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Conserved domains on  [gi|872710493|ref|WP_048561341|]
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MULTISPECIES: 3-dehydroquinate synthase [Bacillus cereus group]

Protein Classification

3-dehydroquinate synthase family protein( domain architecture ID 10785327)

3-dehydroquinate synthase family protein similar to 3-dehydroquinate synthase that catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate to dehydroquinate in the shikimate pathway

CATH:  1.20.1090.10|3.40.50.1970
EC:  4.2.3.-
Gene Ontology:  GO:0003856|GO:0046872|GO:0003856|GO:0000166
PubMed:  9685163
SCOP:  4002924|3001905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 1-353 1.08e-152

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: 433.75  E-value: 1.08e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   1 MGNIHIQTKSKEYDVHVGKESLSHLTTIIQNMqPSVSNIMIISDEAVATLHLQTVVDALQIEQ-TVFSFVVPSGEKEKSF 79
Cdd:COG0337    1 MQTLTVNLGERSYDIRIGRGLLDELGELLAEL-LKGRRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  80 ENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFH 158
Cdd:COG0337   80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 159 QPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKG 238
Cdd:COG0337  160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 239 VRAHLNFGHTLGHALEKELGYgNITHGDGVAVGMLFALFLSEQVYKVDLS-YEEMKQWFLKYGYPKMPSDLNVERLVQLM 317
Cdd:COG0337  240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRLPALDPEALLAAM 318

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 872710493 318 KQDKKANAGAIHMVLMQEYGVVNVVS-IPDETVHIAL 353
Cdd:COG0337  319 KRDKKVRGGKLRFVLLRGIGKAVIVDdVDEELLRAAL 355
 
Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 1-353 1.08e-152

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: 433.75  E-value: 1.08e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   1 MGNIHIQTKSKEYDVHVGKESLSHLTTIIQNMqPSVSNIMIISDEAVATLHLQTVVDALQIEQ-TVFSFVVPSGEKEKSF 79
Cdd:COG0337    1 MQTLTVNLGERSYDIRIGRGLLDELGELLAEL-LKGRRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  80 ENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFH 158
Cdd:COG0337   80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 159 QPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKG 238
Cdd:COG0337  160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 239 VRAHLNFGHTLGHALEKELGYgNITHGDGVAVGMLFALFLSEQVYKVDLS-YEEMKQWFLKYGYPKMPSDLNVERLVQLM 317
Cdd:COG0337  240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRLPALDPEALLAAM 318

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 872710493 318 KQDKKANAGAIHMVLMQEYGVVNVVS-IPDETVHIAL 353
Cdd:COG0337  319 KRDKKVRGGKLRFVLLRGIGKAVIVDdVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 12-353 1.84e-149

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: 424.93  E-value: 1.84e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  12 EYDVHVGKESLSHLTTIIQNMQPSvsNIMIISDEAVATLHLQTVVDAL-QIEQTVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08195    1 SYPILIGSGLLDKLGELLELKKGS--KVVIVTDENVAKLYGELLLKSLeAAGFKVEVIVIPAGEKSKSLETVERIYDFLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  91 ENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPF 169
Cdd:cd08195   79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 170 LQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08195  159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 250 GHALEKELGYGnITHGDGVAVGMLFALFLSEQVYKVDLS-YEEMKQWFLKYGYPKMPSDLNVERLVQLMKQDKKANAGAI 328
Cdd:cd08195  239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEdLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317

                        330       340
                 ....*....|....*....|....*.
gi 872710493 329 HMVLMQEYGVVNVVS-IPDETVHIAL 353
Cdd:cd08195  318 RFVLLKGIGKAVIVDdVSEEEIREAL 343
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 67-323 4.66e-135

3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.


Pssm-ID: 426414  Cd Length: 260  Bit Score: 385.31  E-value: 4.66e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   67 SFVVPSGEKEKSFENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAI 145
Cdd:pfam01761   1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  146 NHPLGKNMIGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPV 225
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  226 KANIVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFALFLSEQVYKVDLSY-EEMKQWFLKYGYPKM 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADvERIRALLKKYGLPTS 240

                         250
                  ....*....|....*....
gi 872710493  305 PSDLNVERLVQLMKQDKKA 323
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKV 259
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 13-350 1.18e-126

