGDKKAR 324
Cdd:pfam01761 242 -PDLDVEQLLAAMARDKKVR 260
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-346 |
1.31e-100 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 304.00 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 1 MKTLEVKTSSATYPVFIGDGIKRNiVDLITSTGHSyTKLLIVTDTAVDAIYGDEMVRLLQQKWP---VNKVVVPSGEQSK 77
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDH-GELLQRHVHG-KRVLVVTNETVAPLYLEKVVEALTAKGPeltVESVILPDGEKYK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 78 SFAEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGA 156
Cdd:PLN02834 145 DMETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 157 FHQPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSELMS-IRSLTDLSKSELAHMLYQGIQVKASIVQEDEKE 235
Cdd:PLN02834 225 FYQPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEAnMEKLLARDPGALAYAIKRSCENKAEVVSLDEKE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 236 QGVRAFLNLGHTLGHAIEAEYGYGAITHGDAIAIGMQFALYVSEKeLG---LSL-NRleLKEWMKELGFPVQVTQEISTK 311
Cdd:PLN02834 305 SGLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYR-LGwidMSLvNR--IFALLKRAKLPTNPPEKMTVE 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 751617995 312 TFVDRMIGDKKARGGSVQFVLLKQ-------VGDV-------TLQSFTK 346
Cdd:PLN02834 382 MFKSLMAVDKKVADGLLRLILLKGelgncvfTGDFdrealeeTLRAFCK 430
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-339 |
8.77e-96 |
|
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: 289.10 E-value: 8.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 12 TYPVFIGDGIKRNIVDLITSTGHSytKLLIVTDTAVDAIYGDEMVRLL-QQKWPVNKVVVPSGEQSKSFAEFEHIHTKAI 90
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKAD--RHFLVTDSNVNDLYGDRLLEGLkKAGIPVELLVVPAGESNKTLSTLTELAERLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 91 QFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLA-HDSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSM 169
Cdd:cd08197 79 AAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAqSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 170 LETLSQIERRSGFAEVIKHALISSEDFLSELMSI-RSLTDLSKSELAHMLYQGIQVKASIVQEDEKEQGVRAFLNLGHTL 248
Cdd:cd08197 159 LKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYlNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 249 GHAIEAEYGyGAITHGDAIAIGMQFALYVSeKELGLSLNRLELKEW--MKELGFPVQVTQEISTKTFVDRMIGDKK---- 322
Cdd:cd08197 239 GHAIELLSG-GELSHGEAVAIGMCVAAEIS-HLLGLLSEEDVDKHYelLEKIGLPTIIPDGISVEAILEVIRYDNKrgyi 316
|
330
....*....|....*...
gi 751617995 323 -ARGGSVQFVLLKQVGDV 339
Cdd:cd08197 317 kADADTIRMVLLEKLGKP 334
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
13-338 |
1.24e-92 |
|
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: 280.06 E-value: 1.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 13 YPVFIGDGIKRNIVDLITSTGhsYTKLLIVTDTAVDAIYGDEMVRLLQQKWPVNKVVVPSGEQSKSFAEFEHIHTKAIQF 92
Cdd:cd08169 2 YPVFFGEGVFESVNSYIPRDA--FDQCLIIVDSGVPDLIVNYLAEYFGYYLEVHVFIIQGGEAYKTFQTVVEELERAAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 93 QLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSMLE 171
Cdd:cd08169 80 HLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQsDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 172 TLSQIERRSGFAEVIKHALISSEDFLSELMS-IRSLTDLSKSELAHMLYQGIQVKASIVQEDEKEQGVRAFLNLGHTLGH 250
Cdd:cd08169 160 TLPFRQVRAGMAELVKMALIADNDFFEFLEDkANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTFGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 251 AIEAEYGYGaITHGDAIAIGMQFALYVSEKELGLSLNRLELKEW-MKELGFPVQVTQEISTKTFVDRMIGDKKARGGSVQ 329
Cdd:cd08169 240 ALELASGYK-IPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWlLNKLGLPLDHPLALDPDSLYEYLESDKKSLYGNLG 318
|
....*....