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: 367.34  E-value: 1.18e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   13 YDVHVGKESLSHLTTIIQNMQPsvsnIMIISDEAVATLHLQTVVDALQI-EQTVFSFVVPSGEKEKSFENFYAAHTSALE 91
Cdd:TIGR01357   1 YPVHVGEGLLDQLVEELAEPSK----LVIITDETVADLYGDKLLEALQAlGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   92 NKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPFL 170
Cdd:TIGR01357  77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  171 QSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIH-ILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHLEeLIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  250 GHALEKELGYGNITHGDGVAVGMLFALFLSEqvYKVDLSYEEMK---QWFLKYGYP-KMPSDLNVERLVQLMKQDKKANA 325
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSE--RLGLLPAELIErlvQLLKRYGLPtDLPKDLDVDELLNAMLNDKKNSG 314

                         330       340
                  ....*....|....*....|....*.
gi 872710493  326 GAIHMVLMQEYGVVNV-VSIPDETVH 350
Cdd:TIGR01357 315 GKIRFVLLEEIGKAALaREVPDEMVL 340
PLN02834 PLN02834
3-dehydroquinate synthase
 10-334 2.87e-95

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 290.52  E-value: 2.87e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  10 SKEYDVHVGKESLSHlTTIIQNMQPSvSNIMIISDEAVATLHLQTVVDALQ---IEQTVFSFVVPSGEKEKSFENFYAAH 86
Cdd:PLN02834  76 DRSYPIYIGSGLLDH-GELLQRHVHG-KRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETLMKVF 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  87 TSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVY 165
Cdd:PLN02834 154 DKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGAFYQPQCVLI 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 166 HTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNF 245
Cdd:PLN02834 234 DTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNL 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 246 GHTLGHALEKELGYGNITHGDGVAVGMLFALFLSEQVYKVDLS-----YEEMKQWFLkygyPKMPSD-LNVERLVQLMKQ 319
Cdd:PLN02834 314 GHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSlvnriFALLKRAKL----PTNPPEkMTVEMFKSLMAV 389

                        330
                 ....*....|....*
gi 872710493 320 DKKANAGAIHMVLMQ 334
Cdd:PLN02834 390 DKKVADGLLRLILLK 404
 
Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 1-353 1.08e-152

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: 433.75  E-value: 1.08e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   1 MGNIHIQTKSKEYDVHVGKESLSHLTTIIQNMqPSVSNIMIISDEAVATLHLQTVVDALQIEQ-TVFSFVVPSGEKEKSF 79
Cdd:COG0337    1 MQTLTVNLGERSYDIRIGRGLLDELGELLAEL-LKGRRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  80 ENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFH 158
Cdd:COG0337   80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 159 QPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKG 238
Cdd:COG0337  160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 239 VRAHLNFGHTLGHALEKELGYgNITHGDGVAVGMLFALFLSEQVYKVDLS-YEEMKQWFLKYGYPKMPSDLNVERLVQLM 317
Cdd:COG0337  240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRLPALDPEALLAAM 318

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 872710493 318 KQDKKANAGAIHMVLMQEYGVVNVVS-IPDETVHIAL 353
Cdd:COG0337  319 KRDKKVRGGKLRFVLLRGIGKAVIVDdVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 12-353 1.84e-149

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: 424.93  E-value: 1.84e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  12 EYDVHVGKESLSHLTTIIQNMQPSvsNIMIISDEAVATLHLQTVVDAL-QIEQTVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08195    1 SYPILIGSGLLDKLGELLELKKGS--KVVIVTDENVAKLYGELLLKSLeAAGFKVEVIVIPAGEKSKSLETVERIYDFLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  91 ENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPF 169
Cdd:cd08195   79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 170 LQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08195  159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 250 GHALEKELGYGnITHGDGVAVGMLFALFLSEQVYKVDLS-YEEMKQWFLKYGYPKMPSDLNVERLVQLMKQDKKANAGAI 328
Cdd:cd08195  239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEdLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317

                        330       340
                 ....*....|....*....|....*.
gi 872710493 329 HMVLMQEYGVVNVVS-IPDETVHIAL 353
Cdd:cd08195  318 RFVLLKGIGKAVIVDdVSEEEIREAL 343
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 67-323 4.66e-135

3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.


Pssm-ID: 426414  Cd Length: 260  Bit Score: 385.31  E-value: 4.66e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   67 SFVVPSGEKEKSFENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAI 145
Cdd:pfam01761   1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  146 NHPLGKNMIGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPV 225
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  226 KANIVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFALFLSEQVYKVDLSY-EEMKQWFLKYGYPKM 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADvERIRALLKKYGLPTS 240

                         250
                  ....*....|....*....
gi 872710493  305 PSDLNVERLVQLMKQDKKA 323
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKV 259
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 13-350 1.18e-126

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: 367.34  E-value: 1.18e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   13 YDVHVGKESLSHLTTIIQNMQPsvsnIMIISDEAVATLHLQTVVDALQI-EQTVFSFVVPSGEKEKSFENFYAAHTSALE 91
Cdd:TIGR01357   1 YPVHVGEGLLDQLVEELAEPSK----LVIITDETVADLYGDKLLEALQAlGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   92 NKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPFL 170
Cdd:TIGR01357  77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  171 QSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIH-ILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHLEeLIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  250 GHALEKELGYGNITHGDGVAVGMLFALFLSEqvYKVDLSYEEMK---QWFLKYGYP-KMPSDLNVERLVQLMKQDKKANA 325
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSE--RLGLLPAELIErlvQLLKRYGLPtDLPKDLDVDELLNAMLNDKKNSG 314

                         330       340
                  ....*....|....*....|....*.
gi 872710493  326 GAIHMVLMQEYGVVNV-VSIPDETVH 350
Cdd:TIGR01357 315 GKIRFVLLEEIGKAALaREVPDEMVL 340
PLN02834 PLN02834
3-dehydroquinate synthase
 10-334 2.87e-95

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 290.52  E-value: 2.87e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  10 SKEYDVHVGKESLSHlTTIIQNMQPSvSNIMIISDEAVATLHLQTVVDALQ---IEQTVFSFVVPSGEKEKSFENFYAAH 86
Cdd:PLN02834  76 DRSYPIYIGSGLLDH-GELLQRHVHG-KRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETLMKVF 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  87 TSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVY 165
Cdd:PLN02834 154 DKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGAFYQPQCVLI 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 166 HTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNF 245
Cdd:PLN02834 234 DTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNL 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 246 GHTLGHALEKELGYGNITHGDGVAVGMLFALFLSEQVYKVDLS-----YEEMKQWFLkygyPKMPSD-LNVERLVQLMKQ 319
Cdd:PLN02834 314 GHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSlvnriFALLKRAKL----PTNPPEkMTVEMFKSLMAV 389

                        330
                 ....*....|....*
gi 872710493 320 DKKANAGAIHMVLMQ 334
Cdd:PLN02834 390 DKKVADGLLRLILLK 404
DOIS cd08197
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ...
 12-354 7.71e-85

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: 260.98  E-value: 7.71e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  12 EYDVHVGKESLSHLTTIIQNMqpSVSNIMIISDEAVATLHLQTVVDAL-QIEQTVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08197    1 LTDIYLGRGILESLLSILEEL--KADRHFLVTDSNVNDLYGDRLLEGLkKAGIPVELLVVPAGESNKTLSTLTELAERLI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  91 ENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLA-HDSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPF 169
Cdd:cd08197   79 AAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAqSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 170 LQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08197  159 LKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 250 GHALEKeLGYGNITHGDGVAVGMLFAL-------FLSEQVykVDLSYEEMKqwflKYGYPKM-PSDLNVERLVQLMKQDK 321
Cdd:cd08197  239 GHAIEL-LSGGELSHGEAVAIGMCVAAeishllgLLSEED--VDKHYELLE----KIGLPTIiPDGISVEAILEVIRYDN 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 872710493 322 K-----ANAGAIHMVLMQEYGVVN------VVSIPDETVHIALE 354
Cdd:cd08197  312 KrgyikADADTIRMVLLEKLGKPAnpdgdyLTPVPEEIVKEALE 355
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 41-337 1.52e-78

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: 243.85  E-value: 1.52e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  41 IISDEAVATLHLQTVVDALQIEQTVFSFVVPSGEKEKSFENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFM 120
Cdd:cd08169   28 IIVDSGVPDLIVNYLAEYFGYYLEVHVFIIQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDVVGFAAATYF 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 121 RGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHW 199
Cdd:cd08169  108 RGIAFIRVPTTLLAQsDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIADNDFFEF 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 200 LKEEVQTLA-DLRD--EKLIHiltKAIPVKANIVSQDETEKGVRAHLNFGHTLGHALEKELGYGnITHGDGVAVGMLFAL 276
Cdd:cd08169  188 LEDKANSATvYSPEqlEKLIN---KCISLKLDVVVADEDEQGKRRGLNYGHTFGHALELASGYK-IPHGEAVAVGMAYAA 263

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872710493 277 FLSeqVYKVDLSYEEMKQ--WFL-KYGYP-KMPSDLNVERLVQLMKQDKKANAGAIHMVLMQEYG 337
Cdd:cd08169  264 KIA--NRLGLLPEHDVSRiiWLLnKLGLPlDHPLALDPDSLYEYLESDKKSLYGNLGMILLSGVG 326
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 4-358 1.27e-50