gi 751617995 330 FVLLKQVGD 338
Cdd:cd08169 319 MILLSGVGD 327
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
27-349 |
5.16e-58 |
|
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: 191.59 E-value: 5.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 27 DLITSTGHSYTKLLIVTDTAVDAIYGDEMVRLLQ-QKWPVNKVVVPSGEQSKSFAEFEHIHTKAIQFQLDRSSCIIALGG 105
Cdd:cd08199 17 TLADAYGRPGRRRLVVVDENVDRLYGARIRAYFAaHGIEATILVLPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 106 GVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSMLETLSQIERRSGFAE 184
Cdd:cd08199 97 GVLLDVVGFAASLYRRGVPYIRVPTTLLGLvDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 185 VIKHALISSEDFLSEL-----MSIRSLTDLskSELAH-MLYQGIQVKASIVQEDEKEQGVRAFLNLGHTLGHAIEAEYGY 258
Cdd:cd08199 177 IIKMALVKDAELFELLeehgaALVETRFFQ--DEVADeIIRRAIQGMLEELAPNLWEHDLERLVDFGHTFSPILEMAAAP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 259 GaITHGDAIAIGMQFALYVSeKELGLsLNRLELKEW---MKELGFPVqVTQEISTKTFVDRMIGDKKARGGSVQFVLLKQ 335
Cdd:cd08199 255 E-LLHGEAVAIDMALSAVLA-YRRGL-LSEEELDRIlrlMRRLGLPV-WHPLCTPDLLWRALEDIVKHRDGLQRLPLPKG 330
|
330
....*....|....*
gi 751617995 336 VGDVT-LQSFTKDEL 349
Cdd:cd08199 331 IGECVfVNDVTEEEL 345
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
13-339 |
1.11e-50 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 177.36 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 13 YPVFIGDGIKRNIVDLItstGHSYTKLLIVTDTAVDAiYGDEMVRLLQQK-WPVNKVVVPSGEQSKSFAEFEHIHTKAIQ 91
Cdd:PRK14021 189 YDVRIGEGAMNHLPQVL---GPKPVKVALIHTQPVQR-HSDRARTLLRQGgYEVSDIVIPDAEAGKTIEVANGIWQRLGN 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 92 FQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTSML 170
Cdd:PRK14021 265 EGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMvDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 171 ETLSQIERRSGFAEVIKHALISS-------EDFLSELMSIRSLTDLS---KSELAHMLYQGIQVKASIVQEDEKEQGVRA 240
Cdd:PRK14021 345 ATLPNDIFIEGLGEVAKSGFIRDpeilrilEDHAAELRAFDGSTFLGsplEDVVAELIERTVKVKAYHVSSDLKEAGLRE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 241 FLNLGHTLGHAIEaEYGYGAITHGDAIAIGMQFAlyvseKELGLSLNRLEL------KEWMKELGFPVQvTQEISTKTFV 314
Cdd:PRK14021 425 FLNYGHTLGHAIE-KLEHFRWRHGNAVAVGMVYA-----AELAHLLGYIDQdlvdyhRSLLASLGLPTS-WNGGSFDDVL 497
|
330 340
....*....|....*....|....*
gi 751617995 315 DRMIGDKKARGGSVQFVLLKQVGDV 339
Cdd:PRK14021 498 ALMHRDKKARGNELRFVVLDEIGHP 522
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
68-302 |
1.25e-42 |
|
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: 151.95 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 68 VVVPSGEQSK-SFAEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGI 145
Cdd:cd08198 70 LIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQnDSGVGVKNGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 146 NHPLGKNLIGAFHQPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSELmsIRSLTDLSKSELAHMLYqgiQVK 225
Cdd:cd08198 150 NFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWL--ERNAAALRQRDPDAMEK---LIR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 226 AS-------IVQE-DEKEQGVRAFLNLGHTLGHAIEAEYGYgAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMK 296
Cdd:cd08198 225 RCaelhldhIAASgDPFETGSARPLDFGHWSAHKLEQLSGY-ALRHGEAVAIGIALDSLYARLLGLLSREDFDrILALLQ 303
|
....*.