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 176.98  E-value: 1.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   4 IHIQTKSKE-YDVHVGKESLSHLTTIIQNmQPSvsnimiisdeAVATLHLQTV------VDAL--QIEQTVFSFVVPSGE 74
Cdd:PRK14021 179 VHVTGAGIEpYDVRIGEGAMNHLPQVLGP-KPV----------KVALIHTQPVqrhsdrARTLlrQGGYEVSDIVIPDAE 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  75 KEKSFENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNM 153
Cdd:PRK14021 248 AGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMvDASTGGKTGINTPQGKNL 327

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 154 IGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTL-----ADLRDEKL----IHILTKAIP 224
Cdd:PRK14021 328 VGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELrafdgSTFLGSPLedvvAELIERTVK 407

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 225 VKANIVSQDETEKGVRAHLNFGHTLGHALEKeLGYGNITHGDGVAVGMLFALFLSEQVYKVDLSYEEMKQWFL-KYGYPK 303
Cdd:PRK14021 408 VKAYHVSSDLKEAGLREFLNYGHTLGHAIEK-LEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLaSLGLPT 486

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 872710493 304 MPSDLNVERLVQLMKQDKKANAGAIHMVLMQEYG-VVNVVSIPDETVHIALEAFQK 358
Cdd:PRK14021 487 SWNGGSFDDVLALMHRDKKARGNELRFVVLDEIGhPVHLDNPPAEAVEEAFRRIQQ 542
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 41-337 3.12e-47

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: 163.47  E-value: 3.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  41 IISDEAVATLH---LQTVVDALQIEQTVFsfVVPSGEKEKSFENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAA 117
Cdd:cd08199   31 VVVDENVDRLYgarIRAYFAAHGIEATIL--VLPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLLDVVGFAAS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 118 SFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKL 196
Cdd:cd08199  109 LYRRGVPYIRVPTTLLGLvDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALVKDAEL 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 197 YHWLKEEVQTLADLR--DEKLIH-ILTKAIpvkanIVSQDETEKGVRAH-----LNFGHTLGHALEKELGYGnITHGDGV 268
Cdd:cd08199  189 FELLEEHGAALVETRffQDEVADeIIRRAI-----QGMLEELAPNLWEHdlerlVDFGHTFSPILEMAAAPE-LLHGEAV 262

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872710493 269 AVGMLFALFLSEQvyKVDLSYEEMKQWF---LKYGYPKMPSDLNVERLVQLMKQDKKANAGAIHMVLMQEYG 337
Cdd:cd08199  263 AIDMALSAVLAYR--RGLLSEEELDRILrlmRRLGLPVWHPLCTPDLLWRALEDIVKHRDGLQRLPLPKGIG 332
DHQS-like cd08198
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 39-272 7.28e-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: 149.64  E-value: 7.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  39 IMIISDEAVATLHLQTVVD--------ALQIEQTVFSFVVPSGEKEK-SFENFYAAHTSALENKLDRNSLIIALGGGMIG 109
Cdd:cd08198   33 VLFVIDSGVAAAHPALVKQieryfqahPDRLELVAPPLIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 110 DLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKH 188
Cdd:cd08198  113 DAVGFAAAIAHRGIRLIRVPTTVLAQnDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 189 ALIGDVKLYHWLKEEVQTLADlRD----EKLI---------HILTkaipvkanivSQDETEKGVRAHLNFGHTLGHALEK 255
Cdd:cd08198  193 ALIKDASFFEWLERNAAALRQ-RDpdamEKLIrrcaelhldHIAA----------SGDPFETGSARPLDFGHWSAHKLEQ 261

                        250
                 ....*....|....*..
gi 872710493 256 ELGYGnITHGDGVAVGM 272
Cdd:cd08198  262 LSGYA-LRHGEAVAIGI 277
aroB PRK06203
3-dehydroquinate synthase; Reviewed
 69-272 3.57e-41

3-dehydroquinate synthase; Reviewed


Pssm-ID: 235740  Cd Length: 389  Bit Score: 148.51  E-value: 3.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  69 VVPSGEKEK-SFENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAIN 146
Cdd:PRK06203  83 VVPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQnDSGVGVKNGIN 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 147 HPLGKNMIGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYHWLKEEVQTLADlRD----EKLI------ 216
Cdd:PRK06203 163 AFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAA-RDpeamEELIyrcael 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 872710493 217 ---HILTkaipvkanivSQDETEKGVRAHLNFGHTLGHALEkELGYGNITHGDGVAVGM 272
Cdd:PRK06203 242 hleHIAG----------GGDPFEFGSSRPLDFGHWSAHKLE-QLTNYALRHGEAVAIGI 289
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
68-344 3.76e-36