gi 751617995 297 ELGFPV 302
Cdd:cd08198 304 NLGLPL 309
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
68-302 |
1.99e-41 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 149.28 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 68 VVVPSGEQSK-SFAEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATYMRGIDFIQIPTTLLAH-DSAVGGKTGI 145
Cdd:PRK06203 82 LVVPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQnDSGVGVKNGI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 146 NHPLGKNLIGAFHQPKAVIYDTSMLETLSQIERRSGFAEVIKHALISSEDFLSELMSIRS-LTDLSKSELAHMLYQGIQV 224
Cdd:PRK06203 162 NAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAaLAARDPEAMEELIYRCAEL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 225 KASIVQE--DEKEQGVRAFLNLGHTLGHAIEAEYGYgAITHGDAIAIGMQF-ALYVSEKELglslnrLELKEW------M 295
Cdd:PRK06203 242 HLEHIAGggDPFEFGSSRPLDFGHWSAHKLEQLTNY-ALRHGEAVAIGIALdSLYSYLLGL------LSEAEAqrilalL 314
|
....*..
gi 751617995 296 KELGFPV 302
Cdd:PRK06203 315 RALGFPL 321
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
40-339 |
1.80e-39 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 146.20 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 40 LIVTDTAVDAIYGDEMvrllqqkwPVNKVVVPSGEQSKSFAEFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFAAATY 119
Cdd:PRK13951 189 LVFTTERVEKIYGRYL--------PENRLLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTF 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 120 MRGIDFIQIPTTLLAH-DSAVGGKTGINHPLGKNLIGAFHQPKAVIYDTsmLETLSQIERR--SGFAEVIKHALISSEDF 196
Cdd:PRK13951 261 KRGVGLSFYPTTLLAQvDASVGGKNAIDFAGVKNVVGTFRMPDYVIIDP--TVTLSMDEGRfeEGVVEAFKMTILSGRGV 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 197 lSELMSIRSLTDLSKSELAHMLYQGIQVKASIVQEDEKEQGVRAFLNLGHTLGHAIEAEYGygaITHGDAIAIGM-QFAL 275
Cdd:PRK13951 339 -ELFDEPEKIEKRNLRVLSEMVKISVEEKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEG---VPHGIAVAWGIeKETM 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751617995 276 YVSEKELGLSLNRLELKEWMKELgFPVQVtQEISTKTFVDRMIGDKKARGGS-VQFVLLKQVGDV 339
Cdd:PRK13951 415 YLYRKGIVPKETMRWIVEKVKQI-VPIPV-PSVDVEKARNLILNDKKILKGSrVRLPYVKEIGKI 477
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
36-304 |
3.61e-32 |
|
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: 121.70 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 36 YTKLLIVTDTAVDAIYGDEMVRLLQQKWPVNKVVVPSGEQSksfaeFEHIHTKAIQFQLDRSSCIIALGGGVIGDLAGFA 115
Cdd:cd07766 22 FDRALVVSDEGVVKGVGEKVADSLKKGLAVAIFDFVGENPT-----FEEVKNAVERARAAEADAVIAVGGGSTLDTAKAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 116 AATYMRGIDFIQIPTTLLAhDSAVGGKTGINHPLGKNL-IGAFHQPKAVIYDTSMLETLSQIERRSGFAEVIKHALisse 194
Cdd:cd07766 97 AALLNRGIPFIIVPTTAST-DSEVSPKSVITDKGGKNKqVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAV---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 195 dflselmsirsltdlsksELAHMLYQGIQVKASIVQedekeqgvRAFLNLGHTLGHAIEAEYGygaITHGDAIAIGMQFA 274
Cdd:cd07766 172 ------------------ELEKVVEAATLAGMGLFE--------SPGLGLAHAIGHALTAFEG---IPHGEAVAVGLPYV 222
|
250 260 270
....*....|....*....|....*....|.
gi 751617995 275 LYVSEKELGLSLNRLE-LKEWMKELGFPVQV 304
Cdd:cd07766 223 LKVANDMNPEPEAAIEaVFKFLEDLGLPTHL 253
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
15-186 |
6.44e-11 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 62.99 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 15 VFIGDGIKRNIVDLITSTGHSyTKLLIVTDTAVDAIYGDEMVRLLQQKWPVNKVVVPSGeqskSFAEFEHIHTKAIQFql 94
Cdd:PRK00843 14 VVVGHGVLDDIGDVCSDLKLT-GRALIVTGPTTKKIAGDRVEENLEDAGDVEVVIVDEA----TMEEVEKVEEKAKDV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 95 dRSSCIIALGGGVIGDLAGFAAatYMRGIDFIQIPTTlLAHDSAVGGKTGINHpLGKNLIGAFHQPKAVIYDTsmlETLS 174
Cdd:PRK00843 87 -NAGFLIGVGGGKVIDVAKLAA--YRLGIPFISVPTA-ASHDGIASPRASIKG-GGKPVSVKAKPPLAVIADT---EIIA 158
|
170
....*....|....*
gi 751617995 175 QIERR---SGFAEVI 186
Cdd:PRK00843 159 KAPYRllaAGCGDII 173
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-186 |
3.85e-10 |
|
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: 60.23 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 14 PVF--IGDGIKRNIVDLITSTGHSYTKLLIVTDTAVDAIYGDEMVRLLQQKWPVNKVvvpsgeQSKSFAEFEHIHTKAiq 91
Cdd:cd08174 1 PLIlkIEEGALEHLGKYLADRNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTV------EENTDNSAEELAEKA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 92 FQLDRSSCIIALGGGVIGDLAGFAAatYMRGIDFIQIPTTlLAHDS-----AV----GGKTGINHPLgknligafhqPKA 162
Cdd:cd08174 73 FSLPKVDAIVGIGGGKVLDVAKYAA--FLSKLPFISVPTS-LSNDGiaspvAVlkvdGKRKSLGAKM----------PYG 139
|
170 180
....*....|....*....|....
gi 751617995 163 VIYDTSMLETLSQIERRSGFAEVI 186
Cdd:cd08174 140 VIVDLDVIKSAPRRLILAGIGDLI 163
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-186 |
6.18e-08 |
|
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: 53.71 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 15 VFIGDGIKRNIVDLItSTGHSYTKLLIVTDTAVDAIYGDEMVRLLQQKWPVNKVV-VPSGEQSKSFAEFEHIHTKaiqfq 93
Cdd:cd08173 5 VVVGHGAINKIGEVL-KKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVdIATIEEAAEVEKVKKLIKE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 94 lDRSSCIIALGGGVIGDLAGFAAatYMRGIDFIQIPTTlLAHDsavggktGINHPL-------GKNLIGAfHQPKAVIYD 166
Cdd:cd08173 79 -SKADFIIGVGGGKVIDVAKYAA--YKLNLPFISIPTS-ASHD-------GIASPFasikggdKPYSIKA-KAPIAIIAD 146
|
170 180
....*....|....*....|...
gi 751617995 167 TSMletLSQIERR---SGFAEVI 186
Cdd:cd08173 147 TEI---ISKAPKRllaAGCGDLI 166
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
15-302 |
2.47e-07 |
|
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: 51.74 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 15 VFIGDGIKRNIVDLItSTGHSYTKLLIVTDTAVDAIYGDEMVRLLQQK-WPVNKVVVPSGEQSksFAEFEHIHTKAIQFQ 93
Cdd:cd08175 4 IVIGEGALKKLPEYL-KELFGGKKVLVVADENTYAAAGEEVEAALEEAgVTVCLLIFPGEGDL--IADEAAVGKVLLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 94 LDrSSCIIALGGGVIGDLAGFAAatYMRGIDFIQIPTTllahdSAVGGKTGINHPLgknLIGAF------HQPKAVIYDT 167
Cdd:cd08175 81 KD-TDLIIAVGSGTINDLTKYAA--YKLGIPYISVPTA-----PSMDGYTSSGAPI---IVDGVkktfpaHAPKAIFADL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 168 SMLETLSQIERRSGFAEVI-K----------HaLISSEDF-----------LSELMS------------IRSLTD-LSKS 212
Cdd:cd08175 150 DVLANAPQRMIAAGFGDLLgKytaladwklsH-LLGGEYYcpevadlvqeaLEKCLDnaegiaardpeaIEALMEaLILS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 213 ELAhMLYQGIQVKASivqedekeqgvraflnlG--HTLGHAIE---AEYGYGAITHGDAIAIGMQF--ALYVSEKELGLS 285
Cdd:cd08175 229 GLA-MQLVGNSRPAS-----------------GaeHHLSHYWEmefLRLGKPPVLHGEKVGVGTLLiaALYILEQLPPPE 290
|
330
....*....|....*..