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 136.96  E-value: 3.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  68 FVVPSGEKEKSFENFYAAHTSALENKLDRNSLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAIN 146
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQvDASVGGKNAID 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 147 HPLGKNMIGAFHQPEVVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVKLYhwLKEEVQTLADLRDEKLIHILTKAIPVK 226
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVE--LFDEPEKIEKRNLRVLSEMVKISVEEK 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 227 ANIVSQDETEKGVRAHLNFGHTLGHALEKELGygnITHGDGVAVGMLF-ALFLSEQVYKVDLSYEEMKQwFLKYGYPKMP 305
Cdd:PRK13951 367 ARIVMEDPYDMGLRHALNLGHTLGHVYEMLEG---VPHGIAVAWGIEKeTMYLYRKGIVPKETMRWIVE-KVKQIVPIPV 442

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 872710493 306 SDLNVERLVQLMKQDKKANAGA-IHMVLMQEYGVVNVVSI 344
Cdd:PRK13951 443 PSVDVEKARNLILNDKKILKGSrVRLPYVKEIGKIEFLEV 482
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 13-317 4.69e-27

Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


Pssm-ID: 341447 [Multi-domain]  Cd Length: 271  Bit Score: 107.83  E-value: 4.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  13 YDVHVGKESLSHLTTIIQNMQPSVSnimIISDEAVATLHLQTVVDALQIEQTVFSFVVPSGEKekSFENFYAAHTSALEN 92
Cdd:cd07766    2 TRIVFGEGAIAKLGEIKRRGFDRAL---VVSDEGVVKGVGEKVADSLKKGLAVAIFDFVGENP--TFEEVKNAVERARAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  93 KLDrnsLIIALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAhDSAVGGKVAINHPLGKN-MIGAFHQPEVVVYHTPFLQ 171
Cdd:cd07766   77 EAD---AVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST-DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDITK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 172 SLPEKEWRSGYAEVIKHALIGdvklyhwlkeevqtladlrdEKLIHILTKAIPVKANIVSqdetekgvrahLNFGHTLGH 251
Cdd:cd07766  153 GLPPRQVASGGVDALAHAVEL--------------------EKVVEAATLAGMGLFESPG-----------LGLAHAIGH 201

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872710493 252 ALEKELGygnITHGDGVAVGMLFALFLSEQVY-KVDLSYEEMKQWFLKYGYP-----KMPSDLNVERLVQLM 317
Cdd:cd07766  202 ALTAFEG---IPHGEAVAVGLPYVLKVANDMNpEPEAAIEAVFKFLEDLGLPthladLGVSKEDIPKLAEKA 270
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 17-312 1.69e-08

Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.


Pssm-ID: 341453 [Multi-domain]  Cd Length: 332  Bit Score: 55.22  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  17 VGKESLSHLTTIIQNMQPSVSNIMIISDEAVATLHLQTVVDALQIEQTVFSFVVPSGEkekSFEnfYAAHTSALENKLDr 96
Cdd:cd08174    6 IEEGALEHLGKYLADRNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDN---SAE--ELAEKAFSLPKVD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  97 nsLIIALGGGMIGDLAGFVAasFMRGIRFVQVPTTlLAHDS-----AV----GGKVAinhpLGKNMigafhqPEVVVYHT 167
Cdd:cd08174   80 --AIVGIGGGKVLDVAKYAA--FLSKLPFISVPTS-LSNDGiaspvAVlkvdGKRKS----LGAKM------PYGVIVDL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 168 PFLQSLPEKEWRSGyaevikhalIGDV-----KLYHWL------KEEVQTLA-----------------DLRDEKLIHIL 219
Cdd:cd08174  145 DVIKSAPRRLILAG---------IGDLisnitALYDWKlaeekgGEPVDDFAyllsrtaadsllntpgkDIKDDEFLKEL 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 220 TKAIpVKANI----------VSQDEtekgvrahlnfgHTLGHALEKeLGYGNITHGDGVAVGMLFALFLSEQvykvdlSY 289
Cdd:cd08174  216 AESL-VLSGIameiagssrpASGSE------------HLISHALDK-LFPGPALHGIQVGLGTYFMSFLQGQ------RY 275

                        330       340
                 ....*....|....*....|...
gi 872710493 290 EEMKQWFLKYGYPKMPSDLNVER 312
Cdd:cd08174  276 EEIRDVLKRTGFPLNPSDLGLTK 298
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 14-203 5.25e-08

NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed


Pssm-ID: 179139  Cd Length: 350  Bit Score: 54.13  E-value: 5.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  14 DVHVGKESLSHLTTIIQNMQPSvSNIMIISDEAVATLHLQTVVDALQIEQTVFSFVVpsgeKEKSFENFYAAHTSALENK 93
Cdd:PRK00843  13 DVVVGHGVLDDIGDVCSDLKLT-GRALIVTGPTTKKIAGDRVEENLEDAGDVEVVIV----DEATMEEVEKVEEKAKDVN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  94 LDrnsLIIALGGGMIGDLAGFvaASFMRGIRFVQVPTTlLAHDSAVGGKVAINHpLGKNMIGAFHQPEVVVYHTPFLQSL 173
Cdd:PRK00843  88 AG---FLIGVGGGKVIDVAKL--AAYRLGIPFISVPTA-ASHDGIASPRASIKG-GGKPVSVKAKPPLAVIADTEIIAKA 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 872710493 174 PEKEWRSGYAEVI-KHALIGDVKLYHWLKEE 203
Cdd:PRK00843 161 PYRLLAAGCGDIIsNYTAVKDWRLAHRLRGE 191
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
15-312 2.73e-07

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 51.84  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   15 VHVGKESLSHLTTIIQNMQpsvSNIMIISDEAVATL-HLQTVVDALQ---IEQTVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:pfam00465   4 IVFGAGALAELGEELKRLG---ARALIVTDPGSLKSgLLDKVLASLEeagIEVVVFDGVEP----EPTLEEVDEAAALAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   91 ENKLDrnsLIIALGGGMIGDLAGFVAA---------SFMRG-------IRFVQVPTTlLAHDSAVGGKVAINHPLGKNMI 154
Cdd:pfam00465  77 EAGAD---VIIAVGGGSVIDTAKAIALlltnpgdvwDYLGGkpltkpaLPLIAIPTT-AGTGSEVTPLAVITDTETGEKL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  155 GAFH---QPEVVVYHTPFLQSLPEKEWRSGyaevikhalIGDVkLYHWLKEEVQTLA-DLRD---EKLIHILTKAIPVka 227
Cdd:pfam00465 153 GIFSpklLPDLAILDPELTLTLPPRLTAAT---------GMDA-LAHAVEAYVSKGAnPLTDalaLEAIRLIAENLPR-- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  228 niVSQDETEKGVRAHL------------NFGHTLGHALEKELGYG-NITHGDGVAV----GMLF--------------AL 276
Cdd:pfam00465 221 --AVADGEDLEARENMllastlaglafsNAGLGAAHALAHALGGRyGIPHGLANAIllpyVLRFnapaapeklaqlarAL 298

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 872710493  277 FLSEQVYKVDLSYEEMKQWFLKYGYPKMPSDLNVER 312
Cdd:pfam00465 299 GEDSDEEAAEEAIEALRELLRELGLPTTLSELGVTE 334
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 15-312 5.58e-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: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  15 VHVGKESLSHLTTIIQNMQPSvSNIMIISDEAVATLHLQTVVDALQIEQTVFSFV-VPSGEKEKSFENFYAahtsalENK 93
Cdd:cd08173    5 VVVGHGAINKIGEVLKKLLLG-KRALIITGPNTYKIAGKRVEDLLESSGVEVVIVdIATIEEAAEVEKVKK------LIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  94 LDRNSLIIALGGGMIGDLAGfvAASFMRGIRFVQVPTTlLAHDSAVGGKVAINHPLGKNMIGAfHQPEVVVYHTPFLQSL 173
Cdd:cd08173   78 ESKADFIIGVGGGKVIDVAK--YAAYKLNLPFISIPTS-ASHDGIASPFASIKGGDKPYSIKA-KAPIAIIADTEIISKA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 174 PEKEWRSGYAEVI-KHALIGDVKLYHWLKEE-----VQTLADLRDEkliHILTKAIPVKANIvsQDETEKGVRAHLNFG- 246
Cdd:cd08173  154 PKRLLAAGCGDLIsNITAVKDWRLAHRLKGEyyseyAASLALMSAK---LIIENADLIKPGL--EEGVRTVVKALISSGv 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 247 ---------------HTLGHALEKeLGYGNITHGDGVAVGMLFALFLseqvYKVDlsYEEMKQWFLKYGYPKMPSDLNVE 311
Cdd:cd08173  229 amsiagssrpasgseHLFSHALDK-LAPGPALHGEQCGVGTIMMAYL----HGGD--WKEIREALKKIGAPTTAKELGLD 301


                 .
gi 872710493 312 R 312
Cdd:cd08173  302 K 302
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 14-312 6.28e-06

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: 47.51  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  14 DVHVGKESLSHLTTIIQNMQPSvSNIMIISDE---AVATlhlQTVVDALQIEQTVFSFVVPSGEkeksfENFYAAHtSAL 90
Cdd:cd08175    3 EIVIGEGALKKLPEYLKELFGG-KKVLVVADEntyAAAG---EEVEAALEEAGVTVCLLIFPGE-----GDLIADE-AAV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  91 ENKLDR----NSLIIALGGGMIGDLAGFVaaSFMRGIRFVQVPTTllahdSAVGGKVAINHPLgknMIGAF------HQP 160
Cdd:cd08175   73 GKVLLElekdTDLIIAVGSGTINDLTKYA--AYKLGIPYISVPTA-----PSMDGYTSSGAPI---IVDGVkktfpaHAP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 161 EVVVYHTPFLQSLPEKEWRSGYAEVI-KHALIGDVKLYHWLKEE-----------------VQTLADL--RDEKLIHILT 220
Cdd:cd08175  143 KAIFADLDVLANAPQRMIAAGFGDLLgKYTALADWKLSHLLGGEyycpevadlvqealekcLDNAEGIaaRDPEAIEALM 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 221 KAIpvkanIVSqdetekGVrAHLNFG---------HTLGHALEKE---LGYGNITHGDGVAVGMLF--ALFLSEQVYkvd 286
Cdd:cd08175  223 EAL-----ILS------GL-AMQLVGnsrpasgaeHHLSHYWEMEflrLGKPPVLHGEKVGVGTLLiaALYILEQLP--- 287

                        330       340
                 ....*....|....*....|....*.
gi 872710493 287 lSYEEMKQWFLKYGYPKMPSDLNVER 312
Cdd:cd08175  288 -PPEELRELLRKAGAPTTPEDLGIDR 312
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
1-131 9.58e-06

Alcohol dehydrogenase, class IV [Energy production and conversion];


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 47.04  E-value: 9.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   1 MGNIHIQTKskeydVHVGKESLSHLTTIIQNMqpSVSNIMIISDEAVATL-HLQTVVDALQ---IEQTVFSFVVPsgekE 76
Cdd:COG1454    2 MFTFRLPTR-----IVFGAGALAELGEELKRL--GAKRALIVTDPGLAKLgLLDRVLDALEaagIEVVVFDDVEP----N 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872710493  77 KSFENFYAAHTSALENKLDrnsLIIALGGG--M---------------IGDLAGFVAASfMRGIRFVQVPTT 131
Cdd:COG1454   71 PTVETVEAGAAAAREFGAD---VVIALGGGsaIdaakaiallatnpgdLEDYLGIKKVP-GPPLPLIAIPTT 138
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 15-149 2.22e-05

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: 45.90  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  15 VHVGKESLSHLTTIIQNMQpsVSNIMIISDEAV-ATLHLQTVVDALQ---IEQTVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:cd08551    4 IVFGAGALARLGEELKALG--GKKVLLVTDPGLvKAGLLDKVLESLKaagIEVEVFDDVEP----NPTVETVEAAAELAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  91 ENKLDrnsLIIALGGG--MigDLAGfvAASFM------------------RGIRFVQVPTT-----------LLAhDSAV 139
Cdd:cd08551   78 EEGAD---LVIAVGGGsvL--DTAK--AIAVLatnggsirdyegigkvpkPGLPLIAIPTTagtgsevtpnaVIT-DPET 149

                        170
                 ....*....|
gi 872710493 140 GGKVAINHPL 149
Cdd:cd08551  150 GRKMGIVSPY 159
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 11-131 3.29e-05

Iron-containing alcohol dehydrogenases-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 belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.


Pssm-ID: 341468 [Multi-domain]  Cd Length: 378  Bit Score: 45.54  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  11 KEYDVHVGKESLSHLTTIIQNMqpSVSNIMIISDEAVATLHL-QTVVDALQ---IEQTVFSFVVPsgekEKSFENFYAAH 86
Cdd:cd08189    4 PEPELFEGAGSLLQLPEALKKL--GIKRVLIVTDKGLVKLGLlDPLLDALKkagIEYVVFDGVVP----DPTIDNVEEGL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872710493  87 TSALENKLDRnslIIALGGGMIGDLAGFVAA---------SFMRGI--------RFVQVPTT 131
Cdd:cd08189   78 ALYKENGCDA---IIAIGGGSVIDCAKVIAAraanpkksvRKLKGLlkvrkklpPLIAVPTT 136
Fe-ADH-like cd14862
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 17-176 3.71e-05