gi 751617995 286 lnrlELKEWMKELGFPV 302
Cdd:cd08175 291 ----ELRELLRKAGAPT 303
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
15-302 |
5.21e-07 |
|
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: 50.94 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 15 VFIGDGIKRNIVDLITSTGHsytKLLIVTDTAVDAIYGDEMVRLLQQKWPVNKVVVPSGEqsksfAEFEHIHTKAIQFQL 94
Cdd:COG0371 9 YVQGEGALDELGEYLADLGK---RALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGE-----CSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 95 DRSSCIIALGGGVIGDLAGFAAatYMRGIDFIQIPTTlLAHDSAVGGKTGINHPLGKNLIGAF--HQPKAVIYDTSML-- 170
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI-ASTDAPASPLSVIYTEDGAFDGYSFlaKNPDLVLVDTDIIak 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 171 ---ETLsqierRSGFAEVI------KHALISSEDFLSELMSIrsltdlSKSELAHMLYQ-----GIQVKASIVQEDEKEQ 236
Cdd:COG0371 158 apvRLL-----AAGIGDALakwyeaRDWSLAHRDLAGEYYTE------AAVALARLCAEtlleyGEAAIKAVEAGVVTPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 237 GVR-----------AFL------NLG--HTLGHAIEAEYGYGAITHGDAIAIG--MQFALYvsekelGLSLNRLELKEWM 295
Cdd:COG0371 227 LERvveanlllsglAMGigssrpGSGaaHAIHNGLTALPETHHALHGEKVAFGtlVQLVLE------GRPEEIEELLDFL 300
|
....*..
gi 751617995 296 KELGFPV 302
Cdd:COG0371 301 RSVGLPT 307
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
17-306 |
8.36e-07 |
|
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: 50.26 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 17 IGDGIKRNIVDLITSTghSYTKLLIVTDTAVDAIYGDEMVRLLQQkwpvNKVVVPSGEQSKSFAEFEHIHTKaiqfqldr 96
Cdd:cd08549 6 VGDGAINKIEEILKKL--NLKRVLIITGKNTKAKYCRFFYDQLKT----VCDIVYYDNIDNLEDELKKYTFY-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 97 sSCIIALGGGVIGDLAGFAAatYMRGIDFIQIPTTlLAHDsavggktGINHPLGKNLI-GAFHQ-----PKAVIYDTSML 170
Cdd:cd08549 72 -DCVIGIGGGRSIDTGKYLA--YKLKIPFISVPTS-ASND-------GIASPIVSLRIpGVKKTfmadaPIAIIADTEII 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 171 ETLSQIERRSGFAEVI---------KHALISSEDFLSELMSIRSLTDLsKSELAHMLyqgiqvKASIVQEDEKEQgVRAF 241
Cdd:cd08549 141 KKSPRRLLSAGIGDLVsnitavldwKLAHKEKGEKYSEFAAILSKTSA-KELVSYVL------KASDLEEYHRVL-VKAL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 242 LNLG----------------HTLGHAIEA---EYGYGAITHGDAIAIGMQFALYVSEKELGLSLNRLE-LKEWMKELGFP 301
Cdd:cd08549 213 VGSGiamaiagssrpasgseHLFSHALDKlkeEYLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHErIKMILKKVGAP 292
|
....*
gi 751617995 302 VQVTQ 306
Cdd:cd08549 293 TTAKQ 297
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
15-301 |
3.63e-04 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 42.03 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 15 VFIGDGIKRNIVDLITSTGHSytKLLIVTD-TAVDAIYGDEMVRLLQQKWPvnKVVVPSG-EQSKSFAEFEHIHTKAIQF 92
Cdd:COG1454 11 IVFGAGALAELGEELKRLGAK--RALIVTDpGLAKLGLLDRVLDALEAAGI--EVVVFDDvEPNPTVETVEAGAAAAREF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 93 QLDrssCIIALGGG-VIgDLAGFAAATY--------MRGID--------FIQIPTTLLAH----------DSAVGGKTGI 145
Cdd:COG1454 87 GAD---VVIALGGGsAI-DAAKAIALLAtnpgdledYLGIKkvpgpplpLIAIPTTAGTGsevtpfavitDPETGVKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 146 NHPlgkNLIgafhqPKAVIYDTSMLETLS-QIERRSGFaEVIKHALissedflsE-LMSIRS--LTDLskseLAhmlYQG 221
Cdd:COG1454 163 ADP---ELL-----PDVAILDPELTLTLPpSLTAATGM-DALTHAI--------EaYVSKGAnpLTDA----LA---LEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 222 IQ-VKASIVQ--EDEKEQGVR----------------AFLNLGHTLGHAIEAEYGygaITHGDAIAI----GMQF-ALYV 277
Cdd:COG1454 219 IRlIARNLPRavADGDDLEARekmalasllagmafanAGLGAVHALAHPLGGLFH---VPHGLANAIllphVLRFnAPAA 295
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 751617995 278 SEK------ELGLSLNRL----------ELKEWMKELGFP 301
Cdd:COG1454 296 PERyaeiarALGLDVGLSdeeaaealieAIRELLRDLGIP 335
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-131 |
5.68e-04 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 41.41 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 14 PVFI--GDGIKRNIVDLITSTGhsYTKLLIVTDT-AVDAIYGDEMVRLLqqkwPVNKVVVPSGEQSK-SFAEFEHIHTKA 89
Cdd:cd08196 6 PVKIifGEGILKELPDIIKELG--GKRGLLVTDPsFIKSGLAKRIVESL----KGRIVAVFSDVEPNpTVENVDKCARLA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 751617995 90 IQFQLDrssCIIALGGGVIGDLAGFAAATYM-----------------RGIDFIQIPTT 131
Cdd:cd08196 80 RENGAD---FVIAIGGGSVLDTAKAAACLAKtdgsiedylegkkkipkKGLPLIAIPTT 135
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
240-318 |
9.89e-04 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 40.60 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 240 AFLNLGHTLGHAIEAEYGygaITHGDAIAIGMQFAL-YVSE------KELGLSLN---------------RLELKEWMKE 297
Cdd:cd14863 254 AGTHIGHAIAHALGALYH---IPHGLACALALPVVLeFNAEaypekvKKIAKALGvsfpgesdeelgeavADAIREFMKE 330
|
90 100
....*....|....*....|.
gi 751617995 298 LGFPVQVTQEISTKTFVDRMI 318
Cdd:cd14863 331 LGIPSLFEDYGIDKEDLDKIA 351
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
15-301 |
1.94e-03 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They 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, among 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: 341481 [Multi-domain] Cd Length: 372 Bit Score: 39.74 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 15 VFIGDGIKRNIVDLITSTGhsYTKLLIVTDTAV-DAIYGDEMVRLLQQKwpVNKVVVPSG-EQSKSFAEFEHIHTKAIQF 92
Cdd:cd08551 4 IVFGAGALARLGEELKALG--GKKVLLVTDPGLvKAGLLDKVLESLKAA--GIEVEVFDDvEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 93 QLDrssCIIALGGG-VIgDLAGFAAATYM----------------RGIDFIQIPTT-----------LLAhDSAVGGKTG 144
Cdd:cd08551 80 GAD---LVIAVGGGsVL-DTAKAIAVLATnggsirdyegigkvpkPGLPLIAIPTTagtgsevtpnaVIT-DPETGRKMG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 145 INHPlgkNLIgafhqPKAVIYDTSMLETLSQ--------------IErrsgfaevikhALISSE-DFLSELMSIRSLTDL 209
Cdd:cd08551 155 IVSP---YLL-----PDVAILDPELTLSLPPsvtaatgmdalthaIE-----------AYTSKKaNPISDALALEAIRLI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 210 SKS-ELAH-----------MLYqgiqvkASIVqedekeqGVRAF----LNLGHTLGHAIEAEYGygaITHGDAIAI---- 269
Cdd:cd08551 216 GKNlRRAVadgsdleareaMLL------ASLL-------AGIAFgnagLGAVHALAYPLGGRYH---IPHGVANAIllpy 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 751617995 270 GMQF------------ALYVSEKELGLSLNRL------ELKEWMKELGFP 301
Cdd:cd08551 280 VMEFnlpacpekyaeiAEALGEDVEGLSDEEAaeaaveAVRELLRDLGIP 329
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
34-130 |
2.99e-03 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 39.04 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751617995 34 HSYTKLLIVTDTAV-DAIygdemvrllQQKWP-VNKVVVP----SGEQSksFAEFEHIHTKAIQFQLDrssCIIALGGGV 107
Cdd:cd08172 21 FGIKRPLIIHGEKSwQAA---------KPYLPkLFEIEYPvlryDGECS--YEEIDRLAEEAKEHQAD---VIIGIGGGK 86
|
90 100
....*....|....*....|...
gi 751617995 108 IGDLAGFAAatYMRGIDFIQIPT 130
Cdd:cd08172 87 VLDTAKAVA--DKLNIPLILIPT 107
|
|
| |