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: 341484 [Multi-domain]  Cd Length: 375  Bit Score: 45.29  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  17 VGKESLSHLTTIIQnmqpsvSNIMIISDE-AVATLHLQTVVDALQ---IEQTVFSFVVPsgekEKSFENFYAAHTSALEN 92
Cdd:cd14862   11 FGEDALSHLEQLSG------KRALIVTDKvLVKLGLLKKVLKRLLqagFEVEVFDEVEP----EPPLETVLKGAEAMREF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  93 KLDrnsLIIALGGGMIGDLA------------GFVAASFM------RGIRFVQVPTT----------LLAHDSAVGGKVA 144
Cdd:cd14862   81 EPD---LIIALGGGSVMDAAkaawvlyerpdlDPEDISPLdllglrKKAKLIAIPTTsgtgseatwaIVLTDTEEPRKIA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 872710493 145 INHPlgKNMigafhqPEVVVYHTPFLQSLPEK 176
Cdd:cd14862  158 VANP--ELV------PDVAILDPEFVLGMPPK 181
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 15-131 4.91e-05

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: 44.88  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  15 VHVGKESLSHLTTIIQnmQPSVSNIMIISDE-AVATLHLQTVVDAL-QIEQTVFSFVVPsgekEKSFENFYAAHTSALEN 92
Cdd:cd08196    9 IIFGEGILKELPDIIK--ELGGKRGLLVTDPsFIKSGLAKRIVESLkGRIVAVFSDVEP----NPTVENVDKCARLAREN 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 872710493  93 KLDrnsLIIALGGGMIGDLAGFVAA---------SFM--------RGIRFVQVPTT 131
Cdd:cd08196   83 GAD---FVIAIGGGSVLDTAKAAAClaktdgsieDYLegkkkipkKGLPLIAIPTT 135
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 15-312 1.11e-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: 43.62  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  15 VHVGKESLSHLTTIIQNMQpsvSNIMIISDEAVATLHLQTVVDALQIEQTVFSFVVPSGEKekSFENFYAAHTSALENKL 94
Cdd:COG0371    9 YVQGEGALDELGEYLADLG---KRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGEC--SEEEIERLAEEAKEQGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  95 DrnsLIIALGGGMIGDLAGFVAasFMRGIRFVQVPTTlLAHDSAVGGKVAINHPLGKNMIGAF--HQPEVVVYHTPFLQS 172
Cdd:COG0371   84 D---VIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI-ASTDAPASPLSVIYTEDGAFDGYSFlaKNPDLVLVDTDIIAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 173 LPEKEWRSGyaevikhalIGDV--KLY------------------------------HWLKEEVQTLADLRD----EKLI 216
Cdd:COG0371  158 APVRLLAAG---------IGDAlaKWYeardwslahrdlageyyteaavalarlcaeTLLEYGEAAIKAVEAgvvtPALE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493 217 HILTKAIpVKANIVSQDETEkgvRAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFALFLSEQvykvDLSYEEMKQWF 296
Cdd:COG0371  229 RVVEANL-LLSGLAMGIGSS---RPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGR----PEEIEELLDFL 300

                        330
                 ....*....|....*.
gi 872710493 297 LKYGYPKMPSDLNVER 312
Cdd:COG0371  301 RSVGLPTTLADLGLDD 316
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 15-106 1.13e-04

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.


Pssm-ID: 341473 [Multi-domain]  Cd Length: 378  Bit Score: 43.67  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493  15 VHVGKESLSHLTTIIQNMqpSVSNIMIISDEAVATL-HLQTVVDALQ---IEQTVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:cd08194    4 IIIGGGALEELGEEAASL--GGKRALIVTDKVMVKLgLVDKVTQLLAeagIAYAVFDDVVS----EPTDEMVEEGLALYK 77

                         90
                 ....*....|....*.
gi 872710493  91 ENKLDrnsLIIALGGG 106
Cdd:cd08194   78 EGGCD---FIVALGGG 90
PDD cd08180
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ...
 4-131 5.24e-04

1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.


Pssm-ID: 341459 [Multi-domain]  Cd Length: 333  Bit Score: 41.32  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872710493   4 IHIQTKskeydVHVGKESLSHLTTIIQNmqpsvsNIMIISDEAVATLH-LQTVVDAL--QIEQTVFSFVVPsgekEKSFE 80
Cdd:cd08180    1 FSLKTK-----IYSGEDSLERLKELKGK------RVFIVTDPFMVKSGmVDKVTDELdkSNEVEIFSDVVP----DPSIE 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 872710493  81 NFYAAHTSALENKLDrnsLIIALGGGMIGDLA------GFVAASFMRGIRFVQVPTT 131
Cdd:cd08180   66 VVAKGLAKILEFKPD---TIIALGGGSAIDAAkaiiyfALKQKGNIKKPLFIAIPTT 119
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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